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POM > Extracellular matrix > Flashcards

Extracellular matrix Flashcards

1
Q

What is the extracellular matrix?

A

A complex network of proteins and carbohydrates filling spaces between cells.

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2
Q

Key functions of extracellular matrix?

A

Provides physical support. Influences growth, adhesion and differentiation status of the cells and tissues with which it interacts.

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3
Q

What makes up connective tissue?

A

Collagens, multi adhesive glycoproteins and proteoglycans and ECM.

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4
Q

What is a the structure of a collagen molecule?

A

Made of 3 alpha chains forming a triple helix.

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5
Q

Why is every third amino acid in collagen glycine?

A

Glycine is the smallest amino acid. Allows for compact structure as it can occupy the interior.

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6
Q

Difference between pro collagen and collagen?

A

Pro collagen has non collagenous domains at n and c termini.

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7
Q

Why is vitamin c required for production of collagen?

A

Vitamin C is required for properly hydroxylated collagen which is needed for cross links. Proline and lysine need hydroxylation.

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8
Q

When is pro collagen converted to collagen?

A

In secretion of fibrillar collagens.

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9
Q

What is required for hydroxylation of collagen once its been secreted?

A

Vitamin C and Fe2+

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10
Q

What forms the cross links in collagen?

A

Lysine and hydroxylysine.

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11
Q

Explain the fibrillar collagen synthesis pathway?

A

Pro alpha chain synthesis. Hydroxylation and glycosylation occurs. Three of these form triple helix. Secretion out of cell. Cleavage of propeptides to form collagen. Assembled into fibril and then into fiber.

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12
Q

What causes fibrotic diseases such as liver cirrhosis?

A

Excess collagen production.

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13
Q

What is collagen type IV?

A

Network forming collagen.

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14
Q

Where is collagen type IV found?

A

Basement membranes.

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15
Q

What are ehlers–Danlos syndromes (EDS)?

A

Group of inherited connective tissue disorders whose symptoms include stretchy skin and loose joints.

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16
Q

What do fibril associated collagens do? Give an example?

A

Regulate organisation of collagen fibrils. Collagen type IX and XII.

17
Q

What occurs in Alport syndrome?

A

Mutations in collagen IV result in an abnormally split and laminated glomerular basement membrane.

18
Q

What are laminins?

A

Role in adhesion. Interacts with integrin and dystroglycan. Made up of alpha,beta and gamma chain.

19
Q

What is a fibronectin?

A

Glycoprotein dimer involved in cell adhesion, migration and wound healing.

20
Q

What links ECM and actin cytoskeleton of cell?

A

Integrins and fibronectin. Fibronectin is bound to collagen and integrin. Integrin binds to actin in cell.

21
Q

What are the two binding sites in fibronectin?

A

Collagen binding site and cell binding site (for integrin).

22
Q

Proteoglycan role?

A

Keeps cells hydrated and cushioned.

23
Q

Elastic fibre structure?

A

Elastin core and surrounding microfibrils rich in fibrillin.

24
Q

Elastin structure?

A

Alternating hydrophillic and hyrophobic domains. Crosslinking of lysine in hydrophillic domains.

25
Q

Proteoglycan structure?

A

Core proteins attached with glycosaminoglycan chains.

26
Q

Glycosaminoglycan chain structure?

A

Repeating disaccharides.

27
Q

What can increase the negative charge of GAG chains?

A

Sulfation or carboxylation.

28
Q

Glycosaminoglycan chain examples?

A

Hyaluronan, chondroitin sulfate, heparan sulfate and keratan sulfate.

29
Q

Where is aggrecan found?

A

Cartillage.

30
Q

What is aggrecan made up of?

A

Glycosaminoglycan chains.

31
Q

Cleavage of aggrecan causes what?

A

Osteoarthritis.

32
Q

How does aggrecan work?

A

High negative charge. Attracts cations like sodium. Draws in large amounts of water. This resists compressive load.

33
Q

What cleaves aggrecan?

A

Aggrecanases and metalloproteinases.

34
Q

What is marfan syndrome?

A

Mutations in the protein fibrillin-1. Features of Marfan’s syndrome are long slender limbs, long fingers, a predisposition to aortic ruptures and heart murmurs.

POM (41 decks)

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