Cell Division 1 Exam

Front 1

Name the four components of the amino acid.

Back 1

1. Amino group
2. Carboxyl group
3. Hydrogen atom
4. Unique R-group (side chain)

Front 2

What type of chirality do amino acid enantiomers exhibit?

Back 2

L-enantiomers, D-enantiomers do not exist naturally.

Front 3

What is the CORN rule?

Back 3

If the amino acid is oriented with the hydrogen atom sticking out towards you - if the groups can be read (clockwise) as CORN (CO group, R-group, and N group) - the the amino acid is L-amino.

Front 4

What are zwitterions?

Back 4

Electrically neutral molecules that contain one positive charge (of the amine group) and one negative charge (of the carboxyl group)

Front 5

How does pH and H+ relate?

Back 5

pH = -log[H+]

Front 6

What is the equation of pKa?

Back 6

pKa = log{([H+][A-])/[HA]}

Front 7

What is the Henderson-Hasselbach equation?

Back 7

pH = pKa + log([A-]/[HA])

Front 8

Buffer solutions can buffer what range of pH's?

Back 8

Above and below 1 pH of the pKa (+/- 1)

Front 9

Define what the pI is?

Back 9

The pH at which a molecule has no net charge.

Front 10

How do you calculate the pI?

Back 10

1. Figure out which pKa yields the neutral molecule.
2. Figure out which pKa yields the negative molecule.
3. Calculate the average of the two.

Front 11

Name all the aliphatic amino acids (6 total).

Back 11

Glycine, alanine, valine, leucine, isoleucine, proline

Front 12

Which amino acid is achiral?

Back 12

Glycine.

Front 13

Which amino acid is typically seen contributing to sharp turns in amino acid structures?

Back 13

Prolline residues (due to the cyclic structure which promotes turn and provides rigidity in structures)

Front 14

Name all the aromatic amino acids (3 total).

Back 14

Phenylalanine, Tyrosine, Tryptophan

Front 15

Which amino acid occurs the least naturally?

Back 15

Tryptophan (1.1%)

Front 16

G, Gly

Back 16

Glycine

Front 17

V, Val

Back 17

Valine

Front 18

A, Ala

Back 18

Alanine

Front 19

L, Leu

Back 19

Leucine

Front 20

I, Ile

Back 20

Isoleucine

Front 21

P, Pro

Back 21

Proline

Front 22

F, Phe

Back 22

Phenylalanine

Front 23

W, Trp

Back 23

Tryptophan

Front 24

Y, Tyr

Back 24

Tyrosine

Front 25

S, Ser

Back 25

Serine

Front 26

T, Thr

Back 26

Threonine

Front 27

N, Asn

Back 27

Asparagine

Front 28

Q, Gln

Back 28

Glutamine

Front 29

C, Cys

Back 29

Cysteine

Front 30

M, Met

Back 30

Methionine

Front 31

D, Asp

Back 31

Aspartate

Front 32

E, Glu

Back 32

Glutamate

Front 33

H, His

Back 33

Histidine

Front 34

K, Lys

Back 34

Lysine

Front 35

R, Arg

Back 35

Arginine

Front 36

Which two amino acids contain hydroxyl groups?

Back 36

Serine, Threonine

Front 37

Name all the polar but uncharged amino acids (4 total)

Back 37

Serine, threonine, asparagine, glutamine

Front 38

Which two amino acids have amide groups?

Back 38

Asparagine, glutamine [analogs of aspartate an glutamate]

Front 39

What are the two sulfur-containing amino acids?

Back 39

Cysteine and methionine

Front 40

Which amino acid participates in forming disulfide bridges?

Back 40

Cysteine

Front 41

Which amino acids have a net negative charge at physiological pH?

Back 41

Aspartate and glutamate

Front 42

Which amino acids have a net positive charge at physiological pH?

Back 42

Histidine, Lysine, Arginine

Front 43

Which amino acids are hydrophilic?

Back 43

Asparagine, Glutamine, Aspartate, Glutamate, Histidine, Lysine, Arginine [N, Q, D, E, H, K, R]

Front 44

Which amino acids are hydrophobic?

Back 44

Valine, Leucine, Isoleucine, Phenylalanine, Methionine
[V, L, I, F, M]

Front 45

Which amino acids absorb UV light?

Back 45

All aromatic amino acids, F, Y, and W
{phenylalanine, tyrosine, tryptophan}

Front 46

Which three amino acids can be phosphorylated (contain -OH groups)?

Back 46

Serine, threonine, Tyrosine [S, T, Y]

Front 47

Which amino acids have TWO chiral centers?

Back 47

Isoleucine and threonine

Front 48

Which two amino acids form O-glycosidic bonds?

Back 48

Serine and threonine

Front 49

Which amino acid can form N-glycosidic bonds?

Back 49

Asparagine

Front 50

What are non-standard amino acids?

Back 50

Amino acids not encoded by the genetic codes and not used for the synthesis of protein.

Front 51

Which non-standard amino acids are critical to the structure of collagen?

Back 51

3 and 4-Hydroxyproline and 5-hydroxylysine.

Front 52

Which non-standard amino acid is critical to the structure of elastin?

Back 52

Desmosine.

Front 53

Explain the symptoms of scurvy?

Back 53

In the lack of Vitamin C - collagen cannot appropriately form (due to dysfunctionality of hydroxyprolines) - thus collagen breaks down (bloody gums and spotting on the skin)

Front 54

What is the crucial coenzyme required for functionality of hydroxprolines?

Back 54

Vitamin C

Front 55

What provides the flexibility of the peptide bonds?

Back 55

Rotations around the C-Ca [psi bond] bond and the C-N [chi bond]

Front 56

What provides the rigidity of the peptide bonds?

Back 56

Planar unit [in order from N-C] between C_alpha, carbonyl, amino group, and C_alpha of next amino acid residue

Front 57

What can limit the flexibility of the peptide bonds?

Back 57

Steric hindrance of R-group (i.e. tryptophan, tyrosine, or histidine)

Front 58

How do you write out an amino acid sequence?

Back 58

From N-terminal to C-terminal

Front 59

What determines the acid/base characterization of a peptide?

Back 59

Ionizing groups located on the R-groups of each amino acid residue.

Front 60

What determines the 3-D structures of proteins?

Back 60

The primary structure (folding begins before the protein completes translation) - the interactions between the side chains determine the 3-D structure.

Front 61

What are the two types of secondary structures?

Back 61

Alpha-helix and Beta-pleated sheets

Front 62

Where do the hydrogen bonds occur in a alpha helix?

Back 62

Between the n and n+4 amino acid residue - between the oxygen of the carbonyl group (n residue) and the hydrogen off the amine (n+4 residue)

Front 63

Is the alpha-helix left or right handed spiral?

Back 63

Right-handed.

Front 64

What is the overall dipole moment of a alpha helix?

Back 64

Negative on the C-terminal side and positive on the N-terminal side.

Front 65

Describe amphipathic alpha helices?

Back 65

R-groups are hydrophobic on one side (exposed to lipids or other hydrophobic residues) and hydrophilic on the other side (exposed to water)

Front 66

What are the three configurations of the Beta-pleated sheet? And how do you determine what configuration it is in?

Back 66

Parallel (chains all travel in the same direction - i.e. N --> C or C-->N)
Antiparallel (alternating chains, one starts with C the other with N)
Mixed (mix of both antiparallel and parallel)

Front 67

What contributes to the partial double bond characteristic of the carbonyl carbon and nitrogen atom?

Back 67

The resonance between the free electrons on the nitrogen and the carbonyl double bond (this also allows for rigidity of planar peptide bond)

Front 68

All proteins have a _____ structure, but not necessarily a _____ structure. An example of such a protein is ______.

Back 68

Tertiary; quarternary; myoglobin.

Front 69

What is the purpose of super-secondary structures?

Back 69

Many times, the supersecondary structures (a.k.a motifs) provide important binding function (i.e. active sites of enzymes).

Front 70

What supersecondary structures typically form the stable core of many proteins?

Back 70

Beta-barrels and and saddles.

Front 71

What type of loops occur in proteins (for supersecondary structures)? Right-handed or left-handed?

Back 71

Right-handed.

Front 72

What kind of COVALENT bonds are present in TERTIARY structures?

Back 72

Disulfide bonds between cysteine residues.

Front 73

Define the domain of a protein?

Back 73

Unit of the tertiary structure that has a functional purpose (i.e. G3P binding domain of G3P dehydrogenase)

Front 74

How are quarternary structures held together?

Back 74

Non-covalent interactions only!

Front 75

What are chaperones?

Back 75

"Heat shock" proteins that assist in the proper folding of proteins.

Front 76

Once denatured, how are proteins renatured?

Back 76

As long as the primary amino acid sequence is still intact, renaturation can occur as long as the denaturing agent is gone.

Front 77

How is amyloid plaque formed?

Back 77

Proteolytic cleavage of amyloid (protein found on cell surfaces in the brain) into 40-42 amino acid residues that form a Beta-pleated sheet.

Front 78

What type of amyloid plaque is formed in Alzheimers?

Back 78

A-Beta (amyloid beta)

Front 79

How does the "tau" protein play a role in alzheimer's?

Back 79

Normal tau protein helps form microtubular structures; abnormal tau protein thus promote accumulation of neurfibrillary tangles in the brain.

Front 80

How does prion disease progress?

Back 80

Infective agent sets up a template to convert normal PrP to infective PrP.

Front 81

What exactly is the change to create infectious PrP?

Back 81

alpha-helices converted to Beta-sheets (resists proteolytic degradation by the body)

Front 82

What are the two classification of proteins based on their folding patterns?

Back 82

Globular and fibrous proteins.

Front 83

Describe the structure of alpha-keratin?

Back 83

R-handed alpha helices that combine into protofilaments and protofibrils cross-linked by disulfide bonds.

Front 84

How does permanent waving at a salon linked to keratin?

Back 84

Hair is made up of keratin - thus when applying heat to the hair the disulfide bonds are broken and then reformed in a different form (keeping hair curled).

Front 85

All fibrous proteins are _______ in water.

Back 85

insoluble.

Front 86

Describe the structure of collagen?

Back 86

Rich in glycine/proline and provide structural components to bone/teeth/cartilage/tendons/skin/blood vessels

Front 87

What is the repetitive amino acid sequence in collagen?

Back 87

Gly-X-Y.

X = proline
Y = hydroxyproline

Front 88

Lack of vitamin C leads to....

Back 88

Scurvy

Front 89

Explain the clinical symptoms of scurvy?

Back 89

Lack of vitamin C inhibits formation of hydroxyprolines which are critical to structure of collagen (thus blood vessels become fragile, wounds do not heal well, and skin easily hemorrhages).

Front 90

What are the steps in collagen synthesis?

Back 90

1. cleavage of signal peptides.
2. hydroxylation of prolines and lysine residues.
3. glycosylation of some hydroxylysine and asparagine residues.
4. association of three C propeptides
5. disulfide bridges form

Front 91

What is tropocollagen?

Back 91

Three left-handed alpha-chains twisted around each other in a right-handed manner (forms a larger helix)

Front 92

Why is glycine critical to collagen structure?

Back 92

Glycine is the smallest amino acid residue, thus allows for tight turning of collagen.

Front 93

What causes the reduced muscular flexibility and agility in the elderly?

Back 93

Additional covalent-crosslinks in tropocollagen

Front 94

What is lathyrism?

Back 94

Deformed bones, joint dislocations, aortic aneurysms (plant toxin inhibits lysyl oxidase which forms defective tropocollagen).

Front 95

Why can lathyrism be confused with cupper-deficiency?

Back 95

Cupper is required for lysyl oxidase - thus the abnormality of this enzyme will induce similar clinical symptoms.

Front 96

Which type of collagen mutation is lethal?

Back 96

Point mutation in Type II procollagen - leads to osteogenesis imperfecta

Front 97

What is Ehler-danlos syndrome?

Back 97

Errors in processing Type I, III, IV procollagen - hypermobility and skin hyperextensibility.

Front 98

What role does desmosine play in elastin?

Back 98

Links different elastin fibers (helps control the stretched/relaxed positions of elastin

Front 99

What is the key structural difference (in terms of amino acid composition) between elastin and collagen?

Back 99

Elastin LACKS hydroxyprolines (but has glycine/proline residues)

Front 100

What role does alpha-antitrypsin play in emphysema?

Back 100

This glycoprotein inhibits elastase (which breaks down elastin) - in deficiencies of this glycoprotein, elastase levels are high and break down the elasticity of lung tissue causing emphysema.

Front 101

SDS-PAGE separates proteins according to _____.

Back 101

Size.

Front 102

Gel electrophoresis separates protein according to _____.

Back 102

Charge.

Front 103

Isoelectric focusing separates proteins according to ______.

Back 103

pI value (the gel is in a pH scale)

Front 104

Two-dimensional gel electrophoresis separates proteins according to _____ first then by ______.

Back 104

Isoelectric focusing, SDS page
(pI, then size)

Front 105

What is the first step of tissue preparation?

Back 105

Fixation (the processes and structures of that cell must be preserved to give an accurate description).

Front 106

Once fixated, what is the next step in tissue preparation?

Back 106

Dehydration - removal of water from the sample and subsequent replacement with xylene.

Front 107

What is the critical last step of tissue preparation?

Back 107

Staining - allows for different areas of the cell to become prominent (most common staining, H&E)

Front 108

What regions does hematoxylin stain?

Back 108

Basic blue stain, labels acidic regions (i.e. DNA/RNA)

Front 109

What regions does eosin stain?

Back 109

Acidic pink stain, labels basic regions of the cell (i.e. cytoplasm or extracellular matrix)

Front 110

What does the periodic acid-Schiff (PAS) reaction stain emphasize?

Back 110

Carboyhydrates (glycogen/mucus/basement membrane)

Front 111

Which of the following structures are associated with nuclear lamins [microfilaments, intermediate filaments, plasma membrane, rough ER]

Back 111

Intermediate filaments

Front 112

Which of the following is not found in lysosomes (nucleases, lipases, catalses, OR acid phosphatase)

Back 112

Catalase

Front 113

The electron microscopic appearance of plasma membrane is best described as?

Back 113

Trilaminar structure.

Front 114

What is the most abundant organelle in the cell (aside from the cytosol)?

Back 114

Mitochondria

Front 115

How do molecules/substances shift from the nucleus to the cytosol?

Back 115

Via nuclear pores.

Front 116

What is euchromatin?

Back 116

Loosely packed DNA that is transcriptionally active.

Front 117

What is heterochromatin?

Back 117

Tightly packed DNA that is transcriptionally inactive.

Front 118

What is unique about the cellular division of platelet-producing megakarocytes of the bone marrow?

Back 118

Genetic material is replicated but without cell division.

Front 119

Mitochondrial DNA differs from nuclear DNA in that it is _______ and replicates via _________.

Back 119

Circular, fission/fusion.

Front 120

The smooth endoplasmic reticulum is responsible for synthesis of _______ and ____ of compounds.

Back 120

steroid synthesis and detoxification of compounds (liver)

Front 121

The entry side of golgi apparatus is known as ____- side and the exit side is called the _____-side.

Back 121

cis/trans

Front 122

What is the main function of the golgi apparatus?

Back 122

Post-translational modification and packaging of macromolecules/proteins.

Front 123

The environment within a lysozome is (acidic/basic) and therefore the enzymes within are known as ___________.

Back 123

acidic; acid hydrolases

Front 124

What is the cellular explanation of Tay-sachs Disease?

Back 124

Lysosomal storage disease - hexosaminidase is deficient and therefore there is an accumulation of gangliosides in the CNS.

Front 125

Endosomes are divided into _____ and ______ endosomes based on their location.

Back 125

early (by plasma membrane), late (by cell center)

Front 126

What is the cellular explanation of familial hypercholesterolemia?

Back 126

LDL-receptor is mutated and cannot accept LDL (receptor-mediated endocytosis) thus leading to high levels of LDL in the blood.

Front 127

Catalase and oxidative enzymes are found in what cellular organelle?

Back 127

Peroxisomes.

Front 128

What allows the detoxification of hydrogen peroxide in the cell?

Back 128

Catalase.

Front 129

What is the cellular explanation of Zellwegger disease?

Back 129

Peroxisomal enzymes cannot cross the preoxisomal membrane - thus leading to childhood death.

Front 130

The energy stores of the cell are found in the _____ and are typically stored as ____ droplets and _____ deposits.

Back 130

cytosol; lipid; glycogen

Front 131

The cytoskeleton is divided into three types of fibers which are....

Back 131

Actin filaments, intermediate filaments, and microtubules

Front 132

Actin filaments provide what type of cellular movements?

Back 132

Crawling, contraction/pinching of the two daughter cells during mitosis, also compose part of microvilli in intestine

Front 133

Where is the highest concentration of actin located?

Back 133

Beneath the plasma membrane in a region of cells known as the CORTEX.

Front 134

What is the main function of intermediate filaments?

Back 134

Great tensile/mechanical stress that distributes mechanical stress across the cell

Front 135

Intermediate filaments are classified into four different categories, which are....

Back 135

1. Keratin
2. Vimentin
3. Neurofilaments
4. Nuclear lamins

Front 136

Where do microtubules originate from?

Back 136

Centrosomes, the gamma-tubulin ring

Front 137

Describe the structure of microtubules?

Back 137

Heterodimers made up of alpha and beta tubulin.

Front 138

Motor protiens move cargo based on the polarized structure of mirotubules that contain a ____ end and a _____ end.

Back 138

minus; plus.

Front 139

Kinesins move in the _____ direction and dyneins move in the _____ direction.

Back 139

plus; minus

Front 140

Cilia and flagella have a unique microtubuel structure which is....

Back 140

9+2 arrangement of microtubules.

Front 141

What allows the lipid bilayer to aggregate spontaneously?

Back 141

Hydrophobic tails congregate together (to avoid water) while the hydrophilic heads face out towards either the extracellular area or internally to the cell.

Front 142

Which of the following four major phospholipids contain a negative charge? (Phosphatidylcholine, phophatidylethanolamine, phosphatidylserine, sphingomeylin)

Back 142

Phosphatidylserine (PS)

Front 143

Which phospholipid is used for cellular signaling?

Back 143

Phosphatidylinositol (PI)

Front 144

What restricts the mobility/fluidity of the cell membrane?

Back 144

Cholesterol

Front 145

Which of the following phospholipids are found on the cytosolic leaflet of the membrane - and what does this indicate? [PI, PS, PC, PE, SM]

Back 145

PS and PI are on the cytosolic leaflet (thus the inside is negatively charged)

Front 146

What are the function of lipid rafts?

Back 146

Clusters of sphingolipids and cholesterol - thickening of the plasma membrane that typically contain proteins for cell signaling.

Front 147

What type of molecules can transmit through lipid bilayers?

Back 147

Small, non-polar, lipid soluble, hydrophobic molecules.

Front 148

What are the two types of membrane proteins?

Back 148

Integral and peripheral proteins.

Front 149

How are peripheral proteins attached?

Back 149

Via non-covalent binding to integral membrane proteins.

Front 150

Transmembrane proteins contain both ______ and ______ regions.

Back 150

hydrophobic; hydrophilic

Front 151

Which type of secondary protein structure is typically found in membrane proteins?

Back 151

alpha-helices

Front 152

Due to the rigidity of Beta-barrels - these structures are typically confined to ________.

Back 152

Mitochondrial membranes.

Front 153

Glycoproteins are contained only on the _____ surface of the cell.

Back 153

extracellular

Front 154

What is the least likely movement of the lipid bilayer?

Back 154

Flip-flop (where the cytosolic layer becomes the extracellular layer)

Front 155

If a co-factor is covalently linked to an enzyme it is a ______.

Back 155

Prosthetic group.

Front 156

If a co-factor is loosely bound to the enzyme it is a _____.

Back 156

Co-substrate.

Front 157

What is a co-factor?

Back 157

Non-protein containing component of the enzyme.

Front 158

What is an apoenzyme?

Back 158

Protein-containing component of the enzyme.

Front 159

What is the function of oxidoreductases?

Back 159

NAD+, FAD+, dehydrogenases, or oxidases -- redox reactions!

Front 160

What is the function of transferases?

Back 160

Transfer functional groups (hexokinase/glucokinase transfer phosphate group)

Front 161

What is the function of hydrolases?

Back 161

Enzyme that breaks bonds via hydrolysis (H20) [e.g. peptidases]

Front 162

What is the function of lyases?

Back 162

Forming or breaking double bonds (decarboxylases) -- splits one compound into two.

Front 163

What is the function of isomerase?

Back 163

Isomerization of molecules (mutase or isomerase)

Front 164

What is the function of ligase?

Back 164

Joins substituents at the EXPENSE OF ATP (carboxylase)

Front 165

How do enzymes function?

Back 165

They lower the activation energy.

Front 166

Does the free energy of the reactants or products change in a catalyzed reaction?

Back 166

No.

Front 167

What is an endergonic reaction?

Back 167

The free energy of the products are higher than the free energy of the reactants [non-spontaneous, del G >0]

Front 168

What is an exergonic reaction?

Back 168

The free energy of the products is lower than the free energy of the reactants [spontaneous, del G <0]

Front 169

What is a catalytic group?

Back 169

Specific amino acid residues (typically far apart) that come together in the active site to directly interact with the substrate.

Front 170

Identify the catalytic triad for chymotrypsin.

Back 170

Histidine (57), Aspartate (102), Serine (195)

Front 171

What is the purpose of transition state analogs?

Back 171

Inhibit the forward reaction of an enzyme and also help understand enzyme-catalyzed reactions (research)

Front 172

What is the vitamin derivative of thiamine?

Back 172

B1

Front 173

Vitamin B2 is associated with ...

Back 173

Riboflavin

Front 174

Vitamin B3 is associated with ...

Back 174

Niacin

Front 175

What is the vitamin derivative of pantothenic acid?

Back 175

B5

Front 176

Vitamin B6 is associated with ...

Back 176

Pyridoxine

Front 177

What is the vitamin derivative of cobalamin?

Back 177

B12

Front 178

Tetrahydrofolate is a cosubstrate that derives from....

Back 178

Folic acid.

Front 179

What is the function of biotin in teh body?

Back 179

Prosthetic group that helps transfer CO2 [ATP-dependent]

Front 180

What is the function of Thiamin pyrophosphate (TPP)?

Back 180

Derived from B1, transfers aldehyde - acts as a prosthetic group to enzymes like pyruvate dehydrogenase

Front 181

What is the two main differences between FAD and NAD?

Back 181

FAD can be reduced to FADH2 while NAD can be reduced to NADH only.

FAD is a prosthetic group, while NAD is a cosubstrate.

Front 182

Aside from FAD, what other coenzyme is produced from B2 (riboflavin)?

Back 182

FMN

Front 183

What is the main difference between NADH and NADPH?

Back 183

NAD is utilized in catabolic processes, while NADP is utilized in anabolic processes.

Front 184

How is NAD regenerated once reduced?

Back 184

Via FAD.

Front 185

What is the function of tetrahydrofolate (THF)?

Back 185

Transfers one-carbon groups.

Front 186

What is the purpose of cobalamin?

Back 186

Transfers methyl groups.

Front 187

Define what V-max is?

Back 187

Maximum rate of the enzymatic reaction.

Front 188

Define what K-m is?

Back 188

The substrate concentration that yields 1/2(V-max)

Front 189

What are the axes for the Michaelis-Mentel model graph?

Back 189

x-axis is [S] ... mol/L
y-axis is v (reaction rate) ... mol/sec

Front 190

What is the enzyme turnover number?

Back 190

V-max

Front 191

How can you calculate V-max without a graph?

Back 191

V-max = k3 * [E_total]

Front 192

How do you calculate the fraction of the enzyme occupied by the substrate?

Back 192

Rearrange M-M equation:
v/Vmax = [S]/(K-m + [S])

Front 193

What is unique about the pancreatic enzymes and their activation?

Back 193

In a proenzyme (zymogen) form until activated by trypsin which was originally activated by enteropeptidase (released by intestines)

Front 194

What is the main difference between competitive and non-competitive inhibitions?

Back 194

Competitive inhibitions interacts with the active site while non-competitive inhibitions interacts with a non-active site to induce changes at the active site.

Front 195

What changes occur in the Michaelis-Menten model with a competitive inhibitor?

Back 195

Increase in K-m, V-max stays the same.

Front 196

What changes occur in the Michaelis-Menten model with a non-competitive inhibitor?

Back 196

Decrease in V-max, K-m stays the same.

Front 197

How can you determine by what amount an inhibitor is changing a variable in the Michaelis-Menten equation?

Back 197

1+([I]/K-i)
[I] = concentration of inhibitor
K-i is like the K-m, but specific to the inhibitor

Front 198

How do insecticides function?

Back 198

Irreversible inhibitors of acetylcholinesterase (parathion is metabolized to paraoxon that cannot be metabolized by insects) - and thus functions as an inhibitor.

Front 199

How do monoamine oxidases inhibitors function?

Back 199

Irreversible inhibitors of monoamine oxidases preventing degradation of norepinephrine and DOPA [since irreversible, takes 1-2 weeks for new enzymes to regenerate]

Front 200

How is disulfiram used in treatment of alcoholism?

Back 200

Disulfiram is an irreversible inhibitor of ALDH (the 2nd step in alcohol metabolism) - thus worsening the symptoms/effects of ethanol on the body [preventing excess use of EtOH]

Front 201

How is methanol or ethylene glycol poisoning remedied?

Back 201

K-m for ethanol is lower than that for methanol/ethylene glycol - so ethanol is given as a competitive inhibitor.

Front 202

How do statin drugs serve to lower cholesterol?

Back 202

Competitive inhibitor of HMG-CoA Reductase which prevents the formation of cholesterol.

Front 203

How does lead poisoning occur?

Back 203

As lead enters the circulation - creates covalent bonds non-competitively - preventing function of whatever enzyme it has chosen to bind to.

Front 204

How does ACE inhibitors work?

Back 204

Prevent the conversion of angiotensin I to II - which is a potent vasoconstrictor (so keeps the blood vessels open).

Front 205

How does the reaction rate curve change for allosteric enzymes?

Back 205

Sigmoidal because subunits work with each other to bind substrate.

Front 206

How does allosteric regulation work?

Back 206

Inhibitor or activator will bind to one subunit which will also induce a change in the other subunit towards a certain equilibrium.

Front 207

Allosteric inhibitors preferentially bind to ____ state while activators preferentially bind to ____ state.

Back 207

Tense (T), Relaxed (R)

Front 208

If an allosteric enzyme is activated, the curve will shift to the _____ while inhibition will cause the curve to shift to the ______.

Back 208

Left (lower concentration needed for higher rate); Right (vice versa).

Front 209

How many different forms of creatine kinase are there?

Back 209

CK-M, CK-B, CK-MB

Front 210

In case of a heart attack, what levels would you expect to change and how.

Back 210

CK-MB elevates (increased permeability of the heart tissue due to necrosis), and LDH1 will increase (predominantely found in the heart)

Front 211

In a normal person, LDH (lactate dehydrogenase) exists in _____ forms, where the most dominant is _____.

Back 211

Five; LDH2.

Front 212

What is an isoenzyme?

Back 212

Different structure, same function.

Front 213

What is the difference between glucokinase and hexokinase?

Back 213

Glucokinase has a higher K-m than hexokinase since it is found in the liver - and the heart/muscle requires more glucose for conversion to ATP.

Also - hexokinase is inhibited by the product (glucose 6-phosphate) while glucokinase is not.

Front 214

Coat Protein I and II are responsible for shuttling molecules between what to organelles?

Back 214

Golgi body and rough endoplasmic reticulum.

Front 215

Clathrin-coated vesicles facilitate the movement between what two organelles?

Back 215

Golgi body and cell membrane.

Front 216

If the protein coats (vesicle formation) on molecules are temporary - why are they necessary?

Back 216

For the appropriate signaling and shuttling to the right destination.

Front 217

Through what mechanism do vesicles know where to go?

Back 217

SNAREs - v-SNARES (on the vesicles ) that connect with the t-SNARES (on the target membranes)

Front 218

What is the function of Rab proteins and dynamin?

Back 218

Help with the fusion/formation of the vesicle to the membrane (GTP-binding proteins)

Front 219

What are the two non-receptor mediated forms of endocytosis?

Back 219

Pinocytosis and phagocytosis.

Front 220

What is the main difference between pinocytosis and receptor-mediated endocytosis?

Back 220

Pinocytosis is "cellular drinking" ingesting ions/waters while receptor-mediated endocytosis is "cellular eating" ingesting solutions of molecules (still liquid)

Front 221

What is phagocytosis?

Back 221

Ingestion of particulate matter (actual solids) - such as deadened remains of a cell.

Front 222

What is the first step in LDL uptake by a cell?

Back 222

Clathrin-pit and vesicle formation on plasma membrane.

Front 223

What is the critical step in LDL uptake that allows for the dissociation of the receptor and ligand?

Back 223

Reduction of pH from 7 to 5.

Front 224

What is the final step of LDL uptake? (discounting for recycling of receptor to plasma membrane)

Back 224

Degradation by lysozome.

Front 225

What allows the pH to be so low in the lysosomes?

Back 225

Action of vacuolar H+ ATP-ase

Front 226

What are the three mechanisms by which material is delivered to lysosomes?

Back 226

Intracellular receptors signaling autophagy (in aging cells/malformed cells, etc.) or endocytosis (pinocytosis, receptor-mediated endocytosis, phagocytosis)

Front 227

What is the pathology behind I-cell disease?

Back 227

Lysosomal storage disease has dysfunction with mannose 6-phosphate (indicates which enzymes to send to lysosome) - thus lysosomes cannot function.

Front 228

What is the difference between constitutive and regulated exocytosis?

Back 228

Constitutive is constantly occurring (for lipids/proteins to the membrane that are constantly degraded/shifted), but regulated is signal-triggered.

Front 229

Where do proteins go first once formulated in the rough endoplasmic reticulum?

Back 229

Cis-golgi apparatus.

Front 230

How do proteins enter the mitochondria?

Back 230

First unfolded in the cytosol, shuttled across the membrane, and then re-folded.

Front 231

Myoglobin is primarily used for ______.

Back 231

Oxygen storage.

Front 232

Hemoglobin is primarily used for ______.

Back 232

Oxygen transport.

Front 233

Does myglobin contain a quarternary structure?

Back 233

No, it is a single polypeptide unit that binds a single O2.

Front 234

What is the quarternary structure of hemoglobin?

Back 234

Two alpha and beta dimers that form alpha-beta complexes (so two heterodimers)

Front 235

Where is heme synthesized?

Back 235

Succinyl CoA of the citric acid cycle (and requires biotin during synthesis)

Front 236

What does oxygen specifically bind to in hemoglobin?

Back 236

Iron within the porphyrin ring (T-state shifts to the R-state)

Front 237

How does cooperative binding occur?

Back 237

As oxygen binds to each subunit - the T state (deoxy) shifts to R state (oxy) which promotes the equilibrium shift towards oxygenated state.

Front 238

How is the different dissociation curve shapes explained between hemoglobin and myoglobin?

Back 238

Hemoglobin (sigmoidal) due to cooperative binding, and myoglobin (hyperbolic) only one unit that has very high affinity for oxygen.

Front 239

How does 2,3-BPG function in RBC regulation?

Back 239

Allosterically inhibits RBC by binding/stabilizing the T-state of the hemoglobin - leads to increased unloading oxygen in tissues.

Front 240

What effect does low pH have on RBC?

Back 240

T-state favors protonation - so decreased pH promotes T-state and increased unloading of oxygen in tissues.

Front 241

Where is 2,3-BPG synthesized?

Back 241

From the glycolytic pathway (intermediate after G3P has formed and reacts)

Front 242

What effect does carbon dioxide have on hemoglobin?

Back 242

Inhibits hemoglobin via carbamoylation - also accounts for 20% of removal of CO2 from the body.

Front 243

What is the main difference between HbF and HbA?

Back 243

HbF has a much higher affinity for oxygen (small percentage remains as an adult) - and because of this the fetus can get oxygen from maternal blood.

Front 244

How many variations of alpha-thalassemia are there?

Back 244

Four - since there are four total alpha genes (two per gene)

Front 245

Due to defect in the alpha or beta genes in thalassemia - what kind of quarternary structures will develop?

Back 245

Beta tetramers or alpha tetramers (or homodimers form) - body attempts to compensate for defects in subunits.

Front 246

What clinical symptoms will occur in thalassemia?

Back 246

Anemia (in more severe forms there is heart failure due to unoxygenated heart)

Front 247

What is the coagulated form of hemoglobin in the blood called?

Back 247

Heinz body.

Front 248

What is the point mutation in sickle cell anemia?

Back 248

Glutamate changes to valine at beta-6.

Front 249

What can be an indicator of hyperglycemia in diabetic patients?

Back 249

Hba1c (amount of glycosylated hemoglobin)

Front 250

What causes the sickle shape in sickle-cell anemia?

Back 250

Promotion of clumping in the deoxy state of hemoglobin (polymerization)

Front 251

What is pharmacodynamics?

Back 251

Effect of the drug on the body.

Front 252

What is pharmacokinetics?

Back 252

Effect of the body on the drug.

Front 253

What is the first-pass effect?

Back 253

The drug is metabolized by the liver into non-functioning metabolites to be excreted before it is absorbed by the GI tract.

Front 254

Your body will digest drugs to make them more ________ and thus promote ______.

Back 254

hydrophilic; excretion.

Front 255

What is the most important mechanism for absorption of a drug into the body?

Back 255

Diffusion via cell membranes (ergo, lipophilic substances)

Front 256

Unionized forms of a drug are (more/less) likely to pass through membranes.

Back 256

More.

Front 257

What is the Henderson-Hasselbalch equation?

Back 257

pH = pKa + log ([deprotonated]/[protonated])

Front 258

If phenobarbitol (weak acid) has a pKa of 7.4, and the stomach has a pH of 2.4 - is the drug readily absorbed or excreted?

Back 258

Readily absorbed because the protonated form is in a much larger amount than deprotonated.

Front 259

Acids prefer to be _____ while bases prefer to be ______.

Back 259

protonated; deprotonated....always prefer to be neutral.

Front 260

How can you avoid the first pass effect?

Back 260

IV injection, anal suppositories, sublingual adminstration.

Front 261

Molecules that cannot cross the blood brain barrier have what characteristics?

Back 261

Too charged, too large, and not lipid soluble.

Front 262

What are P-glycoproteins?

Back 262

Efflux transporters that remove hydrophobic substances from the cell? - it is a protective mechanism against toxicity.

Front 263

How do you treat a morphine overdose?

Back 263

Since morphine is a weak base, it is not readily absorbed by the stomach - therefore, gastric lavage techniques are used.

Front 264

Why is it bad to chew medications that are not meant to be chewed?

Back 264

Can result in toxic "dumping" of medication into the GI - because it does not follow regular digestion processes.

Front 265

What do agonists do?

Back 265

Drug that activates a receptor

Front 266

What do antagonists do?

Back 266

Prevents an agonist from activating receptor.

Front 267

How do inert binding sites affect the bioavailability of a drug?

Back 267

Drugs can bind to endogenous substances without inducing a response - but since they are no longer a free drug - cannot create a response anymore.

Front 268

How can a partial agonist become an antagonist?

Back 268

If the receptors are already activating, the partial agonist will compete for the same ligands but provide lower functionality.

Front 269

How does Viagra (sildenafil) work?

Back 269

Nitroglycerine (NO) inhibits phosphodiesterase which works to deactivate cGMP (without this, cGMP stays active and promotes relaxation of smooth muscle)

Front 270

What is the EC50 value?

Back 270

Half of the dosage at which maximal responsive was seen.

Front 271

What is LD50 value?

Back 271

Half of the dosage at which the maximal lethal/adverse side effects were seen.

Front 272

How do you calculate the therapeutic index and how does this indicate the safety of the medicine?

Back 272

LD50/ED50 = therapeutic index

The higher the number, the safer (the lethal dose is far higher than the effective dose)

Front 273

What is the IC50 value?

Back 273

In competitive ANTAGONISTS, you want to see the effective inhibition of some process (the 50% mark of maximal inhibition)

Front 274

What is the difference between competitive and non-competitive antagonists?

Back 274

Non-competitive antagonists are irreversible and the therapeutic response cannot be determined by the plasma levels of the drug.

Front 275

What determines the effective duration of an irreversible antagonist?

Back 275

The turnover rate of the receptor.

Front 276

If bound irreversibly to the receptor, how are irreversible antagonists eventually cleared?

Back 276

Via the regeneration of receptors by the cell.

Front 277

What is the difference between potency and efficacy?

Back 277

Potency is the ability to induce an effect at a lower dose - while efficacy is the ability to reach the maximal effect.

Front 278

What is an inverse agonist?

Back 278

Binds to the receptor in the inactive form (preferentially) therefore keeping most receptors inactive.

Front 279

What is the margin of safety?

Back 279

MS = LD1/ED99 (the larger the better)

Front 280

How do you calculate the half-life?

Back 280

Either graphically by seeing time it takes to get to 1/2 of initial concentration OR 0.693/k

Front 281

How long does it take to reach steady-state for a drug?

Back 281

5 half-lives.

Front 282

Calculate the loading dose.

Back 282

D_l = (C_o * V_d)/F

Front 283

Calculate the maintenance dose.

Back 283

D_m = (C_ss * Cl)/F

Front 284

How do you calculate the volume of distribution?

Back 284

V_d = (F*D)/(C_o)

Front 285

How do you calculate the clearance?

Back 285

Cl = V_d * k

Front 286

How do you determine the infusion rate?

Back 286

Q = C_ss * Cl

Front 287

If you have overdosed a patient how can you determine the new dose to reduce the concentration?

Back 287

New dose = old dose * (C-target/C-old)

Front 288

What is the purpose of calculating creatinine clearance?

Back 288

Determines the excretory capabilities of the kidneys

Front 289

How do you calculate the creatinine clearance?

Back 289

C_Cr = [urine concentration of creatinine * urine flow]/(plasma concentration of creatinine)

Front 290

If a person's creatinine clearance is low what does this imply?

Back 290

Kidney function is less than normal - thus the drug you are administering is not being excreted appropriately - and has a prolonged effect (higher likelihood of drug toxicity).

Front 291

Glucose + glucose = ?

Back 291

Maltose

Front 292

Glucose + fructose = ?

Back 292

Sucrose

Front 293

Glucose + galactose = ?

Back 293

Lactose

Front 294

Which GLUT receptors are high affinity?

Back 294

Glut 1, 3

Front 295

Which GLUT receptors are low affinity?

Back 295

Glut 2.

Front 296

Which GLUT receptor is hormone receptive?

Back 296

Glut 4 (not found in liver)....well b/c livers secrete the hormones!

Front 297

Glut 5 receptors are sensitive to ______.

Back 297

Fructose.

Front 298

What substance follows zero-order kinetics? And what IS zero-order kinetics?

Back 298

Alcohol; substance is removed in equal parts consistently (i.e. 5 mg/hr instead of a reduced fraction every time)

Front 299

What is the rate-limiting step in glycolysis?

Back 299

Conversion of fructose 1-phosphate to fructose 1,6-bisphosphatase (by PFK-1)

Front 300

What are the two energy-producing steps of glycolysis?

Back 300

1. Pyruvate kinase (conversion of PEP to Pyruvate)
2. Phosphoglycerate kinase (conversion of 1,3-BPG to 3-PG)

Front 301

What is the fate of Acetyl CoA?

Back 301

TCA cycle or fatty acid synthesis.

Front 302

How is NADH returned to NAD+?

Back 302

Respiratory chain or lactic acid fermentation.

Front 303

How does the NADH/NAD affect the rate of glycolysis?

Back 303

If the ratio is higher, then glycolysis slows down (has to wait for replenishment of NAD+).

Front 304

Why do two types of aldolases exist?

Back 304

One breaks down Fructose 1.6 BP, while the other type converts Fructose 1-P to the intermediates of glycolysis?

Front 305

What intermediate connects fructose with glucose metabolism?

Back 305

Glyceraldehyde 3-Phosphate.

Front 306

What is the energy production from glycolysis?

Back 306

2 ATP and 2 NADH

Front 307

What is the energy production from the conversion of pyruvate to Acetyl CoA?

Back 307

2 NADH

Front 308

How can hemolytic anemias be treated? And what is the purpose of this?

Back 308

Folic acid (tetrahydrofolate) supplementation - which produces thymidilate synthase responsible for regeneration of cells - in this case, RBCs.

Front 309

How does galactose metabolism link into glucose metabolism? And what is the important enzyme in this reaction?

Back 309

Glucose-6 phosphate; UDP-galactose --> UDP-glucose

Front 310

What is the significance of the Cori cycle?

Back 310

Liver uptakes the excess lactate and converts it to glucose for re-use by muscles.

Front 311

What is done with excess glucose?

Back 311

Converted to sorbitol (which is eventually converted to fructose in the liver or sperm cells).

Front 312

What is the characteristic glucose usage by tumors?

Back 312

Very high demands, stimulate HIF-1 (hypoxia-induced factors) which increase glut receptors (thus promoting growth of tumor).

Front 313

What are the clinical symptoms of an excessive fructose diet?

Back 313

Gout and hyperuricemia....excess production of fructose 1-P limits inorganice phosphate use of ADP --> ATP (thus ADP ==> AMP)

Front 314

Enzymatic defects in fructose metabolism has what effect on glycogen metabolism?

Back 314

High amounts of fructose 1-P inhibits glycogen metabolism (thus fructose can't breakdown and neither can glycogen...leading to hypoglycemia)

Front 315

What can cause lactose intolerance?

Back 315

Enzymatic defect in beta-galactosidase or aldolase reductase (either genetic, damage-induced, or from intestinal removal)

Front 316

What is excess galactose converted to - and what clinical problems does this present with?

Back 316

Galactitol; causes cataracts.

Front 317

How does fatty acid metabolism link to carbohydrate metabolism?

Back 317

Triglycerides converted to glycerol 3-P in ADIPOSE TISSUE and then converted to dihydroxyacetone phosphate in the LIVER (either going through glycolytic or gluconeogenic pathways)

Front 318

Is the process of gluconeogenesis an exact reversal of glycolytic steps? Why?

Back 318

No; you have to overcome the three irreversible steps of glycolytic.

Front 319

What is the analog of pyruvate kinase in glycolysis in gluconeogenesis?

Back 319

Pyruvate carboxylase.

Front 320

Why is there an additional step in gluconeogenesis?

Back 320

Oxaloacetate (product of pyruvate carboxylase) has to be converted to PEP (via the additional PEP carboxylase)

Front 321

Why is gluconeogenesis only limited to liver and kidneys?

Back 321

Pyruvate carboxylase is only located in the mitochondria of these organs.

Front 322

Is oxaloacetate permeable to the mitochondrial membrane? [in terms of gluconeogenesis]

Back 322

No - has to be converted to malate - crosses into the cytosol to continue the steps of gluconeogenesis.

Front 323

What is the "opposite" of a kinase? And what role does this enzyme play in gluconeogenesis?

Back 323

Phosphatase; fructose bisphosphatase and glucose 6-phosphatase convert the molecule to glucose (final two steps of gluconeogenesis)

Front 324

The functionality of gluconeogenesis is critical for the brain because....

Back 324

The brain can only consume glucose as a source of energy

Front 325

What are the energy requirements for gluconeogenesis? And what is the final product?

Back 325

6 ATP and 2 NADH required, 2 mol pyruvate become 1 mol glucose.

Front 326

How does insulin/glucagon play a role in regulation of glycolysis?

Back 326

Insulin promotes glycolysis by activating a phosphatase for pyruvate kinase; glucagon promotes gluconeogenesis by activating a kinase for pyruvate kinase.

Front 327

What is the most important regulatory molecule of glycolysis?

Back 327

phosphofructokinase-1

Front 328

How does ATP/AMP levels affect PFK-1?

Back 328

High ATP levels inhibit PFK-1 while high AMP levels activate it.

Front 329

How does PFK-2 regulate PFK-1?

Back 329

Excess glucose converted to fructose in the liver where PFK-2 converts Fructose 6-P to Fructose 1,6-BP (which activates PFK-1)

Front 330

What is the main enzyme regulated in gluconeogenesis and by what mechanism?

Back 330

Fructose 1,6-bisphosphatase - inhibited by low levels of AMP in the body.

Front 331

What bonds cause the "kinks" in glycogen?

Back 331

alpha 1,6 - glycosidic bonds

Front 332

What is the function of glycogenin?

Back 332

enzyme that provides a scaffold/support for new glycogen synthesis.

Front 333

By what mechanism is additional glucose molecules added to the initial chain of glycogen?

Back 333

UDP-glucose catalyzed by glycogen synthase to form alpha 1,4 bonds.

Front 334

What creates the alpha-1,6 glycosidic bonds in glycogen?

Back 334

Glucosyl transferase.

Front 335

Why is the branching of glycogen so important in animals?

Back 335

Makes the compound soluble (if it were purely linear would not be soluble/functional in the body)

Front 336

What is the function of glycogen phosphorylase? How is the regulation of this enzyme unique?

Back 336

Breaks down glycogen to a limit dextrin, is ACTIVATED by phosphorylation.

Front 337

What are the two debranching enzymes in the glycogen breakdown pathway?

Back 337

glucosyl transferase and alpha-1,6 glucosidase.

Front 338

What does a defect in alpha 1,4-glucosidase lead to?

Back 338

Pompe's disease (cardiorespiratory failure/death by age 2) - due to massive increase in glycogen in lysosomes.

Front 339

What is Von Gierke's disease?

Back 339

Defect in glucose 6-phosphatase which leads to accumulation of glycogen in kidney/liver (hepatomegaly and severe hypoglycemia)

Front 340

What will a defect in alpha 1,6-glucosidase cause?

Back 340

Cori disease - milder course of Von Gierke's disease.

Front 341

What is McArdle's disease?

Back 341

Defect in glycogen phosphorylase which leads to a slight increase in glycogen (painful muscle cramps, but otherwise normal).

Front 342

What is the only glycogen storage disease (that we have studied) that deals with the synthesis of glycogen?

Back 342

Andersen's disease - defect in branching enzymes [abnormal glycogen formed leading to liver failure]

Front 343

How does epinephrine glycogen degradation?

Back 343

Epinephrine signals the cAMP cascade which eventually promotes kinase activity to phosphorylate glycogen phosphorylase (which promotes glycogen breakdown).

Front 344

What are the two main purposes of the Pentose phosphate pathway (HMP)?

Back 344

Production of NADPH and ribulose phosphate (for nucleotide biosynthesis)

Front 345

What role does NADPH play in RBCs?

Back 345

Co-factor of glutathione reductase.

Front 346

The products of non-oxidative HMP can yield what type of molecules?

Back 346

Intermediates of the glycolytic pathway.

Front 347

What enzyme is required for the oxidative HMP pathway?

Back 347

Glucose 6-phosphate dehydrogenase.

Front 348

What clinical symptoms will G6PD deficiency cause?

Back 348

Hemolysis/anemia during oxidative stress of RBCs.

Front 349

What are the two main functions of the uronic acid pathway?

Back 349

Formation of:
1. Glucoronate (for glucoronidation reactions)
2. Pentose phosphates (for utilziation in HMP pahtway)

Front 350

What is the purpose of a loading dose?

Back 350

To reach a therapeutic level of a drug faster (does NOT reach steady-state faster)

Front 351

Give two examples of drugs that are NOT given orally due to first-pass effect?

Back 351

Morphine and nitroglycerine.

Front 352

What are the two main types of reactions involved with drug metabolism?

Back 352

Phase I (polarizing reactions)
Phase II (conjugation)

Front 353

What are the types of Phase I reactions?

Back 353

Oxidation, reduction, and hydrolysis

Front 354

What type of reactions are categorized under oxidation reactions?

Back 354

N-Dealkylation, O-dealkylation, deamination, and desulfuration.

Front 355

Give an example of an N-dealkylation reaction?

Back 355

Imipramine --> Desipramine.

Front 356

Give an example of an O-dealkylation reaction?

Back 356

Codeine --> morphine

Front 357

Give an example of a deamination reaction?

Back 357

Amphetamine --> Phenylacetone

Amphetamine (Adderall!)

Front 358

Give an example of a hydrolysis reaction?

Back 358

Procaine --> Cocaine

Front 359

Give an example of a desulfuration reaction?

Back 359

Parathion to paraoxon

Front 360

What are the two types of oxidation in Phase I reactions?

Back 360

microsomal and non-microsomal

Front 361

What are the two non-microsomal oxidation reactions discussed?

Back 361

Alcohol dehydrogenase and aldehyde dehydrogenase (ADH and ALDH)

Front 362

What are the two types of reduction reactions and give examples of each.

Back 362

Azoreductions (prontosil)
Nitroreductions (chloramphenicol)

Front 363

Prontosil and Levodopa are examples of....

Back 363

Prodrugs.

Front 364

What is the terminal oxidase to which the drug binds during microsomal oxidation?

Back 364

cytochrome P450

Front 365

What co-factor is required for microsomal oxidation reactions?

Back 365

NADPH

Front 366

How does malaoxon and paraoxon function as suicide synthesis?

Back 366

Originally were malathion and parathion - then converted to malaoxon and paraoxon which inhibit acetylcholinesterase (this increased amount of acetylcholine causes paralysis/death)

Front 367

What is the most frequent conjugation reaction - provide an example.

Back 367

Glucoronidation (morphine)

Front 368

Name all types of conjugation reactions and provide a drug example for each.

Back 368

Acetylation (isozianid)
Methylation (norepinephrine)
Glucoronidation (morphine)

Front 369

What substances induce P450 activity?

Back 369

Phenobarbitol, rifampin, and tobacco smoke products (PAHs)

Front 370

What substances inhibit P450?

Back 370

Cimetidine and grapefruit juice.

Front 371

While intravenous drug injections provide the most accuracy/tracking of drug concentrations - what is a very serious side effect/concern?

Back 371

Higher risk of toxic effects.

Front 372

What is the energy production of the TCA cycle (from one ACETYL CoA molecule)?

Back 372

3 NADH, 1 FADH2, and 1 GTP

Front 373

ATP homeostasis refers to....

Back 373

constant levels of ATP under normal conditions

Front 374

If delta G is negative the reaction is....

Back 374

spontaneous/moves forward

Front 375

If delta G is positive the reaction is...

Back 375

reverse reaction will tend to occur

Front 376

If detal G is zero the reaction is....

Back 376

at equilibrium

Front 377

What affects the delta G outside of the free energy of the products/reactants?

Back 377

Pressure, initial concentrations of products/reactants, and pH

Front 378

How does delta G relate to equilibrium constant?

Back 378

delta G = -1.362 * ln(Keq)

Front 379

Does the standard free energy of a reaction always have to be less than zero for a reaction to occur spontaneously?

Back 379

No, if this reaction is coupled with another reaction with standard free energy less than zero - the OVERALL delta G will be <0.

Front 380

Oxidation is...

Back 380

Loss of electrons

Front 381

Reduction is....

Back 381

Gain of electrons

Front 382

The more positive a reduction potential the more likely....

Back 382

Electrons will go there

Front 383

How do the reduction potential and standard free energy values relate?

Back 383

The greater the reduction potential, the more spontaneous/negative standard free energy is.

Front 384

Where is the energy in ATP located?

Back 384

In the phosphoanhydride bonds (phosphate groups)

Front 385

Which organ needs the most ATP?

Back 385

Kidneys (think...all that active transport of molecules/ions/water)

Front 386

How does shivering thermogenesis work?

Back 386

Muscles contract, production of ATP increases, and this energy releases as heat.

Front 387

How does non-shivering thermogenesis work?

Back 387

Brown adipose tissue inhibits thermogenin - decreases efficiency of OxPhos and H+ gradient in mitochondria no longer used for ATP-synthase but rather heat production.

Front 388

Why does FAD need to be covalently bonded to the molecule?

Back 388

Because it can produce highly reactive radicals (semiquinones) which would otherwise damage the body.

Front 389

List the four dehydrogenase enzymes involved in TCA cycle.

Back 389

isocitrate dehydrogenase
alpha-ketoglutarate dehydrogenase
succinate dehydrogenase
malate dehydrogenase

Front 390

The last three steps converting succinate to oxaloacetate is similar to what other metabolic process?

Back 390

Fatty acid oxidation and oxidation of branched chain amino acids.

Front 391

What are the three energy-driving reactions in TCA (delta G < 0)

Back 391

1. Formation of citrate
2. Isocitrate --> alpha-ketoglutarate
3. Formation of succinyl CoA (high energy thioester bond)

Front 392

What is the energy production from the conversion of pyruvate to acetyl CoA (just one molecule)?

Back 392

1 NADH

Front 393

What is the only dehydrogenase complex that resides in the inner mitochondrial membrane?

Back 393

Succinate dehydrogenases, all other DHs are located in the matrix.

Front 394

List all three alpha-ketoacid dehydrogenase complexes...

Back 394

1. pyruvate dehydrogenase
2. alpha ketoglutarate dehydrogenase
3. branched chain alpha-ketoacid DH

Front 395

What are the 5 cofactors of these alpha-ketoacid dehydrogenase complexes...

Back 395

1. FAD (prosthetic group)
2. NAD
3. TPP (Thiamine) (prosthetic group)
4. Lipoate (prosthetic group)
5. Coenzyme A (co-substrate)

Front 396

What clinical symptoms may result in thiamine deficiency (which can often occur in chronic alcoholics)?

Back 396

Alpha ketoglutarate, pyruvate, and alpha keto-acid accumulation in the blood.

Front 397

What are the two main purposes of the TCA cycle?

Back 397

1. NADH/FADH2 production
2. Production of intermediates for gluconeogenesis, heme and AA syntehsis

Front 398

Isocitrate dehydrogenase is the only dehydrogenase enzyme sensitive to what regulatory mechanism?

Back 398

ADP stimulates the activity.

Front 399

Malate dehydrogenase is ONLY sensitive to which regulatory mechanism?

Back 399

NAD+ stimulates its activity.

Front 400

What effect does calcium have in TCA cycle?

Back 400

Up-regulates isocitrate DH, alpha ketoglutrate DH, and pyruvate DH.

Front 401

Why are problems with glucose metabolism first detected in the CNS?

Back 401

Because the brain relies heavily on oxidation of glucose and no other energy source - so it is the most sensitive organ.

Front 402

Pyruvate dehydrogenase is regulated by...

Back 402

PD Phosphatase and PD kinase

Front 403

List the three components of the PD-complex.

Back 403

E1 - TPP
E2 - lipoate
E3 - FAD

Front 404

What is the only regulator of PD-phosphatase?

Back 404

Activated by calcium.

Front 405

What all regulates PD-kinase?

Back 405

High levels of ADP and pyruvate INHIBIT kinase (so activate dehydrogenase).
NADH and Acetyl CoA activate kinase to inhibit dehydrogenase.

Front 406

What does a PDC (pyruvate dehydrogenase complex) insufficiency lead to?

Back 406

Severe lactic acidemia (in its severe form can lead to death).

Front 407

How does arsenic poisoning manifest itself?

Back 407

Covalently binds to lipoate on all alpha-ketoacid dehydrogenase complexes - thus removing the functionality of the coenzyme and subsequently the enzyme.

Front 408

How do you obtain cytosolic Acetyl CoA?

Back 408

Cleave citrate (which has traveled to cytosol) into Acetyl CoA and OAA [requires ATP]

Front 409

Succinyl CoA is used as the precursor to....

Back 409

heme.

Front 410

What are the two TCA cycle intermediates that contribute to amino acid synthesis?

Back 410

Oxaloacetate, alpha ketoglutarate.

Front 411

What intermediate of the TCA cycle is utilized in gluconeogenesis?

Back 411

Malate.

Front 412

What intermediate of the TCA cycle is utilized for fatty acid synthesis?

Back 412

Citrate.

Front 413

If all these intermediates are utilized for other pathways - how are they restored to prevent depletion of oxaloacetate?

Back 413

Aneplerotic reactions

Front 414

What are the two main aneplerotic reactions?

Back 414

Pyruvate carboxylase converting pyruvate to OAA.

Synthesis of Succinyl CoA from Ile and Val.

Front 415

Leigh's disease can be caused by what to type of deficiencies?

Back 415

Pyruvate carboxylase deficiency and pyruvate dehydrogenase complex deficiency.

Front 416

Pyruvate carboxylase is regulated by...

Back 416

Acetyl CoA (once enough Acetyl CoA is formed, then it will promote the transformation of pyruvate to OAA)

Front 417

List the order of the electron transport chain...

Back 417

Complex I (NADH DH)
Coenzyme Q
Complex III (b-c)
Cytochrome C
Complex IV (cytochrome c oxidase)

Front 418

What gradient is responsible for the functionality of ATP-synthase?

Back 418

H+ gradient.....high in the intermembrane space and low in the matrix.

Front 419

One turn of the rotor requires ______ protons and synthesizes _____ ATPs.

Back 419

11-12; 3.

Front 420

Since Coenzyme Q contains a quinone....this can lead to the formation of....

Back 420

Semiquinones (free radicals)

Front 421

Each cytochrome contains a bound ______ and therefore requires _____.

Back 421

heme; iron

Front 422

In anemic patients - not only is Hb and Mb function affected, but also....

Back 422

Electron transport chain (because of the dependence of each complex on iron).

Front 423

What is Hemoglobin M?

Back 423

Stabilization of methoglobin (oxidized form of hemoglobin) which can be fatal if homozygous (leads to cyanosis)

Front 424

Only 30-40% of energy gained by NADH and FADH2 are utilized for ATP synthesis....where does teh rest go..

Back 424

Transportation of anions and formation of heat.

Front 425

Anoxia results in the stopping of the _____ ______ _____.

Back 425

Electron transport chain.

Front 426

Carbon monoxide, cyanide, and azide poisoning bind to ________ and stop ____ ____ _____ thus mimicking the effects of _______.

Back 426

cytochrome c oxidase, electron transport chain, anoxia

Front 427

What is a concern when administering sodium nitroprusside for hypertension?

Back 427

Liver can metabolize this drug into cyanide and therefore the thiocyanate levels in the blood must be monitored.

Front 428

OxPhos diseases are typically linked to problems in _____.

Back 428

Mitochondrial DNA.

Front 429

When oxidation is not coupled to phosphorylation what happens?

Back 429

ATP is not synthesized - so the body keeps signaling higher activity of ETC (thus you are increasing the H+ gradient) - so there is increased oxygen consumption and heat production.

Front 430

Dinitrophenol is an example of a....

Back 430

chemical uncoupler

Front 431

Salycilate poisoning (a metabolite of aspirin) can cause....

Back 431

OxPhos uncoupling and therefore overstimulation of glycolytic pathways without ATP production (thus metabolic acidosis)

Front 432

Uncoupling proteins (UCP) can reduce the likelihood of radical formation from Coenzyme Q because....

Back 432

Uncoupling stimulates ETC, thus CoQ is more occupied.

Front 433

How does Pyruvate and ADP enter the matrix of the mitochondria?

Back 433

Through voltage-gated channels

Front 434

How does pyruvate and inorganic phosphates enter the matrix?

Back 434

Via symport with hydrogen ions.

Front 435

How does calcium enter the matrix?

Back 435

Through a uniport (driven by the water potential)

Front 436

How does ATP leave the matrix once produced by ATP-synthase?

Back 436

First by an antiporter (ATP-translocase) with ADP into the intermembrane space, and then via a voltage-dependent anion channels in the outer membrane.

Front 437

What is the key component (intermediate) required to bring metabolites into the matrix of the mitochondria?

Back 437

Malate.

Front 438

The Mitochondrial Permeability Transition Pore (MPTP) is a complex of....

Back 438

Antiporter and Voltage-dependent Anion channel.

Front 439

The proton gradient helps keep the ______ (open/closed) in the MPTP.

Back 439

ANT (antiporter) closed.

Front 440

High amounts of ______ and _____ keep the VDAC in the MPTP (open/closed)

Back 440

hydrogen ions, ATP - keep it closed.

Front 441

Why is it criticial to know that Bax and Bcl-2 connect/control the VDAC?

Back 441

Bax is pro-apoptotic, and Bcl-2 is anti-apoptotic - so cellular signaling may stimulate Bax to open VDAC and cause mitochondrial/cell lysis.

Front 442

Calcium and reactive oxygen species both promote the _______ of the antiporter.

Back 442

Opening.

Front 443

What is ischemia reperfusion injury?

Back 443

If the patient has been oxygen-deprived too long, and you "shock" the patient - the reversal of the ATP synthase at this point will cause the addition of oxygen to induce more problems.

Front 444

Glycolysis is the main energy-producing pathway in the _____ and ______.

Back 444

brain and red blood cells.

Front 445

Why is AMP instead of ADP used as an allosteric activator of PFK-1?

Back 445

Concentrations are usually kept low by adenylate kinase - therefore any alterations/changes will have a greater effect/sensitivity.

Front 446

The transport of NADH into the mitochondria occurs by two pathways, which are....

Back 446

Malate-aspartate shuttle
Glycerol-3-phosphate - DHAP shuttle.

Front 447

Which NADH shuttle pathway reduces the amount of energy available afterwards?

Back 447

G3P - DHAP shuttle

Front 448

If we assume 3 ATP/NADH and 2 ATP/FADH2, what is the total energy production from 1 mol of glucose?

Back 448

38 ATP.

Front 449

If there is an issue with fatty acid metabolism, the clinical symptom that will almost always appear is...

Back 449

Episodes of hypoglycemia during fasting/sleeping.

Front 450

Fatty acids bind to ______ in the blood.

Back 450

Albumin.

Front 451

How do you activate a fatty acid for metabolism?

Back 451

Attach fatty acid to Acyl CoA via a thiokinase.

Front 452

How is the activated fatty acyl CoA transported into the mitochondria?

Back 452

Carnitine.

Front 453

What is the destination of Acetyl CoA in the body?

Back 453

Oxidation in the TCA or ketone body synthesis.

Front 454

Why is CPT I and CPT II required in the cell?

Back 454

Fatty acyl CoA cannot diffuse into the mitochondrial matrix without the attachment to carnitine which is facilitated by CPT I and CPT II.

Front 455

CPT II deficiency leads to ______.

Back 455

hypoglycemia and myoglobinuria.

Front 456

After each cycle of Beta-oxidation how many carbons are lost?

Back 456

Two.

Front 457

Each cycle of Beta-oxidation produces ....

Back 457

1 FADH2 and 1 NADH

Front 458

If you have a 20C fatty acid, what is the product?

Back 458

9 FADH2, 9 NADH, and 10 Acetyl CoA.

Front 459

What are the four steps of Beta-oxidation?

Back 459

1. oxidation
2. hydrolysis
3. oxidation
4. addition of Co-A

Front 460

In Medium-chain acyl coA (MCAD) deficiency what is the clinical manifestation?

Back 460

Acylcarnitines in the blood/ruine, and hypoglecemia and hypoketosis.

Front 461

What is the main difference (in clinical signaling) between MCAD and LCAD deficiency?

Back 461

Acylcarnitines are only in blood and does not show up in urine

Front 462

What happens in an odd-chain fatty acid?

Back 462

Last two products are propionyl CoA and acetyl CoA.

Front 463

What is the product of propionyl CoA?

Back 463

Converted to succinyl CoA with the help of cobalamin (B12) which then goes into glycolysis or heme production.

Front 464

High amounts of FADH2 and NADH (inhibit/stimulate) Beta-oxidation.

Back 464

Inhibit.

Front 465

How does Acetyl CoA indirectly regulate the Beta oxidation?

Back 465

Acetyl CoA is converted to Malonyl CoA thus inhibiting Beta oxidation to prevent further production of Acetyl CoA.

Front 466

How is Acetyl CoA carboxylase regulated and what is its function.

Back 466

Converts Acetyl CoA to malonyl CoA - inhibited by high AMP levels and promoted by insulin.

Front 467

Name two alternate pathways of fatty acid metabolism.

Back 467

Peroxisomal Beta-oxidation and microsomal omega-oxidation.

Front 468

Why doesn't peroxisomal oxidation result in energy production?

Back 468

Because the FADH2 is utilized for reduction of hydrogen peroxide and the remaining 4-6 carbon fatty acid is shifted to the mitochondria.

Front 469

What enzyme converts hydrogen peroxide to water?

Back 469

Catalase.

Front 470

What is the purpose of alpha-oxidation?

Back 470

Due to the additional methyl groups - it only reduces it by one carbon so further Beta oxidation can avoid the methyl groups.

Front 471

What is the purpose of omega oxidation?

Back 471

Converts terminal carbon in fatty acid to carboxylic acid (thus becomes a dicarboxylic acid)

Front 472

What is the regulatory mechanisms of fatty acid oxidation?

Back 472

Substrate levels and THAT'S IT!!

Front 473

If there is any deficiency in beta-oxidation or carnitine what will this manifest as in a clinical test?

Back 473

Presence of dicarboxylic acids in the urine.

Front 474

What is the product of ketone body synthesis?

Back 474

Acetone and Beta-hydroxybutarate.

Front 475

What is an important intermediate of ketone body synthesis and what is an alternate synthetic pathway?

Back 475

HMG CoA....can go into cholesterol production.

Front 476

Ketone bodies can be fuel for the ________ and _______ , but NOT the ______.

Back 476

Skeletal muscle, brain, liver

Front 477

What is the energy production of acetoacetate (main ketone body functioning).

Back 477

Two acetyl CoAs (so 20 ATP total) minus 1 ATP for conversion of acetoacetate to acetyl CoA.

Front 478

What is a possible treatment for pyruvate dehydrogenase deficiency?

Back 478

Ketogenic diet (avoids the need for pyruvate to convert into Acetyl CoA)

Front 479

Why do you see a larger rise in ketone bodies once the body has compensated via fatty acid metabolism?

Back 479

Because the skeletal muscle has lower energy demands - thus not utilizing glucose nor ketone bodies.

Front 480

What is the Jamaican vomiting sickness?

Back 480

ingestion of hypoglycin inhibits acyl CoA dehydrogenase - thus beta oxidation is inhibited and sever hypoglycemia occurs.

Front 481

Which are the only two TRUE ketogenic amino acids?

Back 481

Lysine and leucine.

Front 482

What is propionic acidemia and aciduria?

Back 482

Defect in propionyl-CoA carboxylase leading to an accumulation of propionyl CoA ... as a false substrate to isocitrate....will cause depletion of oxaloacetate and increase in methylcitrate in the urine.

Front 483

What enzyme allows the recycling of biotin in the body?

Back 483

Biotinidase

Front 484

What is methylmalonic aciduria?

Back 484

Defect in methylmalonyl CoA mutase - thus excretion of methylmalonate in the urine is very high.

Front 485

Defects in branched chain alpha-keto acid dehydrogenase leads to....

Back 485

Maple-syrup disease (due to increase in ketoacids in the urine leading to syrup odor"

Front 486

If there is a defect in phenylalanine hydroxylase this causes...

Back 486

Phenylketonuria (phenylalanine is converted in the body to phenylketones)

Front 487

What is the disorder that leads to urine that immediately stains upon exposure to air?

Back 487

Defect in homogentisate oxidase called alkaptonuria.

Front 488

What is tyrosinemia I?

Back 488

Defect in fumarylacetoacetate hydrolase or maleylacetoacetate isomerase which leads to a cabbage-like odor and liver failure.

Front 489

How do you detect Tyrosinemia I?

Back 489

Succinylacetone accumulates in the body.

Front 490

Is Tyrosinemia I more or less severe than Tyrosinemia II?

Back 490

More severe, Tyr. II has a defect earlier in the pathway at tyrosine aminotransferase.

Front 491

What are all the essential amino acids?

Back 491

FILM TV WK HR
phenylalanine, isoleucine, leucine, methionine, threonine, valine, tryptophan, lysine, histidine, arginine

Front 492

Are amino acids a major source of energy?

Back 492

No - fatty acids and glucose are main sources of energy.

Front 493

What are all the ketogenic amino acids?

Back 493

Why Fuck Your King In London?

Tryptophan, phenylalanine, tyrosine, lysine, isoleucine, leucine.

Front 494

Which is more likely to diffuse into the cell - large or small molecules?

Back 494

Small molecules.

Front 495

Which is more likely to diffuse into the cell - polar or non-polar molecules?

Back 495

Non-polar.

Front 496

Which is more likely to diffuse into the cell - ionic or neutral molecules?

Back 496

Neutral.

Front 497

The concentration of all ions are greater outside the cell EXCEPT ______.

Back 497

K+ and proteins.

Front 498

What are the two types of passive diffusion?

Back 498

Simple diffusion (osmosis) or facilitated diffusion.

Front 499

There are two types of facilitated diffusion...

Back 499

Channel and carrier proteins.

Front 500

Which type of facilitated diffusion is non-specific...channel or carrier?

Back 500

Channel.

Front 501

What are the different types of ways channel proteins are selective (without binding to a specific molecule)?

Back 501

Voltage-gated
Ligand-gated
Stress-induced

Front 502

What are the three types of active transport?

Back 502

Symport, antiport, and uniport

Front 503

Does all active transport require energy?

Back 503

YES!

Front 504

The cytoplasmic side of the membrane is usually ______ and the extracellular side is usually ______.

Back 504

Negative; positive

Front 505

What is the significance of the Na-K pump?

Back 505

Maintains the potassium levels high inside and the sodium levels low within the cell.

Front 506

Active transport that utilizes ATP is called...

Back 506

Primary active transport.

Front 507

Active transport that utilizes an electrochemical gradient is called...

Back 507

Secondary active transport.

Front 508

What is the advantage of having very low Calcium concentrations within the cell?

Back 508

Allows sensitivity for signaling (much like how AMP is more sensitive than ADP as a signaling molecule)

Front 509

If the extracellular area is hypertonic then what happens....

Back 509

Cellular water will leave the cell and cell will shrink.

Front 510

If the extracellular area is hypotonic then what happens....

Back 510

Water will flow into the cell and cell will lyse.

Front 511

How is water permeable in the cell membrane?

Back 511

Aquaporins!

Front 512

What percent of the total body weight is water?

Back 512

60%

Front 513

What is the extracellular fluid percentage in the body? Intracellular?

Back 513

Intracellular is 40%....extracellular is 20%

Front 514

What two forces work for flow of fluids in and out of capillaries?

Back 514

Hydrostatic and oncotic pressures.

Front 515

What is the main change in arterioles and venuoles that allow fluid to leave arterioles and fluid to re-enter capillaries?

Back 515

Hydrostatic pressure changes.

Front 516

Vasodilation will ______ hydrostatic pressure while vasoconstriction will ______ hydrostatic pressure and typically acts on the _____.

Back 516

decrease; increase, venous return.

Front 517

What is the purpose of lymphatic system?

Back 517

Not all fluid perfectly returns to the blood circulation - this extra fluid goes into the lymphatic system.

Front 518

What is edema?

Back 518

Excess accumulation of fluids in the interstitial compartment.

Front 519

What is the difference between paracrine and endocrine signaling?

Back 519

Paracrine is nearby, endocrine travels through the blood.

Front 520

How do G-protein linked receptors work?

Back 520

GTP binds, alpha unit splits from beta-gamma unit, cascade of proteins, when action done - GTP hydrolyzed and G-protein reassociates.

Front 521

What is an example of contact signaling?

Back 521

Immune response and antibodies!

Front 522

What is a critical characteristic of those molecules that are intracellular receptors?

Back 522

Lipid-soluble! They must transgress through the membrane.

Front 523

What does nitric oxide stimulate?

Back 523

Guanylyl cyclase....increases cGMP.

Front 524

What does sildenafil do?

Back 524

Inhibits phosphodiesterase, prolongs action of cGMP.

Front 525

What are enzyme-linked receptors?

Back 525

Receptors that have enzymatic activity on their own (growth factors).

Front 526

What mechanism do cGMP and guanylyl cyclase follow?

Back 526

Intracellular receptors.

Front 527

What are the two types of secondary messengers in G-protein coupled receptors?

Back 527

cAMP and DAG/IP3 (protein kinase)

Front 528

What is the enzyme-linked receptor pathway mechanism?

Back 528

Receptor dimerizes, cross-phosphorylation, SH2 then Ras binds - Ras signals a series of protein cascades.

Front 529

30% of cancers are involved with mutations of _____.

Back 529

Ras.

Front 530

What are the two other signaling pathways that resemble enzyme-linked receptors?

Back 530

JAK/STAT - fewer intermediates than enzyme-linked.

TGF-Beta - kinases activate SMADs directly affect gene transcription

Front 531

What are the pro-apoptotic proteins?

Back 531

Bax, Bak
BH3 (separate family of proteins)

Front 532

What are the anti-apoptotic proteins?

Back 532

Bcl-2

Front 533

Once the apoptotic enzymes are activated...what happens...

Back 533

Binds to Apaf to create the apoptosome which then initiates the caspases which lyse specific parts of the cell.

Front 534

Apaf is an ______ protein while the caspases are the ______ proteins.

Back 534

adaptor; effectors

Front 535

How are the pro-apoptotoic proteins activated?

Back 535

Stress-induced or loss of cytokine signals induces the BH3 to throw off the equilibrium of Bcl/Bax (less Bcl) - thus beginning the apoptotic pathway.

Front 536

Aside from stress-induced signals, what is another intracellular apoptotic signal?

Back 536

p53 can induce transcription of Bax or BH3....it can ALSO stimulate death receptors for the EXTRINSIC pathway.

Front 537

What is the extrinsic apoptotic pathway?

Back 537

Death receptors induce tumor necrosis factor (TNF) and induces cytoplasmic proteins which activate caspase 8.

Front 538

What role does cytotoxic T lymphocytes play in apoptosis?

Back 538

Granzyme B from T-cell or NK cell enters the cell via the perforin pore which then activates caspases.

Front 539

How does hypoxia induce cell injury?

Back 539

Lack of oxygen, ATP not produced sufficiently, ion equilibrium lost, ions swell into the cell and lysis can occur unless reversed.

Front 540

What is ischemia?

Back 540

Loss of blood flow to an area.

Front 541

What is anoxia?

Back 541

Extremely low to no oxygen in the system.

Front 542

What is hypoxia?

Back 542

Lack of oxygen (either induced by ischemia or lack of oxygen inspiration)

Front 543

Necrosis is cell ______ while apoptosis leads to cell ______.

Back 543

swelling; shrinking

Front 544

In time of cell injury all activity in the cell decreases except for.....

Back 544

Proteases.

Front 545

High levels of calcium stimulate...

Back 545

degradative enzymes...phospholipases, proteases, and the MPTP is opened.

Front 546

WHat is the Fenton reaction?

Back 546

Utilizes iron as a co-reactant to oxidize peroxide into a hydroxyl and a reactive hydroxyl molecule.

Front 547

What type of cellular damage can ROS cause?

Back 547

Fragmentation of membrane proteins and oxidative damage to nuclear DNA (thymidine and quinine)

Front 548

What are the two reactions by which hydrogen peroxide is reduced to water?

Back 548

1. Catalase (peroxisomes)
2. Glutathione reductase then peroxidase (uses NADPH)

Front 549

What is atrophy?

Back 549

Cell shrinkage.

Front 550

What is hypertrophy?

Back 550

Increased cell size (typically due to increased functional demand).

Front 551

What is hyperplasia?

Back 551

Greater NUMBER of cells.

Front 552

What is metaplasia?

Back 552

Differentiation into a different type of cell than what is normal.

Front 553

Hypertrophy can occur in ______, ______, and ______ muscles BUT hyperplasia can only occur in ______ muscles.

Back 553

Smooth, cardiac, skeletal; smooth

Front 554

What is psoriasis?

Back 554

A type of hyperplasia of the skin.

Front 555

What are keloids?

Back 555

Hypertrophic scars.

Front 556

Metaplasia in the conjunctiva (goblet cells isntead of squamous epithelial) is caused by....

Back 556

Vitamin A deficiency.

Front 557

What is a hydropic change?

Back 557

Accumulation of water due to ionic changes (typically induced by lack of ATP)

Front 558

What is steatosis?

Back 558

Fat accumulation in the liver.

Front 559

What are xanthomas?

Back 559

Intracellular accumulation of cholesterol (hyperlipidemias, atherosclerosis, inflammation)

Front 560

What is anthracosis?

Back 560

Accumulation of carbon in the lungs (not necessarily harmful).

Front 561

What are mallory bodies?

Back 561

Accumulation of proteins typically due to liver damage.

Front 562

What is pneumoconiosis?

Back 562

inflammatory response to carbon/silica dust particles.

Front 563

What is hemosiderin and how can you detect it in cells?

Back 563

Hemosiderin is present in high-iron cells (can be caused of hemolytic anemias) - stains Prussian blue.

Front 564

What is hemochromatosis?

Back 564

Excessive iron in the liver due to cirrhosis and heart failure.

Front 565

What is bilirubin?

Back 565

End product of hemoglobin metabolism.

Front 566

What can cause the accumulation of bilirubin in the hepatocytes? (brown-pigment staining)

Back 566

Excess bilirubin production, impaired bile flow, impaired excretions, reduced hepatic uptake.

Front 567

What is lipofuscin?

Back 567

Can occur in aging people - completely normal "wear and tear" pigment.

Front 568

What are the four types of necrosis?

Back 568

Coagulative, liquifying, caseating, and fat.

Front 569

True/false: Necrosis releases proteolytic enzymes that can damage adjacent cells.

Back 569

True.

Front 570

What usually causes coagulative necrosis?

Back 570

Ischemia/hypoxia injuries leads to dead myocytes.

Front 571

What other type of response will you see around sites of necrosis?

Back 571

Acute inflammatory response - apoptosis comes from macrophages.

Front 572

Bacterial and fungal infections along with brain ischemia leads to what type of necrosis?

Back 572

Liquefactive necrosis.

Front 573

Caseating necrosis normally associated with....

Back 573

tuberculosis.

Front 574

Pancreatitis and direct trauma to the breast typically lead to what type of necrosis?

Back 574

Fat.

Front 575

How do -PRIL drugs work (like captopril)?

Back 575

ACE inhibitors thus preventing vasconstriction - treats hypertension.

Front 576

What does Atorvastatin inhibit?

Back 576

HMG CoA Reductase (reduces cholesterol synthesis...treats high cholesterol).

Front 577

How does digoxin function?

Back 577

Inhibits the Na-K ATPase pump - slows down stimulation of action potentials (for cardiac arrythmias).

Front 578

What drugs inhibit cyclooxygenase?

Back 578

NSAIDs - treats inflammatory responses and headaches, etc.

Front 579

How does nitroglycerine function?

Back 579

Promotes guanylyl cyclase and increases production of cGMP.

Front 580

Why is nitroglycerine and sildenafil (viagra) a dangerous combination?

Back 580

Both increase the levels of cGMP - this excess prolongation of sympathetic stimulation can reduce the blood pressure to dangerous levels.

Front 581

How does heparin function?

Back 581

Inhibits prothrombin III to prevent clotting (anticoagulant).

Front 582

How does minoxidil work?

Back 582

ACTIVATES potassium-channels to promote relaxation of smooth muscle (was for hypertension....now for hair loss!)

Front 583

What does dilitazem, nifedipine, and lidocaine function as?

Back 583

Ion-channel blockers.....typically reduces the signaling/excitation - can treat arrythmias.

Front 584

How does omeprazole work?

Back 584

Inhibits hydrogen pump that releases acid into the gut - treated for acid reflux and ulcers.

Front 585

How does fluoxetine work?

Back 585

Inhibits uptake of serotonin - for antidepression.

Front 586

What is amytryptaline?

Back 586

Inhibits norepinephrine uptake - for anti-depression.

Front 587

How do diuretics function?

Back 587

Ethacrynic acid and hydrochlorothiazide both block ion reabsorption in the renal tubules (promotes excretion).

Front 588

How does epinephrine work?

Back 588

Agonist to Beta receptors - induces cAMP - stimulates heart rate.

Front 589

How does isoproterinol work?

Back 589

Beta-2 receptors for the lungs - bronchodilation treated for ashtma.

Front 590

What are beta-blockers used for cardiology?

Back 590

Propanolol (other -OLOL drugs) block these receptors to reduce the stimulation for hypertension.

Front 591

What does naloxone do?

Back 591

Morphine receptor blocker - treats morphine overdose.

Front 592

What is losartan?

Back 592

Angiotensin II receptor blocker - prevents vasconstriction for hypertension.

Front 593

How do allergy medications work?

Back 593

They are histamine receptor blockers to stop inflammation response!

Front 594

Give two examples of drugs that function as enzyme-linked receptors?

Back 594

Growth factors and insulin.

Front 595

How do steroids work?

Back 595

They are intracellular receptors and alter transcription.

Front 596

What is omalizumab for?

Back 596

Binds to IgE to control asthmatic response.

Front 597

What is cisplatin?

Back 597

Alkylating agent to treat cancer.

Front 598

What is vincristine?

Back 598

Binds to microtubules to control cancer growth.

Front 599

If the reflection coefficient is 1 what does that mean about permeability?

Back 599

The membrane is IMPERMEABLE.