Histo Final 1

Front 1

Fluidity of the cell membrane correlates with what(2):

Back 1

-negatively with the amount of cholesterol and
-positively with the proportion of unsaturated to saturated fatty acids

Front 2

Glycocalyx represents what + made by:

Back 2

the outermost layer of the cell membrane that is composed of oligosaccharide chains of glycoproteins and glycolipids

Front 3

vesicle-mediated transport is used when:

Back 3

New membrane material is assembled in various cisternae of Golgi -> membrane

Front 4

Outer membrane of the nuclear envelope is called:

Back 4

endoplasmic reticulum

Front 5

endoplasmic reticulum continuous with:

Back 5

the RER membrane

Front 6

SER is found manly in which type of cells:

Back 6

in cells that synthesize cholesterol and steroid

Front 7

RER is found manly in which type of cells:

Back 7

cells that synthesize secretory proteins

Front 8

Function of SER:

Back 8

-Steroid hormone synthesis
- Drug detoxification, especially in the liver

- Cam++ storage for skeletal muscle contraction and re-uptake of ions during relaxation

Front 9

Ribophorins are what:

Back 9

RER membrane receptors – bind large ribosomal subunit

Front 10

Function of RER:

Back 10

synthesizes secretory, plasma membrane, and lysosomal proteins.

Front 11

What happens with proteins in RER:

Back 11

initial modifications + transport of proteins + protein sorting pathways

Front 12

What happens with a protein AFTER RER?

Back 12

Only properly-folded proteins are transported from the RER to the Golgi complex

Front 13

The Golgi complex – function of different compartments (in order From ER):

Back 13

-cis face= Forming face
-Golgi stack (-Cis cisterna -Medial cisterna
-Trans cisterna)
-trans face= Maturing face

Front 14

IN trans Golgi proteins are sorted into vesicles that will go where:

Back 14

i) Form primary (nonactive) lysosomes
ii) Deliver plasma membrane proteins
iii)Secrete proteins in the process of exocytosis

Front 15

Lysosomes is what / contains what:

Back 15

small vesicles that contain hydrolytic enzymes active in the acidic pH, ca 5.0

Front 16

GOLGI FUNCTIONS:

Back 16

chemical modifications of exported proteins, sorting of membranes and lysosomes.

Front 17

Golgi processes membrane-packaged proteins – from where + how:

Back 17

Proteins from RER by: GLYCOSYLATION, phosphorylation, acetylation, methylation, sulfation

Front 18

enzymatic marker of lysosomes:

Back 18

Enzyme ACID PHOSPHATASE

Front 19

ATP driven H+ pumps is active in which type of lysosomes?

Back 19

primary=non-active lysosome

Front 20

Lysosomal enzymes pathway:

Back 20

-synthesized in RER,
-transfered and packed in Golgi into primary lysosomes which contain inactive enzymes.

Front 21

How is the precursor lysosomal enzymes are directed in Golgi into right vesicules?

Back 21

Adding mannose-6-phosphate (M6P) to enzyme protein in cis Golgi provides means to deliver it via transport vesicles that budd off from trans Golgi into prelysosomal vesicles

Front 22

M6P receptor – what happes when the job is done?

Back 22

recycles in a small budding vesicle to trans Golgi network.

Front 23

secondary lysosomes contains what:

Back 23

material that is being digested

Front 24

CYTOSKELETON definition:

Back 24

network of filamentous proteins located in the cytoplasm

Front 25

CYTOSKELETON function:

Back 25

• gives a cell its shape
• provides a basis for movement of:
– entire cell (micro- and macrophages)
– organelles (mito-, lysosomes – vesicles (secretory, endosomal)

• enables mitosis = cell division

Front 26

CYTOSKELETON size of materials (large - small):

Back 26

Microtubules – 25
myosin filaments – 16
intermediate filaments – 10
actin filaments(micro) – 6

Front 27

Tubulin proteins make up:

Back 27

microtubules

Front 28

wear and tear cells has a lot of:

Back 28

intermediate filaments

Front 29

Micro/Actin-filaments – function:

Back 29

Maintaning cell shape by resisting pull(tension)
–motility
– muscle contraction
–cell devision

Front 30

Intermediate filaments function:

Back 30

Maintaning cell shape by resisting pull(tension)
–anchors nucleus and other organelles

Front 31

Intermediate filaments made by:

Back 31

Keratin, Vimetin, lamin, etc

Front 32

Microtubles – function:

Back 32

Maintaning cell shape by resisting PUSH/compression
– motility via cilia/flagella
– move chromosomes during divison
– move organelles

Front 33

Microtubles – made by:

Back 33

A-tubulin, b-tubulin

Front 34

Microfilaments Integrated with what in skeletal muscle?

Back 34

Thick(16nm) myosin filaments

Front 35

Microfilaments location in cell:

Back 35

Present as thin sheath just beneath the plasma membrane in most cells

Front 36

contractile string during divison is made by:

Back 36

Microfilaments

Front 37

Microtubles made by:

Back 37

wall composed of 13 protofilaments, each is a polymer made of α- and β-tubulin heterodimers

Front 38

Microtubles Provide basis for the structure of:.

Back 38

Centrioles Cilia Basal body of cilia mitotic spindle fibers

Front 39

Important proteins in intracellular transport:

Back 39

Mechanoenzymes or motor proteins like dynein or kinesin - They belong to the protein superfamily of myosin I

Front 40

non—muscular myosin is which type:

Back 40

myosin I

Front 41

myosin I proteins has which compontents:

Back 41

have „head” with ATPase activity and a short „tail” – a fibrillar part

Front 42

Cylindrical structure of a Centriole:

Back 42

9 MT triplets are located at the periphery of a tubule

Front 43

Centriole’s functions:

Back 43

1. Forming of mitotic spindle basal bodies of cilia and flagella
2. centriole’s replication in S phase of cell Cycle
3. Two pairs of centrioles move to opposite cell sides (poles) during mitosis

Front 44

Basal body of a cilium has how many MT?

Back 44

9 MT triplets

Front 45

Centrosome is what:

Back 45

– region of cytoplasm adjacent to nucleus that contains centriole known as Microtubule organization center (MTOC)

Front 46

Nucleus maximum diameter:

Back 46

- 10 um

Front 47

Outer layer of Nuclear envelope is continuous at certain sites With:

Back 47

RER, vimentin mesh, ribosomes

Front 48

perinuclear cisterna is what?

Back 48

A space between Inner and outer layers of Nuclear envelope

Front 49

Chromatin consists of:

Back 49

-double-stranded DNA complexed with histones (basic proteins) and acidic proteins (DNPs)
-rRNA complexed with ribosomal proteins, mRNA connected to other proteins (RNPs)
-Condensed chromatin – heterochromatin

Front 50

Heterochromatin/ Euchromatin – which is active:

Back 50

Euchromatin

Front 51

Heterochromatin stains:

Back 51

lightly intensively with basic stain

Front 52

Euchromatin stains:

Back 52

lightly

Front 53

Which substances get in to the nucleus?

Back 53

-proteins (structural, enzymatic, regulatory)
-nucleotides and other small molecules

Front 54

Which substances get out of the nucleus?

Back 54

mRNA and tRNA,
+rRNA complexed with proteins = almost complete ribosomal subunits

Front 55

Nuclear pores average ?? nm in diameter:

Back 55

80

Front 56

Nucleolus do what:

Back 56

synthesis of rRNA and its assembly into ribosome precursors

Front 57

The function of the nucleolus in ribosome synthesis:

Back 57

Transcription of rRNA genes (of rDNA) -> Assembly and export of almost complete small and large ribosome subunits

Front 58

full ribosome assembly takes place where + whats needed:

Back 58

in cytoplasm in the presence of mRNA

Front 59

Messenger RNA (mRNA) do what:

Back 59

carries genetic information of the DNA

Front 60

Transfer RNA (tRNA) do what:

Back 60

binds specific aminoacids and respective codons at mRNA

Front 61

Ribosomal RNA (rRNA) do what:

Back 61

catalyzes translation (peptide bond formation)

Front 62

Ribosomes size:

Back 62

40S + 60S = 80S

Front 63

mRNA binding site - A site (aminoacyl) – function:

Back 63

site of tRNA and amino acid entry into the ribosome

Front 64

mRNA binding site - P site (peptydyl) – function:

Back 64

site of amino acid introduction into the growing polypeptide

Front 65

mRNA binding site - E site – function:

Back 65

exit site of empty tRNA

Front 66

mRNA binding site - Catalytic site – function:

Back 66

formation of peptidyl bond

Front 67

The steps of translation(4):

Back 67

Initiation
• Elongation
• Translocation
• Termination

Front 68

Polysome are what + function:

Back 68

Consists of 3-30 or more Ribosomes -> synthesizes protein for intracellular use

Front 69

Mitosis =

Back 69

karyokinesis + cytokinesis

Front 70

Formation of the 2nd pair of centrioles – when:

Back 70

during the S and G2 phase is the first sign of the incoming mitosis

Front 71

Centromere?

Back 71

Place where the chromosomes “sisters” are joined into 1 unit.

Front 72

Prophase – what happens:

Back 72

-chromatin fibers become coiled into chromosomes
-mitotic spindle forms in the cytoplasm
-kinetochores are formed from the protein complexes

Front 73

chromatin fibers become coiled into chromosomes – due to:

Back 73

- phosphorylation of H1 histone molecules <- kinase
-dephosphorylation of H3 histone molecules -< phosphatase

Front 74

In late prophase – what happens:

Back 74

- nuclear envelope breaks up
- polar fibers reach from each cell pole to the cell's Equator
-kinetochores attach to kinetochore MT fibers (plus end)

Front 75

nuclear membrane disappears completely – by what + when:

Back 75

the phosphorylation of nuclear lamina and nucleolin
– Metaphase

Front 76

Metaphase – what happens:

Back 76

-2 pairs of centrioles align at opposite poles of the cell
-chromosomes move randomly until they attach (at their kinetochores) to MT fibers from both sides of their centromeres

Front 77

Metaphase Check point:

Back 77

If mitotic spindle microtubules are not bound to even one chromosome

Front 78

Anaphase – what happens:

Back 78

contraction’ of spindle MT -> paired centromeres in each distinct chromosome begin to move apart

Front 79

Anaphase – contraction MT works how:

Back 79

-depolymerization of kinetochore MT
- polymerization of polar MT

Front 80

Telophase – what happens:

Back 80

- chromosomes are cordoned off into distinct new nuclei in the emerging daughter cells
-nuclear envelopes are formed from remnant pieces of the parent cell's nuclear envelope and from pieces of ER

Front 81

Cytokinesis=

Back 81

the division of the original cell's cytoplasm

Front 82

Cleavage occurs by the contraction of:

Back 82

a thin ring of actin and myosin filaments (contractile ring)

Front 83

Karyoplasm constitutes what:

Back 83

the nucleus and is surrounded by the nuclear envelope

Front 84

the hydrophilic polar heads face what:

Back 84

the periphery, forming the extracellular and intracellular surfaces

Front 85

the surface of the inner leaflet (closest to the protoplasm) is called:

Back 85

the P-face.

Front 86

the surface of the outer leaflet (closer to the extracellular space) is called:

Back 86

the E-face

Front 87

types of proteins on the cell membrane:

Back 87

Transmembrane proteins, Peripheral proteins ( not embedded into the membrane)

Front 88

lipid rafts function in:

Back 88

cell signaling.

Front 89

ion channels are:

Back 89

hydrophilic

Front 90

Which channels are always open:

Back 90

Ungated channels

Front 91

most common ungated channel:

Back 91

K + leak channels

Front 92

ungated channel examples:

Back 92

K+, Aquaporins

Front 93

symport=

Back 93

transport of 2 molecules in same direction

Front 94

antiport =

Back 94

transport of 2 molecules in opposite direction

Front 95

uniport =

Back 95

transport of 1 molecule

Front 96

Na+ K+ -ATPase – which amount go where?,

Back 96

three sodium ions against a concentration gradient out of the cell and two potassium ions into the cell

Front 97

polar molecule. – location of receptor:

Back 97

the cell membrane

Front 98

G-protein system – what happes when the receptor is activated:

Back 98

When the Gs protein is activated, it exchanges its gDP for GTP -> α subunit dissociates and contacts adenylate cyclase, activating it to catalyze the transformation of cytoplasmic AtP to cAMP.

Front 99

G-protein system – cAMP do what:

Back 99

cAMP, one of the secondary messengers of cells, activates A kinase, which initiates the eliciting of a specific response from the cell.

Front 100

Transcription=

Back 100

that is, the synthesis of a messenger RNA(mRNA)

Front 101

Translation=

Back 101

assembly of the correct amino acid sequence, based on the nucleotide template of the mRnA

Front 102

the small ribosomal subunit has binding sites for:

Back 102

mRnA and three additional binding sites:
(tRnA) (P-site)
aminoacyl tRnA (A-site)
, and an exit site (E-site)

Front 103

the seR functions in:

Back 103

lipid and steroid synthesis, glycogen metabolism, and detoxification of noxious substances,

Front 104

the cisterna of the ReR is continuous with:

Back 104

the perinuclear cistern of the nuclear envelope.

Front 105

Methionine =

Back 105

initiator tRNA on the P site

Front 106

Translation occurs in which direcetion?

Back 106

5′to 3′direction on the mRNA

Front 107

small ribosomal subunits attach where on the mRNA?

Back 107

to the 5′end of the mRnA

Front 108

signal recognition particle(SRP) location + function:

Back 108

freely floating in the cytosol. sRP binds to the signal peptide, protein synthesis ceases, and the ribosome-mRnA-sRP complex moves to the ReR.

Front 109

Golgi: convex entry face near the nucleus known as the:

Back 109

cis-Golgi network(CGN)

Front 110

Cis-face function:

Back 110

where newly synthesized proteins from the ReR enter the golgi complex

Front 111

the functions of the golgi complex include:

Back 111

carbohydrate synthesis and the modification and sorting of proteins.

Front 112

Proteins leaves where on ER in what type of vesicle:

Back 112

Proteins leave the transitional ER , packaged in small transport vesicles whose membrane, derived from the ReR, is covered by coP ii

Front 113

coP i–coated vesicles is used when?

Back 113

COP 2 from ER can do either:
retrograde transport -> ER
-anterograde transport -> Golgi
– both in COP 1

Front 114

After GOLGI the modified proteins are packaged in? to?

Back 114

clathrin-coated vesicles or coP ii–coated -> the cell membrane
-storage
-Late endosomes (->lysosomes)

Front 115

discontinuous exocytosis requires what + called what:

Back 115

a clathrin coat and is said to follow the regulated pathway of secretory proteins,

Front 116

continuous exocytosis requires what + called what:

Back 116

coP ii–coated vesicles and is said to follow the constitutive pathway of secretory proteins

Front 117

ERGIC is what:

Back 117

Area/structure between Transitional ER and cis-face of golgi

Front 118

Which structure after trans-face?

Back 118

trans-Golgi network

Front 119

the transfer of material from the extracellular space into the cytoplasm is known as:

Back 119

endocytosis

Front 120

smaller molecules (ligands) are “eaten” how:

Back 120

pinocytosed into a pinocytotic vesicle

Front 121

Pinocytotic vesicles lose their clathrin coat and fuse with the:

Back 121

Early endosome,

Front 122

most prevalent enzyme in peroxisomes is + function:

Back 122

catalase, which decomposes h2o2 into water and oxygen. -

Front 123

peroxisomes also participates in:

Back 123

lipid biosynthesis,

Front 124

Proteasomes are responsible for:

Back 124

• Degradation of proteins that are misfolded, damaged, denatured, or otherwise malformed
• cleaving of antigenic proteins into smaller fragments known as epitopes

Front 125

Proteolysis via proteasomes works how:

Back 125

energy-requiring attachment of multiple copies of ubiquinone to the candidate protein to form a polyubiquinated protein

Front 126

the mean life span of a mitochondrion is about :

Back 126

10 days,

Front 127

Mitochondria - Intermembrane space located between:

Back 127

the outer and inner membranes

Front 128

Mitochondria- Matrix (intercristal) space bounded by:

Back 128

the inner membrane

Front 129

Mitochondria - matrix a viscous fluid with a high concentration of:

Back 129

proteins, ribosomes, RnA, circular DNA(which codes for only 13 mitochondrial proteins)

Front 130

Mitochondria – H+ ions are first transported from -> to?

Back 130

from the matrix into the intermembrane space. (then used by ATPase)

Front 131

inclusions are what + examples:

Back 131

nonliving elements of the cell that are freely present within the cytosol and are not membrane bound. the major inclusions are glycogen, lipids, pigments, and crystals

Front 132

microtubules – which ends grows:

Back 132

plus end

Front 133

microtubules – which transport proteins + which way:

Back 133

to the plus end (kinesin) or the minus end (dynein)

Front 134

the minus ends of most microtubules of a cell originate from:

Back 134

the same region of the cell, known as the centrosome, or the microtubule organizing center(MTOC) of the cell

Front 135

Centrioles are small cylindrical structures composed of:

Back 135

two pairs of nine triplet microtubules

Front 136

Thin filaments(microfilaments) are composed Of:

Back 136

G-actin monomers that have assembled (a process requiring AtP) in a polarized fashion into two chains of F-actinfilaments coiled around each other,

Front 137

15% of the protein content of most cells – which protein:

Back 137

Actin

Front 138

Actin grows at which end:

Back 138

the lengthening of the filament occurs at a faster pace at the plus end

Front 139

the principal classes of intermediate filaments are:

Back 139

keratins, desmin, vimentin, neurofilaments, and nuclear lamins

Front 140

The nucleus contains three major components:

Back 140

-chromatin, the cell’s genetic material;
-nucleolus, where ribosomal RnA (rRnA) is synthesized, and ribosomal subunits are assembled;
-nucleoplasm,

Front 141

nuclear lamina location + made by:

Back 141

an interwoven meshwork of specialized intermediate filaments
- located at the periphery in the nucleus.

Front 142

nuclear lamins function:

Back 142

organize and support the perinuclear chromatin and the inner nuclear membrane,
- assist in the reassembly of the nuclear envelope after cell division

Front 143

outer nuclear membraneis continuous with:

Back 143

the rough endoplasmic reticulum, and its cytoplasmic surface is enmeshed in a network of vimentin(intermediate filaments)

Front 144

nuclear pore complex - the three sets of rings layered above one another are named:

Back 144

the cytoplasmic ring, luminal spoke ring,and nuclear ring.

Front 145

nuclear pore complex size:

Back 145

- (100 to 125 nm in diameter)

Front 146

suspended from the nuclear ring is what + end of it is called:

Back 146

the nuclear basket, the end of the nuclear basket is called - Distal ring

Front 147

which substances can enter via the nuclear pore complex :

Back 147

substances larger than 11 nm cannot pass through the pore in either direction without engery

Front 148

euchromatin wrapped around beads of :

Back 148

nucleosomes, to be transcripted into RnA

Front 149

each nucleosome is an octomer of proteins known as:

Back 149

histones(H2A, H2B, H3, and H4) wrapped with two complete turns of DnA representing about 150 nucleotide pairs.

Front 150

the linker DNAis how long + location:

Back 150

about 200 base pairs that occupy the space between neighboring nucleosomes.

Front 151

RNA has uracil rather than:

Back 151

Thymine

Front 152

Messenger RNA(mRNA) catalyzed by:

Back 152

RnA polymerase ii

Front 153

Transfer RNA(tRNA) catalyzed by:

Back 153

RnA polymerase iii

Front 154

main enzyme in transcription:

Back 154

polymerase ii

Front 155

the nucleolus observed only during + structure:

Back 155

interphase, is a highly basophilic RnA and protein-rich structure present within the nucleus

Front 156

checkpoints during cell devision:

Back 156

-Start/restriction point in gap 1
-G2/Mcheckpoint,
-Metaphase/anaphase checkpoint

Front 157

Start/restriction point in gap 1(checkpoint) function:

Back 157

which permits chromosome duplication and the entry into gap 2;

Front 158

G2/M checkpoint function:

Back 158

, which initiates the condensation of chromosomes and other events necessary to permit the beginning of mitosis; and

Front 159

Metaphase/anaphase checkpoint function:

Back 159

which permits the separation of sister chromatids, the completionof the M phase, and the process of cytokinesis

Front 160

G1 cyclins – name/function:

Back 160

cyclin D, early in the g1phase, binds to cDK4 and to cDK6.

Front 161

G1/S cyclins – name/function:

Back 161

cyclin e is synthesized late in the g1 phase and binds to cDK2.
these three complexes permit the cell to enter and progress through the s phase.

Front 162

S cyclins – name/function:

Back 162

cyclin A binds to cDK2 and cDK1 forming '
complexes that permit the cell to leave the s phase and enter the g2phase and induce the formation of cyclin B.

Front 163

M cyclins – name/function:

Back 163

cyclin B binds to cDK1,
and this complex allows the cell to leave the g2phase and enter the M phase.

Front 164

cyclin A – binds with what + when:

Back 164

cDK2+ cDK1 : S -> G2 phase + cyclin B

Front 165

cyclin B – binds with what + when:

Back 165

cDK1 : G2 -> M phase

Front 166

cyclin D – binds with what + when:

Back 166

cDK4 + cDK6 : G1 phase

Front 167

cyclin E – binds with what + when:

Back 167

cDK2 - G1/S->S phase

Front 168

interphase is subdivided into three phases:

Back 168

G1(gap) , S (synthetic) phase and G2 phase,

Front 169

G1(gap) phase – what happens:

Back 169

when the cell prepares to synthesize DnA;

Front 170

S(synthetic) phase – what happens:

Back 170

when DnA is replicated;

Front 171

G2 Phase – what happens:

Back 171

when the cell prepares for the mitotic event

Front 172

At the conclusion of mitosis the newly formed daughter cells enter:

Back 172

the g1phase of the cell cycle, a stage characterized by the synthesis of the regulatory proteins necessary for DnA replication

Front 173

first event in MIToSIS:

Back 173

karyokinesis, the division of the nuclear material, and is followed by cytokinesis, cytoplasmic division

Front 174

Mitosis stages:

Back 174

prophase, prometaphase, metaphase, anaphase, and telophase

Front 175

two sister chromatids held together at the:

Back 175

centromere by cohesin(a chromatin binding protein),

Front 176

mitotic spindle apparatus comes when?

Back 176

prophase – its done in prometaphase

Front 177

phosphorylation of the nuclear lamins leads to + when:

Back 177

nuclear envelope disappears – prometaphase

Front 178

Anaphase begins when the:

Back 178

cohesion proteins that attach the sister chromatids to each other at the centromere disappear, and the sister chromatids (chromosomes) start to be pulled apart.

Front 179

chromosome migration – how:

Back 179

the depolymerisation of the mitotic spindle microtubules in association with dyneinis

Front 180

cleavage furrow develops when?

Back 180

anaphase

Front 181

the intrinsic pathway of apoptosisis initiated by:

Back 181

mitochondria that release cytochrome c into the cytosol.

Front 182

cytochrome c binds with + then what:

Back 182

apoptotic procaspase-activating adaptor protein(Apaf1), which combines with other Apaf1 units to form a wheel-like apoptosome that induces a caspase cas cade resulting in programmed cell death.

Front 183

nonpolar molecule. – location of receptor:,

Back 183

(hydrophobic ) -> intracellular or intranuclear (e.g., steroid hormone),