extracellular matrix Flashcards

extracellular matrix molecular structure: list the major components of the ECM, summarise their molecular characteristics and functional specialisation

1
Q

properties of soluble extracellular matrix

A

contains large proteins, modular architecture, multi-adhesive so multifunctional

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2
Q

components of soluble extracellular matrix

A

glycoproteins, proteoglycans and glycosaminoglycan

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3
Q

examples of glycoproteins in soluble extracellular matrix

A

laminins, fibronectin

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4
Q

examples of proteoglycans in soluble extracellular matrix

A

decorin, aggrecan

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5
Q

where is laminin located

A

only in basement membranes as a sheet-like network

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6
Q

structure of laminin

A

3 a, B and y chains cross-shaped, forming a “coiled-coil”, with globular regions at the N-terminus

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7
Q

properties of laminin

A

very large and multi-adhesive, as different regions have different binding capacities with cell surface receptors

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8
Q

self-association with basement membrane

A

laminins, basement membrane matrix, collagen IV, proteoglycans

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9
Q

genetic diseases caused by laminin mutation

A

congenital muscular dystrophy. epidermolysis bullosa

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10
Q

chain mutation causing congenital muscular dystrophy

A

absence of a2 in laminin 2

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11
Q

consequences of congenital muscular dystrophy

A

weakness, joint deformities

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12
Q

fibronectin location

A

insoluble fibrillar matrix or soluble plasma matrix

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13
Q

fibronectin structure

A

V-shaped; 2 chain dimer connected by disulphide bridge

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14
Q

fibronectin derivation

A

derived from one gene with alternate mRNA splicing

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15
Q

properties of fibronectin

A

large and multi-adhesive, interacting with cell surface receptors and other matrix molecules

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16
Q

fibronectin function

A

regulates cell adhesion, migration in embryogenesis, tissue repair and wound healing

17
Q

fibronectin in wound healing

A

forms mechanical continuum between EC collagen fiber with IC actin using integrin and adapter protein within the membrane

18
Q

fibronectin necessity

A

no known mutations so essential for life

19
Q

what is the fibronectin binding site for integrin

A

RGD molecule

20
Q

define proteoglycan

A

core protein with 1 or more glycosaminoglycan chain covalently attached via link tetrasaccharide

21
Q

define glycosaminoglycan

A

long, unbranched sugars with repeating disaccharides; 1 sugar is always amino; high -ve charge as sulfated/carboxylated

22
Q

what do glycosaminoglycans form and significance

A

hydrated gels which occupy large volumes so are resistant to compression

23
Q

families of proteoglycans

A

basement membrane, aggregating, small leucine-rich, cell surface

24
Q

what proteoglycan is located at the basement membrane

A

perlecan

25
Q

what proteoglycan is aggregating

A

aggrecans

26
Q

what proteoglycan is small leucine-rich

A

decorin

27
Q

what proteoglycan is located at the cell surface

A

syndecans I-IV

28
Q

4 regions on proteoglycans

A

hyaluron, chondroitin sulfate/dermatan sulfate, heparan sulfate, keratan sulfate

29
Q

hyaluron: structure, location of synthesis and properties

A

no core protein - just glycosaminoglycan chain; synthesised at cell surface not ER/Golgi; unsulfated and can be very large

30
Q

decorin: function and absence

A

small; binds to collagen fibres; regulates size and arrangement of collagen fibre size; absence causes fragile skin and reduced tensile strength

31
Q

what is embedded in the network of proteoglycans

A

type III cartilage matrix

32
Q

which proteoglycan is abundant in hyaline cartilage

A

aggrecan

33
Q

what regions are present in aggrecan

A

chondroitin sulfate and keratin sulfate

34
Q

consequence of presence of negative chondroitin sulfate and keratin sulfate in hyaline cartilage

A

attracts osmotically active cations e.g. Na+, meaning large amounts of water retained, forming hydrated gel which, under compression, water is forced out from, before returning after compression relieved; cushioning effect at long bone ends

35
Q

composition of aggrecan aggregates

A

aggrecan, hyaluronan and link protein