CB18: Proteins of ECM Flashcards

1
Q

How many types of collagen are there?

A

28

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2
Q

What are the 4 most common types of collagen & where are they found?

A

Type I: found in skin, tendons & bones.
Type II: found in cartilage.
Type IV: found in basement membranes.
Type XI: found in bones & skin.

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3
Q

What is laminin?

A

A sheet-like network protein found in basement membranes that forms complexes with collagen type IV.

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4
Q

What is tenascin?

A

A protein that regulates tissue interactions during foetal development & oncogenesis.

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5
Q

What is fibronectin?

A

A protein involved in the guidance of migrating cells during embryogenesis & adhesion of cells to matrix.

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6
Q

What is 1 collagen molecule made of?

A

3 polypeptide alpha chains with glycine as the third amino acid.

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7
Q

How are collagen fibres made from collagen molecules?

A

Collagen molecules form covalent cross-links between lysine residues of collagen molecules. This forms collagen fibrils, which are then bound together to form collagen fibre.

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8
Q

How do collagen fibres form intermolecular cross-links?

A

The enzyme lysyl oxidase deaminates some lysines & hydroxylysines. This forms highly reactive aldehyde groups which can react with other lysines/hydroxylysines to form covalent bonds.

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9
Q

Where are intermolecular cross-links formed in collagen fibres?

A

In non-helical segments at the end of the molecules.

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10
Q

What is the role of proteoglycans in cartilage?

A

To resist compressive forces & allow rapid diffusion of nutrients, metabolites & hormones between blood & tissue cells.

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11
Q

What do proteoglycans do

A

They form ground substance to embed fibrous proteins.

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12
Q

How do proteoglycans give ground substance its gel-like consistency?

A

Proteoglycans are negatively charged so they attract cations and water is drawn in by osmosis, giving ground substance its gel-like consistency.

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13
Q

What are proteoglycans composed of?

A

Glycosaminoglycans linked to a core protein. They associate with each other & other components of ECM.

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14
Q

What are glycosaminoglycans?

A

They are polysaccharides composed of repeating disaccharides. They have sulphate/carboxyl groups so they are negatively charged.

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15
Q

What is the composition of the disaccharides in glycosaminoglycans?

A
  • First disaccharide: amino sugar.
  • Second disaccharide: uronic acid.
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16
Q

What are the characteristics of hyaluronan?

A
  • It’s a special type of GAG that is not covalently linked to a core protein. It is not sulphated.
17
Q

What is hyaluronan composed of?

A

Identical disaccharides.

18
Q

What’s the size of hyaluronan?

A

25 000 monomers which is huge.

19
Q

What is hyaluronan used for?

A

It facilitates cell migration during development & repair. It’s used in joint fluid & wound healing.

20
Q

What are the 4 main groups of GAGs?

A
  • Hyaluronan (special type of GAG)
  • Chondroitin sulphate & dermatan sulphate
  • Heparan sulphate
  • Keratan sulphate
21
Q

How does the structure of elastin allow it to stretch & relax?

A

Elastin is made of hydrophobic molecules that form extracellular extensible fibres. They are arranged in discontinuous sheets in the ECM.

22
Q

How are proteins of the ECM used in soft tissues?

A

Soft tissues have little ECM so they can remain soft.How are proteins of the ECM used in

23
Q

How are proteins of the ECM used in bone?

A

ECM proteins become calcified using calcium phosphate crystals to make it rock-hard.

24
Q

How are proteins of the ECM used in tendons?

A

ECM proteins are rope-like to give tendons an enormous tensile strength + flexibility.

25
Q

How are proteins of the ECM used in the vitreous humour of the cornea?

A

ECM proteins become transparent & soft.

26
Q

How are proteins of the ECM used in cartilage?

A

ECM proteins are tough & shock-absorbent.