Fun 1 Test 2

Front 1

Functions of Epithelium
1. Protection
2. Absorption
3. Secretion
4. Excretory
5. Lubrication
6. Sensory
7. Reproduction

Back 1

1. Epidermis.
side note, epidermis is going to line all of your cavities, respiratory tract, oral and nasal cavity down to alveoli of the lungs
these systems are open --> systems that interact with outside enviroments
closed systems - no interaction with outside environment, like vasculature
2. cells in the digestive tract, secreting digestive enzymes
3. secretory cells within glands are derived from epithelial tissue
4. Excretory - in the kidneys
5. present in the pleura, pericardium and peritoneum, allows movement of organs within cavities
6. many cells are derived from epithelium, like taste buds and retina
7. in males, sperm are modified epithelial cells

Front 2

Structural features of epithelium
1. What does epithelium cover?
2. what does epithelium sit on?
3. Is epithelium vascular?
4. Are cells polarized?
5. Which germinal layers is epithelium derived from?

Back 2

1. free or exposed body surfaces, can be an outside environment or a body cavity
2. Basement membrane
3. No. Skin is a barrier and a protection, we don't want blood picking up external toxins and stuff. All nutrients come from diffusion across the basement membrane
4.

4. Ahhh yeah. Facing the lumen is apical domain, facing other cells and basement membrane is basolateral domain

5. all three germ lines

Front 3

Transport across epithelium / tight junctions
1. What creates watertight barrier in a cell?
2. Do they ever leak? Why?
3. Need another name for tight junction, can't remember it

Back 3

1. tight junction
2. yes. they leak on PURPOSE, in case a lot of material needs to be absorbed
3. occluding junction. I remembered.

Front 4

Basal lamina
1. serves as the interface between epithelia and the...
2. How does it anchor the cell?
3. Basal lamina serves as what kind of barrier?
4. Also involved in signaling, growth, and...

Back 4

1. underlying connective tissue
2. physically binds the epithelial cells to factors and proteins
3. a diffusion barrier - epithelial cells have to receive nutrients through diffusion, and the basal lamina is the barrier that filters
4. repair. During growth and repair, molecules in the basement membrane will bind and sequester growth factors

Front 5

WHAT IS THE DIFFERENCE BETWEEN THE BASAL LAMINA AND THE BASEMENT MEMBRANE?


THIS QUESTION HAS HAUNTED MY DREAMS FOR YEARS

Back 5

Basal lamina is the physical structure, basement membrane is the structure referred to in microscopy. It is the structure we can predominantly see

Front 6

The basal lamina is a filter. What specific structure can we reference?

Back 6

the glomeruli

Front 7

Any time we want to move material without a bunch of connective tissue in the way, we will the arrangement found in the

Back 7

glomerulus! and...deep in the lung!

Front 8

Basal lamina
1. How can we see the basal lamina?
2. What two layers does it have?
3. What major component is secreted by epithelial cells?
4. What shape is this in?
5. how does laminin attach to cell?
6. What kind of collagen is in the basal lamina, and is the major component of epithelial cells?
7. There are also accessories that contain linkers, like...

Back 8

1. by EM
2. Lamina densa (dense layer)
laminae lucidia (on one or both sides of the dense layer
3. laminin - self assemble to form lace like sheets
4. cross shaped
5. integrins
6. Type IV collagen
7. nidogen, perlecan, and others

Front 9

Major components of basal laminae and extracellular matrix
1. Many of components in basal lamina are proteins, and some of these proteins are...
2. What is the best stain to see some carbohydrate proteins?

Back 9

1. glycosylated
2. PAS

Front 10

Protein or Glycosaminoglycan?
1. laminin
2. perlecan
3. Type IV collagen
4. nidogen
5. hyaluronan
6. fibrillar collagen
7. decorin
8. aggrecan
9. fibronectin

Back 10

1. protein
2. protein/GAG
3. protein
4. nidogen
5. GAG
6. protein
7. protein/GAG
8. protein core, mostly GAG bristles
9. protein

Front 11

Organization of the basement membrane
1. what makes up the criss cross network?
2. What are integrins and what do they react with?
3. what keeps the cell attached to basal lamina?

Back 11

1. laminin
2. cell surface receptors that react with laminin
3. laminin + integrin complex

Front 12

Are the connections of the molecules connected in a covalent or noncovalent way?

Back 12

Noncovalent way

Front 13

How is basal lamina attached to connective tissue below?

Back 13

Collagen VII loops around reticular fibers of connective tissue in the reticular layer

Front 14

Classification of epithelial tissue
1. do all epithelium sit in a basement membrane and have polarity?
2. Classification based on
3. simple
4. stratified
5 pseudostratified

Back 14

1. Yes
2. cell shape, number of layers, presence of specialized structures
3. epithelium with one layer
4. epithelium with multiple layers
5. falsely stratified, like so false. super duper duper duper

Front 15

Classification of Epithelial Tissue
1. squamous
2. cuboidal
3. columnar
4. Transitional

Back 15

1. looks like a fried egg, prominent nucleus with very thin cell cytoplasm
2. shaped like a cube
3. shaped like a column
4. unique to urinary tract, has special properties that allow it to distend

Front 16

Simple squamous epithelium
1. Found lining the blood vessels. What is the proper name for this?
2. What are these cells (number1) specialized to do?
3. What is on the distal end of basement membrane, made of loose dense connective tissue that's underlying an epithelium
4. Also found lining body cavities, secretes lubricant to keep organs moving around. what's the tissue layer called?
5. Also found where? (where things must be transferred)

Back 16

1. Endothelium
2. make blood clots, interact with white blood cells
3. lamina propria
4. mesothelium
5. kidney and lung cells

Front 17

Simple cuboidal epithelium:
where at?

Back 17

lines most exocrine glands, kidney tubules, thyroid follicles, surfacy of ovary

Front 18

Simple Columnar Epithelium
1. what does it line?
2. what specializations can it have?
3. Where is the nucleus usually located?
4. If it is simple layer, does that mean every cell is the same?

Back 18

1. stomach, intestines, gallbladder, some exocrine glands
2. cilia and microvilli
3. Basolateral region
4. No. stomach is all simple columnar but it is interspersed with chief cells, parietel cells, mucous cells,

Front 19

Pseudostratified epithelium
1. all cells sit on...
2. looks like multiple layers but it is really a
3. where found?

Back 19

1. basement membrane
2. single layer
3. trachea, bronchi, nasal cavity, male reproductive tract

Front 20

Stratified squamous
1. where found?
2. which is always assumed, keratinized or non keratinized?

Back 20

1. epidermis, oral cavity, esophagus, vaginal canal
2. non keratinized

Front 21

are the mouth, tongue, keratinized or non keratinized?

Back 21

Non keratinized

the tongue is keratinized

Front 22

Stratified cuboidal and stratified columnar
1. where found?
2. how many layers, typically?

Back 22

1. glands - salivary glands, sweat glands, pancreatic glands, and anorectal junction
2. not any more than two

Front 23

Transitional epithelium:
1. restricted to the...
2. looks like...

Back 23

urinary tract

puffy pillows

Front 24

Glands
types
1. Exocrine
2. Endocrine

Back 24

1. secretes content into lumen, ductwork
2. cells secrete directly into environment, usually vascular and into blood stream

Front 25

Development of glands
1. how do all glands begin?
2. structure of a gland consists of 2 parts:
3. do exocrine glands keep their duct work?
4. Do endocrine glands keep their duct work?

Back 25

1. epithelial tissue that invaginates through connective tissue
2. secretory portion and duct work
3. yes
4. NO, they lose the duct work and are infiltrated with vasculature

Front 26

Classification of Exocrine Glands
1. Structural organization, like
2. Nature of secretory products. SO, serous:
3. mucous:

Back 26

1. simple tubed, compound
2. secretes protein materials. cells have a lot of RER and secretory granules. Red dots on slide 50
3. secrete glycoprotein solution, like a goblet cell

Front 27

What are the name of cells that help glands to contract?

Back 27

Myoepithelial cells

Front 28

What are three ways to classify exocrine glands?

Back 28

1. structural organization
nature of secretory products
mechanism of secretion

Front 29

Mechanisms of secretion:
Merocrine secretion

Back 29

Basic exocytosis pathway. Granules build up, fuse with the plasma membrane, contents are delivered outside

Front 30

Holocrine secretion
what is it?

where is it found?

Back 30

secretory cell itself disintegrates and whole cell is secreted.

EXCLUSIVELY in sebaceous glands of the skin

Front 31

Apocrine secretion
What is it?

example:

Back 31

part of apical membrane pinches off to become secretion.

mammary glands

Front 32

When you hear a cell is a secretory cell, it is going to be...

Back 32

MEROCRINE

unless otherwise specified

Front 33

Cellular adaptation

1. Hypertrophy
2. Atrophy
3. Hyperplasia
4. Hypoplasia
5. Metaplasia
6. Dysplasia

Back 33

1. increase in cell size
2. decrease in cell size
3. increase in cell number
4. decrease in cell number
5. transformation of one type of epithelium to another. smoker's lung epithelium becomes more stratified to protect against smoke damage
6. total abnormal change in a cell type

Front 34

Epithelium Renewal
1. Can be fast?
2. Can be slow?
3. It will be renewed faster if...
4. can it be variable?
5. In stratified layers, where does mitosis occur?
6. Tumor of epithelial origin
7. Tumor of glandular epithelial origin

Back 34

1. Yes, intestinal epithelium and skin epithelium is replaced weekly.
2. yes, large glands renew slowly because they are not harmed by abrasion (pancreas, secretory saliva glands)
3. there is a lot of material running by it'
4. yes. some can readily replace itself, some cannot
5. At the basal layers
6. Carcinoma
7. adenocarcinoma

Front 35

Connective tissue is made of

(the tree)

Back 35

cells and extracellular matrix

extracellular matrix is made of:
fibers and ground substance

ground substance is made of:
proteins and sugars

Front 36

what is an example of ground substance in the intestine?

Back 36

The intestine has microvilli that have glycosylated sugars that bind water

Front 37

Cells attach to each other or ECM proteins using...

Back 37

Adhesion molecules

Front 38

Two kind of adhesion molecules:
1. homophilic

2. heterophilic

Back 38

1. like binding for two like molecules. Strong bonds that stay in place for a while
Ig superfamily
Cadherins (calcium dependent binding)

binding between two different molecules. Transient binding, short lived.
Selectins - molecules that bind to selectin receptors. HIghly carboxylated molecules

Integrins - bind to an assortment of molecules; usually found in cells that need to stay for a while, need stronger bonds (fibronectin)

Front 39

Homophilic example:
E-cadherin

Back 39

Help keep all the cells tightly attached together during embryogenesis

Front 40

Heterophilic example: diapedesis

(Transendothelial migration)

Back 40

WBCs must get out of blood stream to site of infection. WBCs travel through endothelial cells and attach to selectins, which SELECT the spot where the injury is
(usually occurs in venules)

Then integrins INTEGRATE the WBC out of the blood and into tissue. all this movement causes transient binding

Front 41

Homophilic example: synapse
1. what kind of structures keep neurons in place?

Back 41

1. cadherins and IgA superfamily, so that signals hit the exact right spot

Front 42

Cell Junctions
1. what are most junctions in epithelium?
2. tight junctions aka occluding junctions maintain...
3. desmosomes are
4. hemidesmosomes are desmosomes but instead of cell to cell, they are cell to...
5. All junctions are mediated by...

Back 42

1. Cadherins, because there is not much movement
2. polarity
3. nail spots
4. cell to matrix
5. cell adhesion molecules

Front 43

What are the main cell type laying out the ground substance?

Back 43

fibroblasts

Front 44

Ground substance
1. GAGs
2. Proteoglycans
3. Glycoprotein

Back 44

1. unbranched, very long, acidic polysaccharide chains. molecules include heparin sulfate, keratin sulfate, chondroitin sulfate, dermatan sulfate, hyaluronic acid

2. a bunch of GAGs around a protein core (mostly -glycan)
protein that has a glycosylation, made through the secretory pathway
ex: aggrecan - acts as a cushion, bery dynamic in nature, all of those sugar groups can interact with water

3. a protein that has a sugar on it

Front 45

Collagen
1. what makes most of the collagen types?
2. what kind of structure? density?
3. does irregular collagen bundles have irregular molecules?
4. Fibrillar (I, II, III, V, XI) - these are present in...
5. Fibril associated (IX, XII, XIV)
6. Which collagen type is anchoring fibrils?
7. Which collagen type forms the basement membrane?

Back 45

1. fibroblasts
2. triple helix, tightly packed
3. Newp. Collagen molecules are always ordered
4. bone, cartilage, dentin, tendons, organ capsules, dermis
5. got nothing
6. collagen 7
7. collagen 4

Front 46

Processing of Collagen
1. what pathway, and what kind of production

Back 46

1. secretory pathway, constitutive production (made without regulation)

Front 47

Processing collagen: Intracellular events
1. Hydroxylation of...
2. The above is essential for...
3. What cofactor does #1 require? What happens if you don't have this cofactor?
4. Besides #1, what else must be done?
5. Procollagen has what structure?
6. Is it already assembled in the ER?
7. In what form is it secreted? Which ary structure is this?
8. What organelle packages procollagen into secretory vesicles?

Back 47

1. prolines and lysines
2. forming the quaternary structure
3. Vitamin C, deficiency causes scurvy
4. glycosylate select residues
5. triple helix
6. Yes
7. triple helix form, which is quaternary structure
8. golgi apparatus

Front 48

Processing collagen:
Extracellular events

1. how to go from procollagen to collagen?
2. When can molecules be made into fibers?
3. Polymerization of collagen molecules into...

Back 48

1. cleave off non helical ends
2. once ends are cleaved off
3. collagen fibrils

Front 49

What are the three kinds of fibers?

Back 49

Collagen
Elastic
Reticular

Front 50

Elastic fibers
1. synthesis is from a promolecule that is...
2. Tropoelastin is synthesized in...
3. what two things form the fibers?
4. What gives Elastin it's elastic property?

Back 50

1. secreted and made into fibers
2. fibroblasts
3. elastin and fibrillin
4. fibrillin

Front 51

Reticular
1. Cells make fibers and then
2. What type of collagen is reticular fibers?
3. reticular fibers are enveloped by what?
4. The fibers are extracellular or intracellular?
5. What lymph nodes are made of
6. Reticular fibers are found within...

Back 51

1. Hold onto them
2. Collagen III
3. cytoplasm of reticular cells
4. extracellular
5. reticular fibers
6. sinus like spaces, provide structural support

Front 52

Functions of Connective Tissue:
1. Provide and maintain...
2. Also provides ...
3. Involved in ...

Back 52

1. shape in body
2. structural and metabolic support
3. defense, protection, storage of fat, tissue repair, immune reactions

Front 53

General features
1. What tissue layer origin?
2. does it contain blood and vasculature?
3. what are all held together by connective tissue?
4. consists of a diverse group of cells with a tissue specific...
5. forms a continuum with which tissues to maintain a functionally integrated body?

Back 53

1. mesoderm
2. Yes
3. epithelial, muscle, and nerve
4. extracellular matrix
5. epithelial, muscle, and nerve

Front 54

Classification of connective tissues:
'For embryonic connective tissues:

Back 54

Mesenchymal and mucous

Front 55

Connective tissue proper:
1. What is it?
2. Loose
3. Dense

Back 55

1. Involve loose or dense connective tissue
2. smaller, loose association of fibers
3. high density of fibers

Front 56

What are two kinds of dense connective tissue?

Back 56

regular or irregular

Front 57

Two kinds of dense regular tissue:

Back 57

collagenous
elastic

Front 58

Specialized connective tissue
1. Cartilage
2. Bone
3. Blood
4. Adipose

Back 58

1. chondrocytes and matrix
2. osteocytes and matrix
3. WBC + matrix
4. big ol fat globules everywhere

Front 59

What are the resident cells?

Back 59

fibroblasts
chondrocytes
osteocytes
chondroblasts
osteoblasts

Front 60

why do they call them resident cells?

Back 60

No idea

Front 61

If the cell is a -blast, it is

if the cell is a -cyte, it is

Back 61

immature

mature

Front 62

Where are resident cells from?

Back 62

The mesenchyme!

Front 63

Accessory cells
1. What are they for?
2. what is their LINEAGE?

Back 63

1. defense and protection. Mostly immune cells (mast cells, plasma cells, macrophages)

2. from hematopoietic cells

Front 64

loose connective tissue
1. what is always going to be in connective tissue?
2. Elastic fibers are more specific and are found in these places:

Back 64

1. collagen

2. dermis of the skin, oral cavity and esophagus, blood vessels, NOT around internal organs as much

Front 65

Cells of Connective Tissues
1. Resident cells
2. Transient cells
3. Everything in the body can be considered either...

Back 65

1. cells that we can find in most sections of CT, particularly loose and dense irregular, like fibroblasts, adipocytes, pericytes, mast cells, macrophages, stem cells

2. white blood cells: leukocytes, neutrophils live in the bloodstream for a day or two before they leave and roam around.
Regions under some kind of attack

3. cell or matrix

Front 66

Fibroblasts
1. is this the major cell of the connective tissue?
2. What does it synthesize?
3. All of the material in number 2 has gone through what to get into the extracellular space?
4. how often do they divide when they are in a safe and secure location?
5. Activity of fibrocyte and fibroblast?

Back 66

1. YES
2. ECM fibers (collagen, elastic, reticular fibers) and ground substance
3. the secretory pathway
4. Not often, usually divide when damage occurs. Divide more often beneath epithelium layers
5. fibrocyte - dormant
fibroblast - secreting lots of material

Front 67

Adipocytes
1. Can they be found both individually and grouped together?
2. what happens to the nucleus if the adipocyte is too full?
3. what is the general shape?
4. What are they used for?

Back 67

1. yes, both
2. it is pushed to the periphery
3. rounded
4. energy storage, insulation, cushioning, release of hormones

Front 68

Hormones used in short term weight control
1. Ghrelin
2. Peptide YY

Back 68

1. Increases appetite
2. induces a feeling of fullness

Front 69

Hormones involved in long term weight control
1. Leptin
produced by, function
2. Insulin

Back 69

1. adipocytes, decrease appetite (some obese people appear to be resilient, high levels of leptin)
2. induces adipocytes to convert glucose to triglycerides

Front 70

Is the lipid mass membrane bound?

Back 70

No

Front 71

Brown fat cells:
1. Where is more found, babies or adults?
2. What kind of animal uses this?
3. Can people adapt to have more brown fat cells?

Back 71

1. BAbies!
2. hibernating animals
3. yes

Front 72

how are free fatty acids and glycerols released from bloodstream made into triglycerides by adipose?

Back 72

ADIPOCYTESSSS

Front 73

Is there heavy vasculature around adipocytes?

Back 73

Yes.

Front 74

Mast Cells
1. Where do they develop?
2. They are large cells, have cytoplasm filled with purple staining granule containing:
3. What kind of receptors does this cell type of?
4. Is degranulation regulated?

Back 74

1. Bone marrow
2. Heparins and Histamines
Heparin - blood thinning agent (anticoagulant) so blood can move quickly and get contents through to a wound
Histamine - promotes permeability of blood vessel, allows cells through like white blood cells
Chemotactic factors that rally troops
Leukotrienes, prostaglandins, growth factors, etc
3. IgE receptors - involved in hypersensitivity reactions, which is why you take antihistamines to break degranulation cycles
4. yes. Waits for the signal to release instead of releasing all the time
signal is antibody-Ag
activates adenylate cyclase to produce cAMP to activate pKA to phosphorylate something else to cause fusion of the granule. this happens supa fast

Front 75

Pericytes
1. what kind of cell are they, divide wise?
2. supports what?

Back 75

1. pluripotent - can modify as needed
2. at capillaries, smooth muscle is absent to allow diffusion through endothelium, pericytes support here by morphing into smooth muscle or endothelium if damage occurs

mostly around post capillary venules

Front 76

Macrophages
1. resident or recruited?
2. Derived from what?
3. cleans up...

Back 76

1. BOTH
2. monocytes. monocytes in the blood, once out of the blood, they are macrophages
3. debris in the cell

Front 77

Specialized macrophages
1. Liver
2. Lungs
3. Epidermis
4. Bone
5. CNS

Back 77

1. Kupffer cells - pick up junk during influx of fluid that is filtered through the liver
2. dust cells
3. Langerhans cells
4. osteoclast
5. microglia

Front 78

Plasma cells
1. what do these cells secrete
2. where are they derived from?
3. what's a normal day like for a plasma cell?
4. unique appearance?

Back 78

1. antibodies
2. B lymphocytes. B and T lymphocytes are both involved in adaptive immune response
3. travel through the blood, find bacteria, secrete antibodies
4. clock face

Front 79

Movement of fluid
1. this kind of pressure pushes fluid out of capillary
2. This kind of pressure pulls fluid back in
3. What is circulated through those beds by this pressure?
4. what picks up leftover fluid?
5. The fluid moves out of the capillaries to build up in tissue during what?

Back 79

1. hydrostatic pressure
2. osmotic pressure
3. nutrients
4. lymphatic capillaries
5. inflammation

Front 80

Atherosclerosis...what is it?

Back 80

build up of CT and lipids in blood vessels, called plaques

Front 81

diabetes...what happens to basement membrane?

Back 81

it thickens, impacting nutrient delivery

Front 82

Cancer
1. how does it metastasize?
2. what do they act like to do their job?

Back 82

1. by moving through the CT
2. WBCs. they move through the CT and into the bloodstream and are carried off to other sites

Front 83

Fibrosis
1. Build up of what kind of fibers?
2. What is an example of this in the liver?
3. what is the impact on blood flow?
4. what does it to the lung?

Back 83

1. CT fibers
2. cirrhosis
3. slows it down
4. impairs air flow

Front 84

Emphysema
1. degradation of what kind of fibers?
2. What does this do to the volume of air in the lungs

Back 84

1. Elastic
2. decreases it

Front 85

ENZYME KINETICS

Back 85

SUPER DUPER FUN TIME!!

Front 86

active site of an enzyme:
1. where is it in relation to the enzyme?
2. what shape is it?
3. where is it in relation to the enzyme, more specifically?
4. If there are two active sites, how are they arranged

Back 86

1. WITHIN THE ENZYME
2. shaped to fit the substrate
3. on the surface. so, within enzyme, but on the surface, so that substrate can come and go quickly
4. close enough to easily share electrons

Front 87

Mechanism of catalysis
1. reactants have higher or lower energy than products?
2. what does enzyme lower, and what does this do?

Back 87

1. higher energy
2. activation energy, speeding the reaction up

Front 88

Active site is accessible to both...

Back 88

reactants and products

Front 89

Single Substrate reactions
1. What is Vo?
2. What does the michaelis menten equation describe?

Back 89

1. initial rate of reaction. slope of the line in the progress curve graph.
2. the slope (Vo) varies with substrate concentration

Front 90

Which enzyme reactions are reversible?

Back 90

ALL OF THEM

Front 91

When substrate concentrate becomes too high, the reaction...

Back 91

slows down

Front 92

The rate of increase of product over time is equal to...

Back 92

Ks times the concentration of S

Front 93

Rate of decrease of substrate over time is equal to

Back 93

Kp times concentration of P

Front 94

With a low substrate concentration, activity increases...

Back 94

linearly

Front 95

If substrate concentration is too high, what is the increase in activity?

Back 95

very little increase. [S] becomes saturated at too high of a concentration. this is because all enzyme active sites are occupied.

Front 96

Do you ever really reach Vmax?

Km equals...

Back 96

No, thou must estimate

1/2Vmax. so Km is the substrate concentration at which the reaction rate is half of its full value

Front 97

Mechanism for an enzyme reaction
1. Reaction of E and S forming ES is known as what? reversible or not?

2. Reaction of ES going to E and P is known as what? reversible or not? what is the rate constant?

Back 97

1. Substrate binding reaction, reversible, k1 and k-1

2. catalytic step, irreversible, k2

Front 98

Vo depends on what, according to michaelis menten equatoin?

Back 98

position of the substrate binding equlibrium and the rate constant k2

Front 99

Km is equal to the...(constants)

Back 99

sum of dissociation rate constants, k1 and k-1, divided by association rate constant, k2

Front 100

flashcards suck for enzyme kinetics, we are moving to carbohydrate chemistry

Back 100

that's right

Hint 100

stop flipping this card

Front 101

Saccharides
1. what makes the earth green? what makes the ocean blue?
2. how much cellulose is being produced per year on land?
3. How much cellulose is being produced per year in the sea?
4. what is the most abundant biomolecule on the planet, and most important for energy transfer and storage?
5. Every molecule is made from basic building blocks based on...

Back 101

1. CARBOHYDRAAAATES
2. 10 to the 15 kg
3. 10 to the 14 kg
4. CARBOHYDRAAAATES
5. CARBOHYDRAAAATES

Front 102

What is the oldest biomolecule?

Back 102

CARBOHYDRAAAAAATES

Front 103

Organisms that burn oxygen for aerobic oxidation burn what to get energy?

Back 103

CARBOHYDRAAAAAATES

Front 104

Stanley Miller experiment: he did something amazing, explain it

Back 104

threw ammonia, methane, hydrogen, and water together, boiled it and shocked it with electricity. It made 11 of 20 amino acids (maybe more) and something else formed...

CARBOHYDRAAAAATES

Front 105

the important role of glucose in the origin of life:

Back 105

Monosaccharides are aldehydes or ketones and therefore very reactive and can provide scaffolds for other modifications and larger molecules

The first living organism wasn't based on amino acids or lipids, it was based on sugars.

simple RNA molecules can have catalytic properties and can actually catalyze formation of other RNA molecules

Unlikely that RNA was made in oceans

something about a self supporting catalytic web, at some point it becomes sufficient and has ability to replicate all of the constituents of the group

saccharides probably played a key role in this

Front 106

Where do most monosaccharides come from?

Back 106

photosynthesis (gluconeogenesis)

Front 107

Sugars and polysaccharides:
Play a key role in:

Back 107

Cell and organism structure
energy storage, transfer, and metabolism
providing scaffold for genetic information
regulation of protein folding, structure, homing
stability, function, interactions with other molecules
Cell to cell interactions
Tissue morphogenesis

Front 108

How much ATP is synthesized by a person in a day?

Back 108

80kg

you synthesize and break down your body weight in ATP per day

Front 109

Disaccharides
what do they provide?

Back 109

energy for biological processes

Front 110

Kinds of Sugars:
1. Monosaccharides
2. Disaccharides
3. Oligosaccharides
4. Polysaccharides

Back 110

1. A simple sugar that can not be hydrolyzed into simpler saccharide moieties
2. two simple sugar moieties
provide energy for biological processes
3. compounds that contain <= 8 monosaccharides
Often associated with glycoproteins or glycolipids
4. Polymers of > 8 monosaccharides
structural function (cellulose, chitin)
energy storage (starch, glycogen)

Front 111

Classifying on the number of Carbons:

Back 111

triose (3 cs)
tetrose(4 cs)
pentose (5 cs)
hexose (6 cs)

Front 112

Two examples of trioses

Back 112

glyceraldehyde (aldose) , dihydroxyacetone (ketose)

Front 113

Saccharides have the ability to form...

how is this possible?

Back 113

Stereoisomers!

Compounds with the same molecular formula and order of attachment of atoms but with different arrangement of these atoms in space

due to the carbon being chiral

Front 114

How does isomerism play a part in inhibition

Back 114

if a receptor is designed fo ra particular stereoisomer, the other configuration can actually bind to it and serve as an inhibitor

Front 115

The number of stereoisomers for a given sugar is dependent on...

Back 115

the number of carbons

Aldoses, stereoisomers = 2 to the n-2

ketoses, stereoisomers = 2 to the n - 3

Front 116

how do optics play a part in chiral molecules?

Back 116

if you shine plane polarized light, the light rotates depending on configuration

you use a polarimeter to measure this

Front 117

What does the d and l determination refer to?

Back 117

The configuration of the furthest asymmetric carbon from the carbonyl group on the sugar

Front 118

WHICH DETERMINATION OCCURS IN NAURE?

Back 118

D

D-SUGAR YALL

Front 119

How do simple sugar cyclize?

glucose's six member ring is similar to pyran so it is referred to as

fructose's five ring formed is similar to furan so it is referred to as

Back 119

carbonyl group interacts with hydroxyl group to form hemiacetals and hemiketals

glucopyranose

fructofuranose

Front 120

Anomers
1. What is it
2. What position is oxygen in in B anomer position

3. What position is oxygen in A anomer position

Back 120

1. a diastereomer that differs in the position of the alpha hydroxyl group

2. UP

3. DOWN

Front 121

Which anomer is preferred in nature?

What is mutarotation?

Back 121

B-D-Glucose is preferred by 63%

It is the slow change of the optical activity of a solution to represent the middle ground between the two different configurations

Front 122

Configurations

Chair vs Boat

1. Which one is favorable energetically?
2. What is the position of the larger groups in chair?

Back 122

1. CHAIR

2. equatorial. glucose can switch chairs to make this happen

Front 123

The saccharides bearing anomeric carbon atoms not forming a glycosidic bond are termed...

Back 123

reducing sugars

Front 124

Sugar based acids like ascorbic acid esterify to form...

Back 124

lactones

Front 125

Reducing aldoses and ketoses form

Back 125

acyclic monosaccharide alcohol alditols

D xylitol (sweet n low) is an example of this

Front 126

Malliard Reaction

Back 126

non enzymatic browning. An amino acid and reducing sugar react induced by heat

carbonyl group of sugar interacts with nucleophilic amino group of amino acid

changes the flavor and smell of the food

Front 127

Deoxy sugars
1. OH is substituted with...

Back 127

H

hydroxyl on C-2 is replaced by H generating B-D-2-deoxyribose, this is important for DNA synthesis

Front 128

Amino sugars
OH substituted with

Back 128

acetylated amino group

B-D-glucosamine

Front 129

Phosphorylated sugars
1. important for the generation of
2. they are anionic and have electrostatic interactions with
3. retain...
4. important reactive intermediates for...

Back 129

1. ATP
2. proteins
3. sugar in cells
4. O and N glycosylation

Front 130

which organs of the body can release glucose into circulation?

why?

Back 130

Liver and kidneys

Only those cells have enough phosphatase to take the phosphate off the glucose. Glucose can move through the membrane, but phosphorylated glucose can't

Front 131

Glycosidic bonds
1. what is it?
2. what are held together by these bonds?
3. Most famous disaccharide is what?
what are the monomers?
what type of glycosidic bond is it held together by?
4. Can glycosidic bonded carbons decyclize? Are they reducing sugars?
5. What is a byproduct of starch and is a dissacharide that is also a reducting sugar?
6. What makes up lactose?

Back 131

1. anomeric hydroxyl of a sugar condenses with alcohols to form glycosidic bonds
2. disaccharides and polysaccharides
3. sucrose, made of gluctose and fructose. O-glycosidic bond between carbon 1 of glucose and carbon 2 of fructose
4. No, and no
5. Maltose, made of glucose+glucose, IS a reducing sugar
6. glucose + galactose

Front 132

Lactose intolerance
1. Absense of what?
2. What then happens to lactose?

Back 132

1. Lactase
2. doesn't break down, travels down to the colon, bacteria switch to lactose metabolism and produce excess gas, causes abdominal pain, flatulence, diarrhea, and acid reflux

Front 133

What group has high levels of lactate?

What group has high incidience of lactose intolerance?

Back 133

infants

african americans and asians

Front 134

Polysaccharide glycans
1. Homopolysaccharide
2. examples

Back 134

1. a polysaccharide with only one kind of monomer, repeating
2. glucans (glucose polymer)
galactans (galactose polymer)

Front 135

heteropolysaccharides

can be linear or...

ends of polysaccharide: are they identical?

Back 135

have many different kinds of units for monomers

branched

No. reducing end = free anomeric carbon.
nonreducing end = anomeric carbon is linked to the next unit
if polysaccharide is branching, it will hav emore than one non reducing end

Front 136

three examples of polysaccharides

Back 136

starch
glycogen
cellulose

Front 137

Cellulose
1. chain of what monosaccharide?
2. how many units per chain?
3. what does this polysaccharide support?
4. Linked together by what?
5. Can people break down cellulose? Can herbivores?

Back 137

1. glucose
2. 15000
3. huge osmotic pressures and immense loads
4. B(1-->4) linkages
beta makes a big difference. each following glucose will be turned around 180 degrees. Hydrogen bonds are formed between the chains of cellulose, also connect to other sheets of molecules. gives form and strength
5. NOoooo, ...yes

Front 138

Chitin
1. type of linkage?
2. type of polymer?
3. hwo much is produced annually?

Back 138

1. Beta 1 4
2. homopolymer
3. 10 to the 14th

Front 139

What is a reducing sugar?

what is a non reducing sugar?

Back 139

any sugar that has the anomeric carbon free

a sugar that does not have a free anomeric carbon, for example, sucrose is turned around and it's anomeric carbon is wrapped up in a glycosidic bond

Front 140

If polysaccharide is branching, will it have more than one non reducing end?

Back 140

Yes

Front 141

What kind of bonds are formed between chains of cellulose?

Back 141

hydrogen bonds.
This is what gives it strength.

Hint 141

http://www.mansfield.ohio-state.edu/~sabedon/051cellu.gif

structure of cellulose

Front 142

Chitin

what is its character linkage?

Back 142

B (1-4) linkage

Front 143

Starch:
1. what is it?
2. insoluble granules of starch are composed of...

Back 143

1. a mixture of glucans made by plants as main food reserves
2. a-amylose and amylopectin

Front 144

A-amylose
1. what kind of linkage?
2. almost identical to what polysaccharide, except...
3. what difference does #2 make?

Back 144

1. alpha 1,4 linkage
2. cellulose, except you have alpha rather than beta linkage.
3. makes huge difference. cellulose is a complex, rigid structure. A-amylose is a helically coiled conformation; not rigid, soluble, easily hydrolyzed. important for any storage molecule because it should be easy to cut

Front 145

Amylopectin
1. long chains of...
2. composed of what kind of bonds?
3. every 24-30 residues there is what kind of linkage? what does this allow?
4. glycosidic bonds have to occur with anomeric carbon but hydroxyl can come from...
5. How many glucose residues per molecule?
6. What is advantage of amylopectin?

Back 145

1. a-amylose
2. a (1,4) bonds
3. a (1,6) linkage, allows molecules to branch to other directions
4. any carbon of the sugar
5. up to 1 million
6. enzyme has many surfaces to begin cutting rather than two, making mobilization faster

Front 146

Glycogen
1. storage polysaccharide in...
2. most prevalent in...
3. first 10 seconds of running are from ATP and creatine. After that it's all about some
4. structure similar to amylopectin, except it is more branched, having branches every how many residues?

Back 146

1. animals
2. liver and skeletal muscle
3. glycogen reserves
4. 8-12 residues

Front 147

1. Glycogenolysis
2. What does glycogenolysis release?
3. What is energy cost of storing glucose as glycogen?

Back 147

1. the breakdown of glycogen into free glucose molecules
2. glucose 1 phosphate
3. HIIIGH

Front 148

Why not store free glucose? Why invest energy instead of storing energy?

Back 148

The reason is osmotic pressure. If you have phosphorylated free molecules, it creates enormous osmotic pressure. there would be an influx of water into the cell, and it would burst

STILL takes a lot of water to store glucose as glycogen

Front 149

In the very first days of dieting on the zero carb plan, what exactly are you losing?

Back 149

You are losing water!

Glycogen is broken down in liver and muscle. Glycogen has a lot of water, and when we burn glycogen, we lose water and it's weight.

When you start eating carbs again, you will store glycogen, and therefore water, and gain that weight back.

Front 150

Glycosaminoglycans
1. Unbranched polysaccharides of alternating [what] resides?
2. what are the properties of solutions with GAGs in them?
3. where are these present?
4. Help to make up gel like mixture called...
5. Examples of GAGs

Back 150

1. uronic acid and hexosamine
2. high viscocity and elasticity
3. extracellular spaces comprising connective tissue
4. ground substance
5. Chondroitin - in cartilage
hyaluronic acid - in synovial fluid and vitreous humor the eye
dermatan sulfate - in skin
heparin - inhibits blood clots

Front 151

Hyaluronic acid
1. what charge is it? what does it bind?
2. what do anionic groups do?
3. occupied volume compared to dry state?
4. An excellent biological what?
5. What does it do all special like in tissue?
6. composed of repeating units of...

Back 151

1. anionic. Binds cations like K+, Na+, Ca++
2. repel it. makes it rigid and highly hydrated
3. occupied volume is ~1000 times larger than in dry state
4. shock absorber and lubricant
5. tissue repair! particularly in the skin
6. glucoronic acid, glycosaminoglycan

Front 152

HYAFF
1. what the hell is this?
2. utilized as a scaffold to...
3. can be implanted in the skin so cells are allowed to reach the wound bed through...

Back 152

1. semisynthetic derivative of hyaluronic acid
2. grow skin cells in the lab
3. microperforations to regenerate the epidermis

Front 153

Knee injection
1. Hyaluronic acid knee injections replenish what in the knee joint?
2. Acts as a natural what?

Back 153

1. Acids
2. natural cartilage by creating a shock absorber between bones

Front 154

Heparin
1. What kind of cells do they hang out in?
2. This has a very special charge. describe it.
3. Prevents clotting of blood by binding to...
4. Murderer interest

Back 154

1. Mast cells. Heparin is in intracellular granules of mast cells that line arterial walls.
2. MOST NEGATIVELY CHARGED BIOLOGICAL POLYMER KNOWN TO MAN
3. antithrombin III, thereby inhibiting fibrin formation
4. can kill people with it, without detection. it all gets degraded

Front 155

Glycoprotein
1. general protein sugar relation
2. What is the most abundant post translational modification?
3. Almost all secreted and membrane associated proteins are...
4. Important in sorting and distributing proteins to proper...

Back 155

1. BIG OLLLLLE PROTEIN....with a lil sugar on it
2. glycosylation
3. glycosylated!
4. cellular destination

Front 156

Microheterogeneity
1. describes...
2. sugar chains are heavily regulated by
3. Random?
4. Is a glycosylation spot on a protein glycosylated, necessarily?
5. glycosylation of proteins is important for...

Back 156

1. variations in glycoproteins
2. enzymes and covalently linked to polypeptide backbone.
3. NO! Very specific
4. no, it doesn't have to be
5. folding, function, destination - both intracellularly and within the body

Front 157

How do oligossaccharides bind to protein?

Back 157

By an N linkage to the amide nitrogen of Asn

By an O linkage to the oxygen of Ser/Thr

Front 158

Glycoprotein structure:
1. N linked glycosylation occurs co transiently in the ER by enzymes and must have the sequence...
2. when does N glycosylation occur?
3. N glycosylation plays a role in protein *, physical *, bio*, rate of *, new functionalities and spec*
4. is O glycosylation more or less specific?

Back 158

1. Asn - x - Ser/Thr
2. co translationally (during protein synthesis)
3. folding, stability, activity, clearance, ificities
4. much less specific than N glycosylation

Front 159

Oligosaccharides
1. typically where on the molecule?
2. do they ever go inside?
3. can move around like branches on a tree because they are...
4. what does an oligosaccharide shield do?
5. do prokaryotes glycosylate?
6. non glycosylated proteins have higher or lower activity? higher or lower stability?

Back 159

1. on the surface
2. hardly ever
3. attached to a single point
4. protects the molecule from interaction with proteases
5. Newp
6. higher activity, lower stability

Front 160

Proteoglycans
Function as what?

Back 160

Organizers of tissue morphology, selective filters, and regulators of activities

Front 161

Aggrecan
1. main proteoglycan component of what?
2. What does the structure look like?
3. How are proteoglycan subunits attached to a hyaluronic acid backbone?
4. How many aggrecan chains hang off an aggrecan?
5. Aggrecan gives cartilage what two properties?

Back 161

1. cartilage
2. bottlebrush
3. covalently
4. over a hundred
5. elasticity and resilience

Front 162

ABO blood group determinants
for each type, antigen and antibody:
1. Group A
2. Group B
3. Group AB
4. Group O


also, what about Rh factors?

Back 162

1. A Antigen (N-acetylgalactosamine) B antibody
2. B antigen (galactose) B antibody
3. Both A and B antigens, no antibodies
(universal accetors)
4. No antigens (no form of galactose) both antibodies

theres over 40 Rhesus factors.
Only one Rh

Front 163

Bacterial cell walls
1. Cell walls permit bacteria to survive in what?
2. Need to withstand what without bursting?
3. how is their incredible strong structure possible?
4. describe the two types of bacteria and their staining
5. Peptidoglycan structure and linkage

Back 163

1. hypotonic environments (water)
2. Super high osmotic pressures
3. polysaccharides in their cell walls
4. Gram positive - contains thick peptidoglycan cell wall, can take up gram stain
Gram negative - contains thin cell wall covered by a membrane. Stain cannot penetrate the lipids of the membrane. looks pink. SUPER PRETTY PINK GUYS YEAH
5. polysaccharides and polypeptides covalently linked. consists of alternating B (1-4) N acetylglucosoamine and N-acetylmuramic acid linked to a tetrapeptide

Front 164

Lysozyme'
1. enzyme present in...
2. Catalyzes the hydrolysis of what?
3. Would it kill gram positive bacteria? would it kill gram negative bacteria?

Back 164

1. tears, mucous, bodily secretions
2. B (1-4) glycosidic linkages
3. Yes, it would kill gram positive bacteria. Not gram negative bacteria because it would not penetrate the lipid layer

Front 165

Penicillin
1. Binds and inactivates enzymes that
2. prevents the new synthesis of...
3. because cell wall expansion requires partial cell wall degradation, penicillin causes
4. Who discovered both lysozyme and penicillin?
5. These discoveries led to

Back 165

1. crosslink peptidoglycan strands of cell wall
2. peptidoglycan
3. cell lysis
4. fleming
5. vaccines and antibiotics

Front 166

Pneumococcal polysaccharides
1. What is the bacteria we bouts to talk about
2. how many annual deaths\
3. More than 90 different serotypes of this bacteria, each withs IT OWN

Back 166

1. streptococcus pneumoniae, a common inhabitant of the upper respiratory tract of humans
2. 1.2 million, 40% in children
3. unique capsular polysaccharide

Front 167

Pneumococcal vaccines
1. unconjugated vaccines
2. conjugated vaccines
3. how do polysaccharides play a part?

Back 167

1. just the vaccine, with nothing coupled to it. Not very immunogenic. doesn't elicit an immune response
2. coupled to a highly antigenic protein such as Diphtheria protein
3. there are 13 polysaccharides included in the most recent polyvalent vaccine. so, vaccine attempting to tackle problem of different serotypes of streptococcus pneumoniae

Front 168

Lipopolysacharides
1. pyrogen

Back 168

a fever inducing substance. Lipopolysaccharides are an example

Front 169

When LPS gets into the blood, it:

Back 169

Induces fever
mediates septic shock
induces cytokine storm
activates complement and clotting cascade
acts as a B cell mitogen, causing activation on non specfic B cells to make many antibodies
these functions lead to cell death

Front 170

Is it sufficient for drugs and medical instruments to be sterile?

Back 170

NO they must also be pyrogen free

Front 171

Detection of endotoxin
1. endotoxin in synonymous with
2. LAL assay

Back 171

1. LPS
2. assay used to dtect endotoxin associated with gram negative bacteria.
the lysate is prepared from the circulating amebocytes of the horseshoe crab
LAL clots in the presence of endotoxin

Front 172

Dr Youngs Lectures:
Metabolism

Back 172

11 hours worth, get ready

Front 173

When do we see metabolic problems in patients?

Back 173

When regulation of metabolism goes wrong. Regulation is key.

Front 174

Two definitions of homeostasis:
1. The classic, less preferred
2. Dr. Young's special def

Back 174

1. maintenance of a constant internal environment

2. Maintenance of biological processes within a physiological range in response to variations in our environment

Front 175

Two components of Whole body homeostasis

Cellular homeostasis

Back 175

maintain a constant level of fuel in the blood

maintain constant level of energetic status in the cell

Front 176

Why is metabolic homeostasis important?

Back 176

Because problems in metabolism result in a wide range of diseases

scientists genetically knock out pathways of interest to study their importance

Front 177

Naturally occuring inborn errors of metabolism
1. definition
2. PKU
3. McArdle's disease
4. LPL deficiency
5. Fructose intolerance
6. VLCAD deficiency

Back 177

1. mutations in critical proteins in metabolic pathways that create a block and leads to genetic diseases

2. Phenylketonuria - mutation of amino acid metabolism. One of the most common IEM. routinely screened during pregnancies. Caught early = modified diet = prevent neurodegenerative effects

3. problem with glycogen metabolism that leads to decrease in exercise tolerance

4. deficiency in a lipase that is important in removing lipids from blood

5. problem in fructose metabolism that leads to liver failure

6. VLCAD deficiency - enzyme involved in oxidation of fatty acids, mutation within the beta oxidation pathway of fatty acids

Front 178

Gene Environment Interactions
1. Definition
2. Obesity
3. Diabetes Mellitus
4. Atherosclerosis
5. Dyslipidermia
6. Heart disease

Back 178

1. More common than inborn errors. Genetic predisposition + environment causes disease
2. over 2/3rd of the US is obese. WOW. multiple genes involved, but really?? genes? where were all the fat people 100 years ago? is this .0001x genes + 10000x environment?
3. type I and type II are common metabolic disorders
4. leads to myocardial infarction, stroke, and death
5. Non alcoholic hepatic steatosis - lipid accumulation in liver leads to liver dysfunction
6. also considered a metabolic disease

Front 179

What are normal glucose numbers:
1. Normal
2. hypoglycemic
3. hyperglycemic

Back 179

1. between 80 and 120 mg/dl
2. below 80
3. above 120

Front 180

Normal range of fatty acids

Back 180

150-500 mg/dl

huge range because it depends on fasting or fed state

Front 181

normal range for amino acids

Back 181

around 35 mg/dl approx
abundance varies

Front 182

Energy store importance
1. The number 1 most important
2. Number 2 most important
3. Number 3

Back 182

1. Lipids
2. Proteins
3. Carbs (weird, huh) mostly bc in relation to lipids, the amount stored isn't nearly as much

Front 183

General overview of Metabolic pathways
1. definition
2. some metabolic pathways occur in cytosol of cell and go like
3. some metabolic pathways involve enyzmes that come together via non covalent or covalent associations and form complexes; pathway performed only in certain location in cell
4. there can be a single polypeptide chain with multiple enzyme activities
5. reactions can occur within a single compartment of a cell or across the cell membrane, can involve integral membrane proteins

Back 183

1. series of enzyme catalyzed reactions wehre product of one rxn is substrate of the next rxn
2. substrate, intermediate, intermediate, product
3. glycogen metabolism
4. fatty acid synthase
5. ETC

Front 184

Anabolic pathways
1. what does it require?
2. when is it favored?

Back 184

1. ATP and reducing equivalents (like NADPH which is oxidized and reduces things around it, donating its electrons)

Front 185

Catabolic pathways
1. What does it do?
2. What does it yield?
3. When is it favored?

Back 185

1. breaks shit down by oxidative degradation, makes small molecules like water, cO2, ammonia
2. ATP and reducing equivalents like NADH and FADH2
3. Activity and fasting

Front 186

How is the overlap of catabolic and anabolic pathways important?

Back 186

switching on/off of certain pathways is very important in regulatin of metabolism

Front 187

Generation of NADH in Catabolic Pathways:
1. substrates of catabolism (proteins, carbs, lipds) are good sources of chemical energy because
2. NADH is highly reduced, a good source of ___
3. Oxidation is stripping away...
4. What is utilized in anabolic reactions instead of NADH?

Back 187

1. their carbon is reduced
2. hydride ions, which is a proton with two electrons
3. electrons and taking a proton with them
4. NADPH

Front 188

Oxidation:
1. NAD+ accepts the hydride ion to form NADH and passes on electrons to...
2. What must be regenerated for oxidative metabolism to continue (important)
3. Regeneration is accomplished by passing
4. WHAT IS THE FINAL ACCEPTOR?

Back 188

1, subsequent acceptors
2. NAD+
3. reducing equivalents on to other acceptors
4. OXYGEN. it forms water, regenerates NAD+

Front 189

What is the critical goal of metabolism?

Back 189

Re synthesizing ATP through catabolic rxns

Front 190

What kind of pathways maintain ATP levels

Back 190

catabolic pathways

Front 191

Two kinds of ATP synthesis

tell us a bit about the second one

Back 191

substrate level

oxidative phosphorylation
This is the primary mechanism of ATP synthesis. It couples substrate level oxidation with ATP generation through the proton motive force, this energy is harnessed to make ATP

Front 192

Substrate level phosphoration
1. to make atp, what should you do with phosphorylated substrate?
2. what should you do with two ADPs?

Back 192

1. take off phosphate, add in adp, it makes atp
2. This is the adenylate kinase rxn.
rip off phosphate group from one adp to place on another adp, results in amp and atp
resynthesizes 1 atp for every 2 adps and makes amp that stimulates catabolism, so that then you can make even more atp through oxidative phosphorylation

previously named myokinase bc of its abundance in muscle to maintain energy charge through contraction. much adp made during muscular contraction

increases turnover with no net utilization of atp during muscle contraction

Front 193

the importance of AMP
1. essential
2. indicates high rate of ATP utilization and that cell needs to make more ATP by...
3. the two ways AMP works

Back 193

1. signaling molecule
2. increasing metabolism
3. allosterically binding to and activating enzymes involved in catabolic rxns
activates AMP kinase to inititiate catabolic rxns

Front 194

Maintaining ATP levels during a marathon

10g of ATP is utilized each second during a marathon. Muscle contains on average 60g of ATP. How are we able to run marathons?

Back 194

Continuous ATP regeneration

increase rate of ATP catabolism to match rate of ATP anabolism

Front 195

What is the golden rule of regulation?

Back 195

Those enzyme catalyzed rxns that are thermodynamically favorable in one direction only in the cell are often important sites of regulation

Front 196

as far as delta G is concerned, a large number or small number means its highly favored in a direction

Back 196

A large number

Front 197

Regular Regulation Metabolism:
Altering Substrate Availability
1. General rule:

2. Coupling the reaction

3. Compartmentalization

Back 197

1. Enzyme catalyzed reactions are substrate dependent. More substrate means faster reaction

2. couple reaction to another pathway. Ex: glycogen breakdown provides substrate for glycolysis

3. Getting substrates into the cell or across compartments within the cell by specific transporters.

if you regulate transporter, you regulate substrate availability. like glucose transport

regualte entry, regulate pathway. like, fatty acyl metabolism, this is most crucial step in beta oxidation

Front 198

Regular Regulation Metabolism:
Change enzyme activity
1. Allosteric regulation

2. Reversible Covalent Modification

3. Expression / Absolute levels of an enzyme

Back 198

1. reversible, non covalent binding of an effector to enzyme at site different from active site (ex: phosphofructokinase, AMP)

2. covalently bonding of group to enzyme that changes enzyme's activity. example: phosphorylation

protein kinase A - slaps on phosphate groups

protein phosphatase - removes a phosphate group from a protein (serine, threonine, or tyrosine residues)

does phosphorylating always activate? no sometimes it inhibits

3. ex: synthesis of ketone bodies in the liver, enzyme glucokinase for this rxn is expressed only in the liver.

pathways switched on and off by expressing / repressing certain genes.

Front 199

Can enyzmes themselves be turned on or off like a switch?

Back 199

No. Either increasing or decreasing their activity accomplishes this turning off and turning on

Front 200

Intracellular Regulation
1. Energy Charge
2. Oxidation / Reduction status
3. Metabolite / Carbon Availability
4. The importance of these signals can depend on the

Back 200

1. ATP ADP AMP. AMP is a nice signaling molecule which indicates energy change is low in the cell which stimulates catabolism

2. NAD+/NADH, FAD/FADH2
shift form to more reduced state to stay within physiological range
3. Metabolite/Carbon availability
acetyl CoA, malonyl CoA, citrate. all three of these are good carbon sensors

4. tissue!
liver is sensitive to carbon availability through nutrients (through hepatic portal vein)
skeletal muscle can go from resting to intense work, sensitive to redox

Front 201

Extracellular regulation
1. what kind of factors can signal distinct states?
2. Anabolic signals
3. Catabolic signals
4. Vitamins and cofactors

Back 201

1. neurohumoral
2. insulin
3. glucagon, norepinephrine, epinephrine, cortisol
cortisol does not require a second messenger
4. ahhh yeee

Front 202

GLYCOLYSIS

Back 202

BREAK DOWN GLUCOSE

Front 203

Key regulatory steps:
1. hexokinase
2. phosphofructokinase
3. pyruvate kinase

Back 203

1. glucose --> glucose 6 phosphate, or g6p

2. fructose 6 phosphate --> fructose 1,6 bisphosphate

3. PEP to pyruvate

Front 204

What is glucokinase?

Back 204

hexokinase of the leeever

Front 205

Hexokinase regulation:
1. substrate availability
2. Glucose transporters
3. Enzyme activity:
allosteric
reversible covalent
level of expression
4. Regulation of reciprocal pathway

Back 205

1. glucose is the substrate
2. GLUT2 and glucokinase are glucose sensors
3. allosteric - inhibited by end product g6p
level of expression - induced by insulin
4. glucokinase and g6p

Front 206

WHAT IS THE MOST IMPORTANT REGULATION STEP IN GLYCOLYSIS?

Back 206

IT'S PHOSPHOFRUCTOKINASE, EVERYBODY SO GET READY

Front 207

phosphofructokinase regulation:
1. wait, why is it the most important?
2. substrate availability
3. Enzyme
allosteric (inhibited/activated)
reciprocal regulated

Back 207

1. this dictates flux through pathway
2. f6p
3. PRIMARILY REGULATED ALLOSTERICALLY
inhibited - ATP ( too much atp) Citrate (signals that glycolysis is too fast)
Activated - AMP (activates glycolysis)
fructose 2,6 bisphosphate (not a glycolytic intermediate) acts as a signal to say there's a lot of carbon to speed up glycolysis
4. reciprocal regulated - couples with fructose 1,6 bisphosphatases from gluconeogenesis

Front 208

Pyruvate Kinase regulation
1. what is the liver isozyme regulated by?
What is the muscle isozyme regulated by?
2. wait, what's an isozyme?
3. substrate regulation
4. Enzyme activity
Inhibited
Activated
5. Reversible covalent modification
6. Reciprocal enzymes

Back 208

1. phosphorylation
not phosphorylation
2. ees like an enzyme that catalyzes the same reaction but differs in amino acid compozeeeeshin
3. PEP is the substrate
4. Inhibited - ATP, Acetyl CoA (similar to citrate effect) alanine (similar to citrate effect)
Activated - AMP, F1,6BisP

Front 209

regulation of pyruvate kinase by reversible covalent interaction

Back 209

phosphorylate the liver isozyme - inhibit it

Front 210

CITRIC ACID CYCLE

Back 210

OR TRICARBOXYLICACID CYCLE

Front 211

First step of regulation:

Back 211

Citrate Synthase catalyzed reaction of
Oxaloacetate + Acetyl CoA --> citrate + CoA

Front 212

Citrate synthase reaction:
1. catalyzes what kind of reaction?
2. substrate availability

Back 212

1. a condensation reaction
2. limited by acetyl coA and oxaloacetate

Front 213

Pyruvate dehydrogenase
1. Uses what to make acetyl CoA
2. Decarboxylation of pyruvate does what?
3. Is this enzyme a complex? How many subunits? what 3 critical cofactors?
4. Allosteric inhibition
5. Level of expression
6. Substrate cycle
7. allosteric activation

Back 213

1. pyruvate
2. acetyl-CoA
3. Ahh yeah. 3 subunits. 3 cofactors - TPP, Lipoic acid, FAD
4. GTP/ATP, NADH, Succinyl-CoA
5. induced by exercise training
6. regulation of reciprocal pathways (citrate synthase vs citrate lyase)
7. CoA, NAD+, NADH

Front 214

Pyruvate dehydrogenase
1. What stimulates complex?
2. What inhibits complex?
3. Pyruvate dehydrogenase kinase does what?
4. Pyruvate dehydrogenase phosphatase does what?
5. reciprocal pathways

Back 214

1. CoA, NAD+, AMP
2. Acetyl-Coa, NADH, GTP/ATP
3. phosphorylates and inactivates the complex
4. dephosphorylates and deactivates the complex
5. citrate synthase vs citrate lyase

Front 215

Isocitrate dehydrogenase
1. what be the reaction
2. substrate availability
3. Allosteric inhibition
4. Allosteric activation

Back 215

1. isocitrate + NAD+ --> a-ketoglutarate + NADH + H+ + CO2
2. limited by isocitrate and NAD+ availability
3. ATP, NADH
4. ADP, Ca++

Front 216

Pyruvate dehydrogenase deficiency - inherited
1. Which subunit has a defiency?
2. what are the symptoms?
3. How common?
4. what condition does it cause?

Back 216

1. E1
2. 1 in a million
3. muscular spasticity, neurological defects, failure to thrive
4. lactic acidosis

Front 217

Pyruvate dehydrogenase deficiency - acquired
1. What vitamin deficiency?
2. what does this cause?
3. get lactic acidoses because pyruvate from glycolysis can't enter the TCA cycle.

Back 217

as;ldkfjasl;dfj

Front 218

EPIDERMOLYSIS BULLOSA

Back 218

skin disorder

Front 219

Definitions:
1. Epithelium
2. Epidermis

Back 219

1. Outermost layer of cells covering all exposed surfaces of the body
2. Outermost layer of the skin

Front 220

Does Epidermolysis bullosa affect keratinized or nonkeratinized skin?

Back 220

BOTH

Front 221

1. Keratinized body parts
2. Non keratinized body parts

Back 221

1. skin, tongue, external lips
2. cornea, oral cavity, esophagus, rectum, vagina

Front 222

Most common abnormal components in epidermolysis bullosa:
1. keratin 5 and keratin 14
2. laminin 5
3. type VII collagen

Back 222

1. form keratin intermediate filaments, present in basal cells and attach basokeratinocytes to hemidesmosome structure

2. anchoring filaments and attaches the hemidesmosome to the lamina densa

3. Type VII densa - extends from the lamina densa and loops around the collagen fibers (type i and III) present in the dermis

Front 223

Epidermolysis bullosa
1. Feature 1
2. Feature 2

Back 223

1. blistering
2. mechanical fragility of the skin

Front 224

Genes of epidermolysis bullosa:
1. Is it hereditary?
2. caused by mutations in what genes?
3. what is their inheritance type?
4. wide range of severity?

Back 224

1. yes
2. the genes that code for the proteins in the BMZ
3. autosomal recessive or dominant
4. can be not so bad to really really bad

Front 225

Categories of EB
1. Patients are broken down into 3 major subtypes:
1. Simplex
2. Junctional
3. Dystrophic

Back 225

1. most superficial
get intraepidermal blisters
separation occurs in most cases in the basokeratinocyte
2. separation occurs in the lamina lucida
3. separation occurs in the lamina densa

Front 226

Nucleotides, flow genetic info
People thought genetic material was protein until what?

Back 226

Avery-Macleod-McCarty experiment and Hershey and Chase blender experiment

in the 50s

Front 227

Central Dogma
1. DNA is transcribed to RNA. Where does this rna go?
2. RNA transcribed to AA's. Why is it called transcribed?
3. how is tRNA bonded to an AA?
4. The flow of all this is often broken by what organism?

Back 227

1. floats outside the nucleus to be transcribed
2. changing the language
3. covalently
4. the retrovirus, like HIV

Front 228

Draw all 5 basic nitrogenous bases

Back 228

DO IT

Front 229

the bases of DNA:

Back 229

Adenine
Thymine
Guanine
Cytosin

Front 230

the bases of rna

Back 230

Adenine
Uracil
guanine
cytosine

Front 231

A cancer treatment involving thymine and uracil relations:

Back 231

preventing uracil from being methylated so that it cannot become thymine. methotrexate is used.

Front 232

Unusual purine bases:

Back 232

hypoxanthine, xanthine, uric acid

Front 233

Keto enol tautomerism
1. Which form is favored in pyrimidines?
2. Which form is favored in purines?

Back 233

1. Lactam, or keto form
2. keto form.

Front 234

UV light
what wavelength do nitrogenous bases absorb light?

what do we use to find out the concentration of DNA/RNA insolution?

Back 234

260nm... cause they TOO SEXY

spectrometer

Front 235

1. Nucleoside has what two components?
2. Purines end in
3. Pyrimidines end in
4. connection of ribose to purine?
5. connection of ribose to pyrimidine?

Back 235

1. base and ribose
2. 'osine' like adenosine and guanosine
3. 'idine' like uradine, cytodine, and thymidine
4. B 1 9 connection
5. B 1 1 connection

Front 236

Gycosidic bond rotation:
1. Syn
2. Anti

Back 236

1. Where bulk of ribose in same orientation as bulk of base
2. where bulk of ribose is in opposite orientation as bulk of base

Front 237

Why is the word nucleotide phosphate redudant?

Back 237

the tide in nucleotide implies phosphate

Front 238

what kind of acids are phosphates?

Back 238

polyprotic

Front 239

where are two places phosphates can attach to ribose sugars/

Back 239

the 5' and 3'

Front 240

Functions of nucleotides
1. Nucleoside 5' triphosphates are carriers of...
2. bases serve as...
3. Cyclic nucleotides are...

Back 240

1. energy, when there are 3 phosphate units attached to 5' end
2. recognition units
3. singal molecules and regulators of cellular metabolism and reproduction

Front 241

what is the name of the bond that gives energy to ATP?

Back 241

phosphoric anhydride bond

Front 242

Different kinds of triphosphates and their functions:
1. GTP
2. CTP
3. UTP

Back 242

1. protein synthesis
2. lipid synthesis
3. carbohydrate metabolism

Front 243

when two phosphate are linked together we call it a

Back 243

pyrophosphate

it still has the high energy bond

Front 244

Types of RNA:
1. rRNA
2. mRNA
3. tRNA

Back 244

1. ribosomal RNA, forms 90% of rna in cell, forms scaffolds for ribosomes, are also enzymes
2. 2% of all rna
3. 2nd most abundant

Front 245

DNA double helix:
1. stabilized by what?
2. base pairs arise from what?
3. who had the pairing data?
4. who had the xray?
5. who knew it was a helix?
6. who figured out the h bonds?

Back 245

1. H bonds
2. h bonds
3. Erwin Chargaff
4. Rosalind franklin
5. Crick
6. Watson

Front 246

Diameter and length of DNA

Back 246

2 nm, 1.6 million nanometers

Front 247

How many protein products are coded for 1 mRNA in
1. eukaryotes
2. prokaryotes

Back 247

1. 1
2. many

Front 248

DNA compaction

Back 248

chromatin + 8 histone proteins
= nucleosome

nucleosomes are twisted into a solenoid, 6 nucleosomes per turn

solenoid forms loops with 50 turns per loop

18 loops organize into minibands

minibands stack on each other to form chromosome

Front 249

mRNA
1. transcription and translation occur at the same time for prokaryotic or eukaryotic?
2. introns and exons are in which kind of cell, eurkaryotic or prokaryotic?
3. diversity in eukaryotic proteins provided by

Back 249

1. prokaryotic
2. eukaryotic
3. alternative splicing

Front 250

postranslational modifications of mRNA:

Back 250

poly A tail on 3' end
5' cap

Front 251

is the poly A tail coded for in the DNA?

Back 251

No. the signal is tho. the tail is added which base pairs with the mRNA

Front 252

Ribosomal RNA
1. subunit size of eukaryotes
2. subunit size of prokaryotes

Back 252

1. 60s and 40s
2. 50s and 30s

Front 253

What is the 3' terminal sequence of a tRNA?

Back 253

CCA

Front 254

ribosomes are 2/3 what and 1/3 what

Back 254

rna, protein

Front 255

Native americans domesticated what percent of agricultural products used in the us today?

Back 255

60%

Front 256

Nixtamalization

who invented this and used it?

Back 256

dry corn and put in alkaline solution. makes niacin in corn easier to absorb. Improved nutritional value.

native americans

Front 257

European settlers:
what did they bring?

what were they at risk for?

Back 257

the domestication of cattle

did not use nixtamalization, so they were at risk for pellagra

Front 258

what was a con of nixtamalization?

Back 258

removed loss of fiber and minerals. but hey the niacen was in there

Front 259

Vitamin B3
1. where absorbed?
2. How much is stored in the body?

Back 259

1. intestine
2. very little

Front 260

Pellagra
1. what does it present as?
2. causes triple D:
3. neurological symptoms?

Back 260

1. Rash
2. dementia, diahrea, dermatitus
3. insomnia, anxiety depressia, delusions, or encephalopathy

Front 261

Vitamin C
1. what is it in?
2. where is it absorbed?
3. amount in blood is regulated by
4. role in synthesis of...
5. disease state is
6. vitamin c deficiency also what?

Back 261

1. citris fruits, tomatoes, brussel sprouts, broccoli, strawberries, spinach and cabbage
2. distal small intestine
3. kidney
4. collagen
5. scurvy
6. causes corkscrew hairs and perifollicular petechiae

Front 262

B1
1. what is the other name?
2. aborbed where?
3. excess excreted where?
4. denatured with...
5. cofactor for metabolism enzymes
6. two different disease

Back 262

1. thiamine
2. jujenum and ilium
3. excretory and urinary system
4. heat, pH
5. truth
6. beri beri and wernicke

Front 263

B1 thiamine diseases:
1. Dry beri beri

2. Wet beri beri

Back 263

1. neuropathy of of distal extremities and impairment of sensory and motor functions
2. same as 1 but also cardiac problems, low blood pressure lets fluid collect in extremeties

Front 264

deficiency of iron causes what?

Back 264

anemia

Front 265

deficiency of iodine causes what

Back 265

goiter

Front 266

In the 1900s...

what was a major problem in the north?

what was a major disease problem in the south?

Back 266

Rickets. Low sunlight, not much fresh fruits and veggies, and no fortified D milk

Pellagra. Diet was mostly grits!

Front 267

top five reasons for dietary deficiencies:

Back 267

1. fruits and veggies only available during short seasons
2. inadequate and time consuming food preservation methods
lack of facilities for rapid transport
contamination of food supplies
methods of processing preserving altered the nutrients

Front 268

When did food preservation take a giant leap?

Back 268

In the 30s and 40s.

Front 269

So what happened in that time?

Back 269

Canning!
commercial freezing - preservation of meats
refrigerated rail cars and trucks allows fruits and veggies to go everywhere
food preservatives

MOST IMPORTANT:
Food fortification.

Front 270

Food fortification:
1. so, food processing methods caused nutrients...
2. nutrients are added back to
3. Iodized salt
4. modern examples

Back 270

1. to be lost
2. staple foods to prevent nutritional deficiencies
3. 1924, added to salt. Goiters gone by 1930
4. milk, OJ, cereal

Front 271

what are some historical methods of food preservation?

Back 271

Drying
Salting
Sugaring
Pickling
Cold storage

Front 272

When was RDA established?

what did it have on it initially?

Back 272

1941

2 minerals
vitamins A C D niacin and thiamin

Front 273

What is the shift in the #1 cause of death attributed to?

Back 273

food advances

Front 274

What is the most important influence on food choice?

Back 274

TASTE

then price

Front 275

What was the total calorie consumption increase between 1983 and 2000?

Back 275

19%

Front 276

What was the total calorie consumption increase between 1970 to 2000?

Back 276

24.5%

Front 277

How much do americans spend on FAFH?

Back 277

42% of budget

Front 278

each additional meal eaten away from home adds how many kcal per day?

Back 278

134

Front 279

How much has grain consumption increased?

Back 279

56lb per person

Front 280

Dairy consumption has improved but there is a catch

Back 280

it is more cheese than milk

has higher fat, sodium content, more processed

Front 281

How much does added fats and oils account for?

Back 281

32%

Front 282

Who was the first director of USDA?

Back 282

wilbur olin atwater

Front 283

1943-55
1. butter has its own...
2. why the servings language?
3. how many basic food groups?

Back 283

1. food group!
2. WWII
3. 7

Front 284

when was the first dietary table published?

Back 284

1984

Front 285

in 1956 to 79
1. how many food groups?
2. first table to recommend a minimum but what about maximum?

Back 285

1. 4

2. no maximum. more if you can get it!

Front 286

When did the USA have to deal with overconsumption?

Back 286

in the 1970s

Front 287

5th group added...

Back 287

fats sweets alcoholic beverages

Front 288

When did the first moderation message come out?

Back 288

1970s

Front 289

When was the first usda and hhs dietary guideline published?

Back 289

1980

published and updated every 5 years since

Front 290

1980: different language, like

Back 290

caution to consume in moderation
eat a variety, maintain ideal weight, avoid too much fats, avoid too much sugar and sodium, drink alcohol in moderation

Front 291

1985: logo change

Back 291

instead of numbering, it is connected to convey groups are interconnected

Front 292

1990
start to distinguish between different kinds of...

what was published?

Back 292

fats

food labeling and education act

Front 293

When was the food guide pyramid born?

Back 293

1992! used in conjunction with newly passed Nutrition labeling and education act

Front 294

When was physical activity added to guidlines?

Back 294

1995

Front 295

Is there a scientific link between quantity of food eaten and quantitity of exercise need to burn calories?

Back 295

well def not in 1995

Front 296

pyramid in 92, hey, what what the goal?

Back 296

to convey variety, proportionality, moderation

Front 297

whoops, food labeling act goes in effect when?

Back 297

1994

Front 298

When was variety introduced?

Back 298

1995

Front 299

2000 dietary guideline motto is...

Back 299

aim build and choose!@

Front 300

2005, guidelines show activity how?

Back 300

guy climbing the pyramid

Front 301

What is dominance of most metabolic disorders?

Back 301

Recessive

Front 302

General features of acute onset metabolic disorders
1. intoxication
2. energy depletion

Back 302

1. abrupt severe symptoms due to accumulation of diffusible small molecules

2. impaired ATP production.

Front 303

Progressive onset metabolic disorders
1. macromolecule buildup
2. symptoms are specific to...
3. developmental...
4. course facial features, organomegaly...
5. lysosomal storage disorder, metal metabolism, mitochondrial disorders

Back 303

1. like glycolipids
2. tissue of enzyme substrate, not enzyme
3. regression
4. skeletal abnorma
5. yeap

Front 304

What is clinical heterogeneity?

Back 304

refers to phenotypic variation within same disorder

it can be mild, it can be really bad

variable influence is modifier genes

Front 305

1. Locus heterogeneity

2. Allelic heterogeneity

Back 305

1. mutations in different genes cause same clinical phenotype
ex: PKU
locus FOCUS - ON SAME CLINCIAL PHENOTYPE

2. different mutations in same gene result in distinct clinical phenotypes
Ex: GFFR3

Front 306

CLINICAL CHALLENGES:

Are signs and symptoms nonspecific?

Back 306

Yes. Routine childhood illnesses are excluded first.

Inborn errors considered secondarily.

THIS IS A CHALLENNGE

Front 307

CLINICAL CHALLENGES

are standard medical professionals familiar with metabolism disorder tests?

Back 307

No. sometimes there is inappropriate sample storage

Front 308

What four standards of diagnosis do you need?

Back 308

clinical evidence
metabolite pattern for the enzyme deficiency
demonstrate enzyme deficiency
demonstrate mutation in gene

Front 309

what is a method to look at metabolite pattern?

Back 309

look at plasma amino acids

Front 310

How to demonstrate a deficiency of an enzyme activity?

Back 310

lysosomal enzyme analysis

Front 311

Standard lab tests in hospital:
1. what will blood tell you?
2. What will urine tell you?

Back 311

1. ammonia, glucose, lactic acid
2. creatinine, ketone bodies

Front 312

Biochemical genetics lab
1. what will blood tell you?
2. Will will urine tell you?
3. CSF?
4. Cultured cells?

Back 312

1. amino acids (HPLC)
acylcarnitines (MSMS)
Organic acids (GCMS)
2. organic acids
amino acids
GSGs
3. amino acids
4. enzyme assays

Front 313

Therapeutic concepts:
Restore enzyme activity
1. Organ transplant
2. Supplement with vitamins
3. ERT
4. Experiments

Back 313

1. not always effective
2. b12, biotin, etc
3. LSDs, others? expensive, blood brain barrier
4. Intrathecal ERT
SRT
molecular chaperones
increase expression levels

Front 314

Therapeutic concepts:
Remove toxic compound
1. decrease source of offending metabolite
2. provide alternate pathway

Back 314

1. PKU - decrease phenylalanine intake
urea cycle disorders - decrease protein intake
hereditary fructose intolerance - decrease sugar intake
LSDs - SRT
2. urea cycle disorder - phenylacetate for nitrogen excretion

Front 315

therapeutic options:
supply or substitute missing product

Back 315

give starch to somebody who has hypoglycemia

arginine supplements

Front 316

monogenic diseases involve a single

Back 316

gene

Front 317

NAMES
1. first cointed the term inborn errors of metabolism
2. one gene one enzyme
3. watson and crick

Back 317

1. Archibald Garrod
2. beadle and tatum
3. dna structure

Front 318

statement about metabolic diseases:

Back 318

accumulation of substrate, depletion of downstream products, and production of unusually and potentially toxic secondary products

Front 319

Galactosemia:
1. caused by a mutation of what enzyme?
2. substrate accumulation
3. product depletion
4. secondary reaction products toxicity

Back 319

1. GALT
2. galactose and gal1P reach high levels causing liver disease
3. UDP galactose isn't being made so glycoconjugates cannot be made
4. galactitiol accumulates in the eye and causes cataracts

Front 320

enzyme that requires a cofactor but does not have one

Back 320

apoenzyme

Front 321

Are all metabolic diseases caused defective enzymes?

Back 321

No.

All sorts of other things can cause metabolic diseases. Like, problems with transporters, cofactors, organelles...

Front 322

Metabolic disorders that involve loss of multiple enzyme activities

Back 322

cofactor Biotin required for 4 different carboxylation pathways

Front 323

What is Tay Sachs and why is it relevant?

Back 323

Lysosomal storage disease

prevalant in askenazi jews

Front 324

most metabolic disease are recessive, but some are also

Back 324

x linked

sorry guys

Front 325

Acute onset disorders are also called

Back 325

small molecule disorders

Front 326

Acute onset illness:
1. what substrate is accumulating?
2. characterized by an abrupt severe illness following...
3. blood pH? other symptoms?
4. include amino whats? organic what?

Back 326

1. toxic substances
2. feeding or fasting
3. acidosis, vomiting, seizures, lethargy, coma, death
4. acidopathies, acidemias

Front 327

what is the best example of true acute onset disorder?

Back 327

organic acidemia.

hours after eating a high protein meal, patient becomes deathly ill

Front 328

Energy depletion of acute onset metabolic disorders:
impaired ATP production
1. primarily involve disorders of...
2. abrupt severe symptoms associated with...
3. is it as abrupt as organic acidemia?

Back 328

1. fatty acid oxidation. but also glycogen storage disorders and mitochondrial disorders
2. fasting or intercurrent illness
3. no

Front 329

Progressive onset metabolic disorders:

patients show...

Back 329

developmental regression

Front 330

clinical heterogeneity:

when do severe forms present?
when do mild forms present?

Back 330

early in life

later in life

Front 331

In cases of clinical heterogeneity, is there a genotype / phenotype correlation?

Back 331

NO.

environmental and whatnot

Front 332

most cases of PKU are bc of mutation in...

but some are in

Back 332

PAH

biopterin

Front 333

if a patient presents with a cold, should you immediately assume its a metabolic disorder?

Back 333

NO

you have to rule out the simple stuff first, then if nothing turns up, think about metabolic disorders

Front 334

Therapeutic options
Restore enzyme activity
pros / cons
1. Organ transplant
2. Reactivate with vitamins
3. ERT
4. experimental

Back 334

1. provides source of cells that have normal enzymes
/
sometimes patients die, not always effective

2. enough cofactor will make the enzyme work
but sometimes enzymes don't need enzymes
3. make recombinant enzymes, tag, localize
doesn't always work. expensive. cannot cross blood brain barrier.
4. intrathecal ERT, use molecular chaperones, use small molecules

Front 335

Therapeutic options
Remove accumulating toxin
1. decrease source of offending metabolite.
2. PKU
3. Urea cycle disorders
4. Heredityary fructose
5. Lysosomal storage

Back 335

1. bonk
2. stop eating phe
3. stop eating protein, or so much of it
4. stop eating sugar
5. SRT

Front 336

Therapeutic options for metabolic diseases:
Supply or substitute the missing product
1. provide what to prevent hypoglycemia?
2. provide what to urea cycle disorder?

Back 336

1. starch for fatty acid oxidation disorders to prevent hypoglycemia
2. arginine

Front 337

Acute onset disorders:
Amino Acid Catabolism
1. Deficiencies in enzymes towards the beginning of the catabolic pathway lead to what
2. Deficiencies in enzymes towards the end of catabolic pathway lead to what?

Back 337

1. aggregation of amino acids, causes PKU
2. organic acids

Front 338

when amino acids are in excess, what do they do normally?

Back 338

become ketone bodies or process through the TCA cycle

Front 339

Diagnosis of LSD's:
1. microscope could find what
2. radiological exams could find what
3. ophthalmologic exams could find what
4. urinary analysis could show what?
5. Enzyme activity assays could show what?

Back 339

1. accumulation of fibroblasts and leukocytes
2. beaking of vertebrae
3. macular cherry red spots
4. accumulation of large molecules like glycoproteins and oligosaccharides
5. evidence of LSD

Front 340

best way to diagnose mitochondrial disease:

other ways too

Back 340

mtDNA genome sequencing

elevated organic acids, red fibers that are mitochondria

Front 341

what does michaelis menten equation describe?

Back 341

initial reaction rate Vo depends on position of substrate binding equilibrium and the rate constant k2

Front 342

assumptions of michaelis menten:
quasi steady state assumption

Back 342

concentration of the enzyme changes so slow it can be set to zero
d[es]/dt = 0

Front 343

assumption of michaelis menten:

Back 343

total enzyme concentration does not change over time

so

E = E + ES = constant

Front 344

if rate determining step is slow compared to substrate dissocation, Km = Kd of ocmplex

Back 344

asdf

Front 345

the measure of catalytic efficiency

Back 345

k2/ km

Front 346

the km is an equilibirum constant for the enyzme and substate binding if:

Back 346

the rate constant for the covnersion of ES to product is very small compared to the other rates constatns

Front 347

when performing enzyme kinetic experiments to measure vmax, wwhat is held constant?

Back 347

enzyme concentration