Lecture 17 Flashcards

The Extracellular Matrix (43 cards)

1
Q

What is the ECM?

A

The extracellular matrix (ECM) is the non-cellualr component present within all tissues and organs.

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2
Q

What does the ECM bear?

A

The ECM directly bears mechanical stresses of tension and compression

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3
Q

Proteins from the ECM are _____?

A

Proteins from the ECM are secreted.

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4
Q

What is the function of the ECM?

A

The ECM is a large network of proteins and other molecules that surround, support and give structure to cells and tissues.

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5
Q

What are some examples of proteins found in the ECM?

A
  • Collagen
  • Proteoglycans
  • Laminin
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6
Q

What are the three proteins that make the ECM?

A
  • Proteoglycans, fibrous proteins, and glycoproteins.
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7
Q

Examples of proteoglycans and GAGs?

A
  • Hyaluronan/Hyaluronic acid
  • Perlecan
  • Decorin
  • Aggrecan
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8
Q

Examples of fibrous proteins?

A
  • Type IV collagen
  • fibrillar collagen
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9
Q

Examples of glycoproteins?

A
  • Laminin
  • nidogen
  • fibronectin
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10
Q

Differences between proteoglycans and glycoproteins?

A

Proteoglycans have huge oligosaccharide chains, whereas glycoproteins generally contain relatively short oligosaccharide chains.

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11
Q

What are GAGs?

A

Glycosaminoglycans (GAGs) are unbranched polysacharide chains made of repeating disaccharide units.

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12
Q

What is hyaluron?

A

Hyaluronan (hyaluronic acid/hyaluronate) is the simplest of the GAGs. It is made out directly from the cell surface by and enzyme complex embedded in th plasma membrane.

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13
Q

What is the function of hyaluronan?

A

Hyaluronan is a space filler and compression protector.

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14
Q

One side chain of a proteoglycan must be…?

A

At leasrt one of the sugar side chains of a proteoglycan must be a GAG.

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15
Q

Where does o-linked glycosylation occur?

A

O-linked glycoylation occurs at the Golgi

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16
Q

Where does GAG addition occur?

A

The addition of GAG happens outside of the cell.

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17
Q

Glycosaminoglycans absorb…?

A

Glycosaminoglycans absorb large quantities of water, causing them to swell.
- The sugars absorb a lot of water

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18
Q

What is an example of fibrous proteins?

A

Collagen is an example of fibrous protein

19
Q

Collagen molecules are…?

A

A collagen molecule is a long, stuff, triple stranded helical structure in which three collagen polypeptide chains called a-chains bind.

20
Q

Collagen molecules assemble into?

A

Collagen molecules assemble at the ECM into thick, long collagen fibres, which we use structurally.
- Fibres are made of fibrils (not cylindrical)

21
Q

Formation of procollagen molecule occurs where?

A

Collagen molecule formation occurs in the ER lumen

22
Q

Collagen fibril and fiber formation occurs where?

A

The formation of collagen molecules, fibrils, and fibers occurs after the secretion from the cell.

23
Q

How do collgane fibres assemble?

A

Collagen fibers assemble by cross linking collagens
- They can be intermolecular (within molecule) or intramolecular (between molecules)

24
Q

Stretching and collagen fibrils, defects?

A

Collagen fibrils form structures that resist stretching forces.
- Defects in the structure or processing of the protein collagen affects the elasticity of the connective tissue.

25
Collagens fit into what two main categories?
Not all collagens will form giant fibrils whilst some will be fibril-associated collagens.
26
Matrix glycoproteins are what kind of proteins?
Many matrix glycoproteins are large scaffold proteins (bind many things at once, stabilizing them) that are containing mutliple copies of specific protein-interaction domains.
27
Features of matrix glycoproteins?
- multiple domains - bind to other matrix molecules and cell receptors - They have cross linking functions
28
Glycoprotein domains?
Glycoproteins have multiple domains and crosslink other matrix molecules and cell receptors. - Repeat domains are a piece of proteins that forms a distinct shape and has a distinct function.
29
What is fibronectin?
Fibronectin is an example of a glycoprotein: - Fibronectin is a dimer joined by disulfide bonds
30
What is laminar and what is it composed of?
Laminin is a large glycoprotein composed of three chains. - It links the ECM to cell surface receptors.
31
What is the role of integrins?
Integrins connect the ECM to the cytoplasm - they have two conformations - they are dimers - the cytoplasmic region binds talin
32
What does the ECM provide for the cell?
The ECM provides essential physical scaffolding for the cell.
33
What are integrins?
Integrins are transmembrane heterodimers that link ECM to actin cytoskeleton
34
Extracellular poritons of integrin?
The extracellular portions of integrin bind ECM proteins like fibronectin or collagen
35
Intracellular integrin tail role?
The intracellular integrin tails bind to a complex of adaptor proteins that link the actin cytoskeleton like talon and viniculin
36
Integrin conformations?
Integrins switch brtween active and inactive conformations
37
Active integrin?
Binding sites are exposed
38
Inactive integrin?
Bidning sites are hidden
39
Integrins can be activated how?
Integrins can be activated from the otuside or from the inside: 1. binding to a ECM substrate 2. Binding to talin in the inside
40
What happens to epithelia without integrins?
Epithelia without integrins detach from the basal lamina - We see this in flies that end up with a bubble strcutre on their wings
41
What do integrin clusters form?
Integrins cluster to form strong and dynamic connections to the ECM called focal adhesion sites.
42
How dynamic are integrins?
Integrins are very dynamic! They form clusters called focal adhesion sites
43
What are focal adhesions?
Focal adhesions are large macromolecular assemblies that form mechanical links between intracellular actin bundles and the ECM. - Talin and viniculin are the main components.