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CBIO3400 > The ECM > Flashcards

The ECM Flashcards

1
Q

contacts basal lamina

A

basal surface

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2
Q

basil lamina physical properties

A

very thin, tough flexible sheet

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3
Q

these rest on basal lamina foundation

A

columnar epithelia

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4
Q

two distinct basal lamiae form a tight barrier that limits:

A

diffusion (between blood and brain)

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5
Q

role basal lamina plays in tissue repair after wounding

A

cell adhesion

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6
Q

basal lamina cell adhesion after:

A

wounding

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7
Q

basal lamina functionally provide a surface for:

A

fibroblast migration

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8
Q

basal lamina composed of 4 major proteins:

A

Type IV collagen, Laminins, Perlecan, Nidogen

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9
Q

trimeric molecules with rodlike and globular domains that form a 2D network

A

Type IV collagen

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10
Q

family of multiadhesive cross-shaped proteins that form fibrous 2D network with Type IV collagen

A

Laminins

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11
Q

large multidomain proteoglycan that binds to and cross-links many ECM components

A

Perlecan

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12
Q

structure of collagen proteins

A

trimeric proteins

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13
Q

three collagen polypeptides form into:

A

triple helix

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14
Q

repeating sequence of collagen peptide

A

Gly - X - Y

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15
Q

collagen peptide sequence X and Y stand for:

A

proline and hydroxyproline (or lysine and hydroxylisine)

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16
Q

collagen peptide amino acid small enough to fit in center of triple helix

A

Gly

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17
Q

collagen triple helix monomer associate in this manner

A

head-to-head or tail-to-tail

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18
Q

collagen small globular domain at N-terminus forms:

A

tetramers

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19
Q

large globular domain at C-terminus forms:

A

dimers

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20
Q

collagen dimers and tetramers associate to form:

A

lattice

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21
Q

some collagen covalent crosslinking occurs between these domains

A

C-terminal globular domains

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22
Q

collogen mutations in Gly cause: (scientific and common name)

A

osteogenesis imperfecta (brittle bone disease)

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23
Q

mutation in Gly from brittle bone disease can disrupt:

A

collagen triple helix

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24
Q

brittle bone disease S/S

A

bones break from normal weight-bearing

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25
Q

deficiency in co-factor leads to scurvy

A

Vitamin C (ascorbic acid)

26
Q

enzyme type requires Vitamin-C

A

hydroxylase

27
Q

scurvy causes these to not be hydroxylated

A

prochains

28
Q

Scurvy: these do not form stable structures

A

collagen triple helices

29
Q

Scurvy: these physical body structures become fragile

A

blood vessels, tendons, and skin

30
Q

S/S of Alport Syndrome

A

progressive loss of kidney function, hearing loss, and blindness

31
Q

Alport Syndrome caused by mutations in these genes

A

COL4A5 (X-linked) and COL4A3/4 (autosomal)

32
Q

S/S of Collagen II mutants

A

shortened/deformed bones

33
Q

bones severly affected when embryos null of this

A

Perlecan

34
Q

fibronectan is present on:

A

fibroblasts

35
Q

normal fibroplasts adhere tightly because of:

A

fibronectan

36
Q

fibronectin is absent from surfaces of:

A

cancerous fibroblasts

37
Q

FN essential for these processes:

A

cell migration, differentiation, wound healing, (and clotting)

38
Q

fibronectin-cultured salivary glands undergo:

A

branching morphogenesis

39
Q

salivary gland culture with anti-Fibronectan Ab blocks:

A

branching

40
Q

structure of Fibronectin

A

dimer

41
Q

Fibronectan dimer polypeptide chains linked by:

A

disulfide bond (at C-terminus)

42
Q

Fibronectin connects to cytoskeleton via:

A

focal adhesions

43
Q

Focal adhesions are:

A

points of contact between cell and surface (ECM or tissue culture plate)

44
Q

form of fibronectin circulates in blood and functions in clotting

A

soluble form

45
Q

insoluble fibronectin assembles into fibrils only on:

A

surface of cells that can find to it

46
Q

Type III fibronectin repeats contain this sequence

A

Arg-Gly-Asp (RGD)

47
Q

Type III fibronectin repeats important for:

A

cell binding

48
Q

this caused when actin cytoskeleton transmits tension to fibronectin (stretching it)

A

binding sites exposed

49
Q

this forms after fibronectin binding sites exposed

A

fibronectin filament

50
Q

experiment proves RGD sufficient to mediate adhesion: different concentrations of:

A

synthetic peptides with various sequences

51
Q

experiment proves RGD sufficient to mediate adhesion: synthetic peptides crosslinked to:

A

antibody attached to dish surface

52
Q

to move through tissue cell has to grab and let go of:

A

ECM

53
Q

integrin outside-in activation controled by:

A

RGD peptide in extracellular domain

54
Q

integrin inside-out activation controled by:

A

regulatory molecules (like PIP2)

55
Q

integrin outside-in activation: in this type of confiuration intracellular domain of two subunits separate and expose binding site for talin on beta-subunit

A

unfolded, active configuration

56
Q

integrin outside-in activation: binding of talin triggers assembly of:

A

actin filaments anchored to integrin

57
Q

integrin outside-in activation: this exerts tension when extracellular domain binds ligand

A

cytoskeleton

58
Q

integrin inside-out activation: this can compete with alpha subunit

A

talin

59
Q

integrin inside-out activation: talin competes with alpha subunit for

A

beta subunit

60
Q

integrin inside-out activation: if this happens, integrin configuration forced to open

A

talin binds to beta subunit

61
Q

integrin inside-out activation: regulatory molecules (like PIP2) activates talin by:

A

increasing affinity for beta-subunit

62
Q

overall structure of insoluble fibronectin binding complex at cell membrane

A

CBIO3400 (8 decks)

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