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Cell Bio (BIOL 4004) > Exam 3 pt 2 > Flashcards

Exam 3 pt 2 Flashcards

1
Q

epithelial cells rely

A

on cell-cell junctions

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2
Q

connective tissue cells rely on

A

cell matrix junctions

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3
Q

tight junctions have _ and function to _

A

no resistance to stress and prevent leaking

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4
Q

intracellular domains of transmembrane adhesion linked to _ proteins are while extracellular domains are linked to

A

linked to cytoskeletal filaments, structures outside of the cell

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5
Q

superfamilies of adhesion proteins

A
  • integrins
  • cadherins
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6
Q

cadherins for _ via _

A

cell cell junctions via actin adherens junctions or intermediate filament desmosomes

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7
Q

integrins form _ via

A

cell matrix junctions (to ECM) via actin linked cell matrix junctions or intermediate filament hemidesmosomes

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8
Q

all cadherin family members

A

have several copeies of the extracellular adherin domain

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9
Q

in cadherins, adjacent domains are linked by

A

flexible hinges

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10
Q

classical cadherins have

A

closely related sequences in their intracellular and extracellular domains

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11
Q

nonclassical cadherins are

A

are more distantly related in sequence

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12
Q

intracellular domains of cadherin are

A

more diverse because IC domain interact w many unique things

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13
Q

the _ of cadherins interact in the _

A

amino termini of cadherins interact in the extracellular space between adjacent cells

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14
Q

how do cadherins bind

A
  • end domains of cadherin contain a knob and pocket
  • knob of one cadherin insert into pocket of another
  • distance between cells determined by structure of cadherins
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15
Q

cadherin interactions are regulated by

A

extracellular Ca levels

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16
Q

how are cadherin interactions regulated

A

binding of Ca to hinge regions prevents EC domains from flexing, resulting in a slightly curved rod
* without Ca, hinges are flexible and the cadherin domains become floppy
* w/o Ca, reduced affinity between cadherins

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16
Q

how are cadherin interactions regulated

A

binding of Ca to hinge regions prevents EC domains from flexing, resulting in a slightly curved rod
* without Ca, hinges are flexible and the cadherin domains become floppy
* w/o Ca, reduced affinity between cadherins

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17
Q

cadherins bind to each other with

A

low affinity ( weak bonds)

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18
Q

how do cadherins form a strong junction

A

clusters of cadherins on one cell bind to clusters of cadherins on another
* accumulation of many weak bonds form velcro effect

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19
Q

cell sorting is mediated by

A

cadherins

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20
Q

cell sorting is mediated by

A

cadherins

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21
Q

cell sorting by cadherins explained

A

cell sorting recognize based on type and level of cadherin expression
* same cadherins stay together, more expression make inner layer called primary ball which has tighter interactions

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22
Q

_ is important for developmet

A

differential expression of cadherins

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23
Q

switching off of _ can allow cells to dissociate and form migrating cells

A

E-caderin

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24
Q

mutations that disrupt _ are found in cancer cells

A

production of E cadherins

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25
Q

in adherens unctions,

A

the intracellular domains of cadherins are indirectly linked to actin filaments

proteins in between them that link the two

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26
Q

adhesion belt

A

networks of actin filaments of adjacent cells connected via adherens juctions, located just beneath the apical surface of an epithelium

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27
Q

contraction of adhesion belt

A

provides the force required to fold epithelial sheets during development
* invagination pinches off to form tubes, vesicles and other structures

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28
Q

desmosomes are

A

clusters of non classical cadherins forming spot like welds that link intermediate filaments networks of adjacent cells

snaps NOT velcro

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29
Q

desmosomes are

A

clusters of non classical cadherins forming spot like welds that link intermediate filaments networks of adjacent cells

snaps NOT velcro

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30
Q

plakoglobin and plakophilin are used

A

cadherins linking to IFs

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31
Q

tight junctions enable _ by

A

unidirectional transport, by preventing molecules from passing between cells and the movement of transporters between apical and basaolateral domains

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32
Q

tight junctions form seals between

A

adjacent epithelial cells

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33
Q

in freeze-fracture, tight junctions

A

appear as branching network of sealing strands encircling the apical membrane

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34
Q

structure of tight junctions

A
  • sealing strans of occludin and claudin proteins extracellular domains adhere and bring the lasma membranes into close proximity
  • makes a tight junction
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34
Q

structure of tight junctions

A
  • sealing strans of occludin and claudin proteins extracellular domains adhere and bring the lasma membranes into close proximity
  • makes a tight junction
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35
Q

tight junctions are composed of three types of transmembrane proteins

A

claudin, occludin, tricellulin

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36
Q

claudin

A
  • most abundant isoform
  • essential for formation and function of tight junctions
  • losds is fatal
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37
Q

occludin is important

A
  • important for limiting the permeability of tight junctions
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38
Q

tricellulin is required

A

to seal membranes and prevent paracellular leakage at the junction points between three cells

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39
Q

ZO proteins

A
  • bind to the cytoplasmic domains of adhesion proteins
  • function as scaffold proteins that provide a structural support on which the tight junction is built
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40
Q

gap junctions form

A

direct passageways between cells

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41
Q

gap junctions structure

A
  • 6 transmembrane **connexin proteins ** assemble into a hemichannel connexons
  • connexons of two adjacent cells align to form an aqueous channel connecting the cytosols of the cells
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42
Q

size of gap junctions vary

A

with the number of connexons in the cluster pairs that form gap junctions

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43
Q

connexons can be

A

homomeric or hetromeric

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44
Q

regulation of gap junctions

A
  • switch between open and closed states in response to many things
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45
Q

turnover of gap junctions

A
  • new connexons are added to the periphery of a gap junction
  • old connexons are removed from the center
  • very rapid turnover rate
  • before they are connexon, they are unpairs hemichannels
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46
Q

gap junction role in muscle

A

electrically couple cardiac and smooth muscle cells so there is no delay and there is synchrony (ex heart beat)

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47
Q

selectins are

A

cell surface, carbohydrate binding proteins with a conserved lectin domain

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48
Q

selectins are

A

cell surface, carbohydrate binding proteins with a conserved lectin domain

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49
Q

L selectin are found in

A

white blood cells

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50
Q

emigration of white blood cells at sites of inflmmation

A
  1. cytokines are release
  2. epithelial cells express E selectin
  3. rolling: selectin binds to carbohy on leukocytes weakly so that the leukocyte can roll along the vessel wall
  4. adhesion integrinds bind to ICAMs and the attachement of leuk to epith cell is stronger
  5. leuk can stop rolling and squeeze through in between epith cells to escape
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51
Q

Tissues are composed of

A

cells and the ECM

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52
Q

Components of ECM

A
  1. Fibers (insoluable): Collogen, Elastic
  2. Ground Substance (soluable): Glycosaminogllycans, Proteoglycans, Multi domain glycoproteins
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53
Q

Glycosaminoglycans are

A

unrbanched polysaccharide chains composed ofo a repeating disaccharide units
* very high negative charge, causing sugars to be repealed by each other and spread out and take up a lot of volume

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54
Q

GAGs negative charges…

A

attract positive ions and water, so they form hydrated gels that resist compression

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55
Q

hyaluronan

A

a unique GAG that is v large and has no sulfated sugars and is not linked to a protein core

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56
Q

proteoglycans are composed of

A

GAG chains covalently linked to a core protein
* core protein and GAG chains point out like a bristles of a straw cleaner

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57
Q

proteoglycan synthesis

A
  • core protein is synthesized by membrane bound ribosomes
  • in the golgi, linkage tetrasaccharide is attached to a serine side chain on the core protein
  • GAG residues are added to the tetrasaccharide one sugar at a time
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58
Q

decorin

A

proteoglycan that has one GAG, binds to collagen fibrils and regulates their assembly

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59
Q

aggrecan

A

proteoglycans that has a lot of GAGs, main proteoglycan in cartilage

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60
Q

proteoglycans can regulate

A

the activities of secreted proteins by binding to the secreted signal molecules and regulating their diffusion through the matrix

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61
Q

cell surface proteoglycans

A

integral components of the plasma membrain, core protein is inserted across the plasma membrane or attached via a GPI anchor

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62
Q

_ is the most abundant protein in animals

A

collegen

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63
Q

collegen molecules structure

A
  • made up of three alpha chains wound around one another in a ropelike superhelix
  • alpha chains are made up of a series of triplets Gly-x-x
  • glycine is small so the alpha chains are closely packed
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64
Q

type one collagen are found in the

A

skin and bones

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65
Q

collagen fibrils are formed by

A

collagen molecules aligned head to tail in overlapping rows

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66
Q

collagen fibers are

A

bundles of collagen fibrils

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67
Q

fibral associated collagens

A
  • the helical structure of alpha chains are interupted by non helical domains
  • more flixible that fribrillar collagens
  • kinks of the molecules allow it to form attaches to the ECM
68
Q

network forming collages

A
  • do not form fibrils
  • form networks instead
69
Q

network forming collages

A
  • do not form fibrils
  • form networks instead
70
Q

what types of collegens dont form fibrils

A
  • fibril associated collagens (type 9)
  • network forming collagens (type 4)
71
Q

elastic fibers structure

A
  • elastin core
  • periphery made of microfibrils that provide the scaffold for elastin
72
Q

elastin structure

A
  • alternating hydrophilic and alpha helixes
73
Q

mutations in _ results in _ syndrome which is a relatively common tissue disease

A

fibrillin, Marfan’s syndrome

causes lens displacement

74
Q

mutations in _ results in _ syndrome which is a relatively common tissue disease

A

fibrillin, Marfan’s syndrome

causes lens displacement

75
Q

elastic fibers form _ which allow

A

coils which allow the fibers to stretch under stress

76
Q

elastin molecules are held together by

A

linker proteins

77
Q

multi domain glycoproteins

A
  • have multiple binding sites
  • function to organize matrix, attach cells to the ECM or guide cell movements in developing tissues
78
Q

fibronectin structure

A
  • composed of two very large similar subunits held together by disulfide bonds at c termini
  • each subunit is folded into multople functionally distinct domains seperated by flexible hinge regions

type of multidomain glycoprotein

79
Q

fibronectin structure

A
  • composed of two very large similar subunits held together by disulfide bonds at c termini
  • each subunit is folded into multople functionally distinct domains seperated by flexible hinge regions

type of multidomain glycoprotein

80
Q

RGD

A

tripeptide repeat that is located in the type 3 fibronectin repeats, binds to integrins on the surface of the cell

81
Q

binds to integrins on the surface of the cell

A

tripeptide RDG

82
Q

insoluable fibernecton fibrils are formed in th eECM when

A

dimers are cross linked by additional disulfide bonds at the surface of cells (ex. with integrins)

83
Q

when fibronectin molecules linked to actin cytoskeleton via integrins are stretched…

A

hidden binding sites ar exposed which allows them to bind to other fibronectin molecules

84
Q

fibrils are only assembles _ because _

A

assembeled when needed because stretch is required for assembly

85
Q

the basal lamina is

A

tough flexible sheet of specialized ECM

86
Q

the basal lamina underlies

A

epithelial tissues, directly surround muscle, adipocytes and schwann cells, form part of the filteration barrier in kidney cells

87
Q

components of the basal lamina

listed

A
  • laminin
  • type IV collagen
  • nidogen
  • perlecan
88
Q

laminin is

A

the primary organizer of the basal lamina

89
Q

laminin structure

A
  • composed of three chains (alpha, beta and gamma) arranged as an assymetric cross held together by disulfide bonds
  • display binding sites for cell surface receptors and other components of the basal lamina
90
Q

laminin heterotrimers require _ to assemble into _

A

require cell interaction to organize into a orderly sheet

91
Q

type 4 collagen molecules

A

Network-forming collagen essential for the formation of the basal lamina, it forms a flexible, felt-like network that gives the basal lamina its tensile strength

92
Q

Perlecan

A

Proteoglycan which links the laminin and type IV networks of the basal lamina

93
Q

Nidogen

A

Along with the proteoglycan perlecan, this protein functions to link the laminin and type IV collagen networks of the basal lamina

94
Q

assembly of basal lamina

A
  • laminin network forms the initial sheet by binding to the cell surface recetors integrin and dystroglycan
  • linkers perlecan and nidogen attach to the collagen IV network to the laminin network
95
Q

agrin

A

specialized junctional basal lamina contains agrin and directs the regenerating nerve and new AceCh receptors

96
Q

degradation of matrix is controlled by

A
  • local activation
  • secretion of inhibitors to protect other cells
  • surface receptor controlled

makes sure onlt the ECM needed is destroyed

97
Q

matrix metalloproteases

A

degrade matrix components, require Ca or Zn

98
Q

serine proteases

A

degrade matrix components, highly reactive serine in their active sites

99
Q

hemidesmosomes link

A

epithelial cells to the basal lamina

100
Q

intracellular attachment to keratins is mediated by the adaptor proteins

A

plectin and BP230

101
Q

Glanzmann’s disease

A

Disease caused by a deficiency in the b3 subunit of integrin, resulting in defective clotting and excessive bleeding

102
Q

Glanzmann’s disease

A

Disease caused by a deficiency in the b3 subunit of integrin, resulting in defective clotting and excessive bleeding

103
Q

Leukocyte adhesion deficiency

A

Disease caused by a deficiency in the b2 subunit of integrin, resulting in repeated bacterial infections

104
Q

integrin outside in activation

A

binding of external ligand to EC domain causes EC domain to unfold and straighten, IC domain move apart, talin binding site is exposed, IC binds to cytoskeleton

105
Q

integrin inside out activation

A

talin binds, EC domain unfolds and binds ECM component

106
Q

talin competes

A

with alpha subunit to bind on beta chain

107
Q

inside out activation depends on

A

intracellular regulator signals that stimulate the ability of talin and other proteins to interact with the beta chain of integrin

thrombin present -> Rap1 active -> talin interact w beta ch -> bind CS

108
Q

Junction which brings the plasma membranes of adjacent cells into close proximity, preventing the paracellular passage of most soluble molecules.

A

tight junction

109
Q

Junction which allows for the passage of small molecules between the cytosols of adjacent cells

A

gap junction

110
Q

A molecule consisting of a core protein with one or more attached GAG.

A

proteoglycan

111
Q

Fibrous protein, rich in glycine and proline that confers tensile strength to the extracellular matrix.

112
Q

Fibrous protein, rich in glycine and proline that confers tensile strength to the extracellular matrix.

A

anchorage dependent

113
Q

_ are the most negatively charged molecules in animals.

A

Glycosaminoglycans

114
Q

Members of the cadherin family function as the adhesion proteins in

A

both adherens junctions and desmosomes.

115
Q

Both _ have binding domains for the linkers perlecan and nidogen.

A

laminin and type IV collagen

116
Q

TRUE or FALSE: Unlike conventional ion channels, gap junctions are always in an open conformation.

A

False (Like conventional ion channels, gap junctions are not always open)

117
Q

_ is a unique GAG containing non-sulfated sugar residues.

A

Hyaluronan

118
Q

Type _ collagen is essential for the formation of the basal lamina.

119
Q

Mixtures of cells expressing two different cadherins will sort _ while mixtures of cells expressing different levels of the same cadherin will sort _

A

into two aggregates, into two layers of the same aggregate.

120
Q

P-selectin is displayed on the surface of

A

blood platelets and endothelial cells activated by inflammatory response

121
Q

Matrix molecules which display multiple binding sites for components of the ECM and cell surface receptors.

A

multi-domain glycoproteins

122
Q

Cadherins promote cell-cell interactions by

A

binding to cadherin molecules of the same or closely related subtype on adjacent cells.

123
Q

Proteoglycan can form

A

noncovalent attachments, via a linker protein, to hyaluronic acid to form large proteoglycan aggregates

124
Q

4 phases of cell cycle

A

M phase, G1 phase, S phase, G2 phase

125
Q

prophase

A
  • condensation of sister chromatids
  • mitotic spindle assembles
  • condensin complex forms
  • centrosome maturation
126
Q

prometaphase

A
  • nuclear envelope diassembles
  • chromatids attache to spindle
  • nuclear lamins phosphorylated
  • nuclear pore complexes are phosphorylated
  • formation of kineticore fiber
127
Q

metaphase

A
  • chromosomes align at metaphase plate
  • microtubles flux
    *
128
Q

anaphase

A
  • Poleward movement of chromosomes
  • M-Cdks active
  • Securin is ubiquitylated by APC/C
129
Q

telophase

A
  • mitotic spindle disassembles
  • nuclear envelope reforms
  • Gene transcription resumes
130
Q

cytokinesis

A
  • cytoplasm division
  • Midbody forms
  • RhoA activates formins
131
Q

cytokinesis

A
  • cytoplasm division
  • Midbody forms
  • RhoA activates formins
132
Q

G1/S checkpoint aka start checkpoint

A
  • make sure favorable conditions, cell procede S
  • or pause in G1 or go to G0
133
Q

G2/M checkpoint

A
  • to eneter mitosis
  • cellls not pass unless DNA repolication is complete and all DNA damage repair
134
Q

metaphase to anaphase transition

A
  • cells not pass unless chromosomes are properly attached to mitotic spindle
135
Q

Cdks are regulated by

A

cyclins. Cdks must be bound to cyclin to be able to phosphorylate proteins

136
Q

_ cycle active during G1

A

G1/S cyclin

137
Q

cylclin active during S, G2, part of M

138
Q

how does cyclin activate Cdk

A
  • binding partially activates by pulling T loop away from active site
  • full activation requires CAK to phosphorylate an amino acid near Cdk active site
139
Q

Wee1

A

inhibits Cycl-Cdk

140
Q

Cdc25 phosphatase

A

activates cyclin-Cdk

141
Q

APC/C

A
  • destroy S amd M cyclin to be able to go through metaphase ot anaphase checkpoint
  • allows completion of M phase and cytokinesis
  • targets securin that holds together mitotic spindle
142
Q

APC/C is activated by

A
  • mid mitosis by Cdc20
  • late mitosis by Cdh1
143
Q

SCF is _ during the cell cycle

A

constant but state of target changes

144
Q

SCF

A

ub Cdk inhibitors in late G1
* triggers DNA replication
* activated by association with F box proteins
* only recognizes phosphorylated proteins

145
Q

Pre-RC

A

formed in late mitosis to early G1, called the licensing of replication
* disassembled with DNA synthesis starts in S phase
* Pre-RC cannot reassemble until the next G1 phase
* makes sure DNA Is only replicated once

146
Q

assembly of Pre-RC

A

ORC bind to OR and Cdc6 and Cdt1 help to bring DNA helicases to site

147
Q

assemble of PreRC inhibited by _ and stimulated by _

A

Cdk, APC/C

148
Q

Pre-Rc disassembled during

A

S phase
* S Cdk phosphorylates and ibhibits the ORC and Cdc6 proteins

149
Q

PreRCs assemble in

A

early G1
* APC/C triggers destruction of Cdt1 inhibitor germinin
* inactivation of Cdks

150
Q

cohesion complex made of

A

Smc3 and Smc1 and glues together sister chromatids

151
Q

early mitosis is triggered by

A

abrupt increase in M-Cdk activity at G2/M checkpoint

152
Q

anaphase triggered by

A

activation of APC/C (inhibit S and M Cdks)
* degregation of securin and cyclins

153
Q

activation of M-Cdk

A
  • M-Cdk accumulates during G2 and M phase due to increased synthesis of M-cylin
  • M Cdk initially inactive due to phosphorylation of inhibitor sites by Wee1
  • M-Cdk activated by Cdc25
  • POsitive feedback increase M Cdk activation
154
Q

Centrosome duplication begins in

155
Q

resolution and condenstation of chromosomes in

156
Q

condensin complex triggered by

157
Q

maturation of chromosomes in

A

prophase

up nucleation of MT

158
Q

dynein motors role in centrosome speration

A

attach cell cortex to astral microtubles and pull centrosomes to opposite ends of chromosomes

159
Q

kinesin 5 motors centrosome speration

A

attach to interpolar microtubles and push centrosomes part

160
Q

minus ends kinesin 14 role in centrosome speration

A

attach to interpolar microtubles and pull centrosomes closer together

161
Q

nuclear lamins are phosphorylated in _ by _

A

in prometaphase by M-Cdk

162
Q

attachment of chromatids to kinetochore microtubles happens in

A

prometaphase

163
Q

separase cleaves

A

the Scc1 subunit of the cohesin complex

164
Q

MT attachement to kineticore mediated by

165
Q

MT attache to kineticore in

A

mid prometaphase, complete attachment complete in metaphase

166
Q

MT flux excert

A

force towards the poles

167
Q

as kinesine walk towards the plus ends of the MT,

A

the attached chromosome is pulled away from the pole

168
Q

sister chromatids freeing

A

before anaphase, securin binds to and inhibits a protease called seperase
* APC/C ub securin, activating seperase
* seperate cleaves Scc1 subunit of cohesin
* this frees the sister chromatids

169
Q

contractile ring assembles during

Cell Bio (BIOL 4004) (8 decks)

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