The ECM Flashcards

(62 cards)

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
deficiency in co-factor leads to scurvy
Vitamin C (ascorbic acid)
26
enzyme type requires Vitamin-C
hydroxylase
27
scurvy causes these to not be hydroxylated
prochains
28
Scurvy: these do not form stable structures
collagen triple helices
29
Scurvy: these physical body structures become fragile
blood vessels, tendons, and skin
30
S/S of Alport Syndrome
progressive loss of kidney function, hearing loss, and blindness
31
Alport Syndrome caused by mutations in these genes
COL4A5 (X-linked) and COL4A3/4 (autosomal)
32
S/S of Collagen II mutants
shortened/deformed bones
33
bones severly affected when embryos null of this
Perlecan
34
fibronectan is present on:
fibroblasts
35
normal fibroplasts adhere tightly because of:
fibronectan
36
fibronectin is absent from surfaces of:
cancerous fibroblasts
37
FN essential for these processes:
cell migration, differentiation, wound healing, (and clotting)
38
fibronectin-cultured salivary glands undergo:
branching morphogenesis
39
salivary gland culture with anti-Fibronectan Ab blocks:
branching
40
structure of Fibronectin
dimer
41
Fibronectan dimer polypeptide chains linked by:
disulfide bond (at C-terminus)
42
Fibronectin connects to cytoskeleton via:
focal adhesions
43
Focal adhesions are:
points of contact between cell and surface (ECM or tissue culture plate)
44
form of fibronectin circulates in blood and functions in clotting
soluble form
45
insoluble fibronectin assembles into fibrils only on:
surface of cells that can find to it
46
Type III fibronectin repeats contain this sequence
Arg-Gly-Asp (RGD)
47
Type III fibronectin repeats important for:
cell binding
48
this caused when actin cytoskeleton transmits tension to fibronectin (stretching it)
binding sites exposed
49
this forms after fibronectin binding sites exposed
fibronectin filament
50
experiment proves RGD sufficient to mediate adhesion: different concentrations of:
synthetic peptides with various sequences
51
experiment proves RGD sufficient to mediate adhesion: synthetic peptides crosslinked to:
antibody attached to dish surface
52
to move through tissue cell has to grab and let go of:
ECM
53
integrin outside-in activation controled by:
RGD peptide in extracellular domain
54
integrin inside-out activation controled by:
regulatory molecules (like PIP2)
55
integrin outside-in activation: in this type of confiuration intracellular domain of two subunits separate and expose binding site for talin on beta-subunit
unfolded, active configuration
56
integrin outside-in activation: binding of talin triggers assembly of:
actin filaments anchored to integrin
57
integrin outside-in activation: this exerts tension when extracellular domain binds ligand
cytoskeleton
58
integrin inside-out activation: this can compete with alpha subunit
talin
59
integrin inside-out activation: talin competes with alpha subunit for
beta subunit
60
integrin inside-out activation: if this happens, integrin configuration forced to open
talin binds to beta subunit
61
integrin inside-out activation: regulatory molecules (like PIP2) activates talin by:
increasing affinity for beta-subunit
62
overall structure of insoluble fibronectin binding complex at cell membrane