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Biochemistry Year 2 > ECM > Flashcards

ECM Flashcards

1
Q

define the ECM

A

a complex network of secreted macromolecules in the extracellular space

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2
Q

The 4 categories of substances found in the ECM are

A
  • organic fibrillar matter
  • organic non-fibrillar matter
  • ions
  • water
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3
Q

organic fibrillar matter means

A

elastin, fibrillin, laminin, fibril-forming collagens

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4
Q

organic non-fibrillar matter means

A

fibronectin, proteoglycans, and lattice forming collagens

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5
Q

ions in the ECM are bound to

A

negatively charged GAG

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6
Q

ECM macromolecules are synthesized by

A

cells of mesenchymal origin such as: fibroblasts, sm cells, chondroblasts, osteoblasts, epithelial cells

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7
Q

fibronectin and laminin are

A

structural glycoproteins

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8
Q

collagens account for x% of total protein mass

A

30%

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9
Q

functions of the ECM

A
  • provide support and anchoring for cells
  • regulates polarity, differentiation, adhesion, migration, proliferation
  • acts as organiser for tissue growth, regeneration, maintenance of tissue structure
  • provides for inter-cellular exchange of metabolites, ion, water
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10
Q

the amount of ECM is a constant?

A

No, it varies depending on tissue types, developmental stage, pathological status

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11
Q

collagen is produced by

A

fibroblasts, osteoblasts, chondroblasts

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12
Q

the basic unit of collagen is

A

tropocollagen, which is a triple helix formed by 3 alpha polypeptide chains, enriched in glycine and Pro,HydroxyPro. They do not contain Cys, Trp

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13
Q

each tropocollagen alpha chain has x aa

A

1000

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14
Q

how many types of collagen are there

A

28

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15
Q

which direction is the helix turn of one of the tropocollagen alpha chains

A

left-handed helical structure

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16
Q

what direction is the helix turn once all three alpha chains are bound together

A

right handed triple helix

17
Q

the repeated aa sequence of collagens is

A

glycine, proline, hydroxyproline. (The side chains of the Pro/Hyp form lateral interactions with other triple helices)

18
Q

the H bonds in the CTH are between

A

NH2 group of Gly residues on one chain, and the CO group of the Pro/Hyp residues on neighbouring chains

19
Q

what collagen types are fibril forming

A

1, 2, 3, 5, 11

20
Q

most common types of collagen are

A

1: skin, tendon, heart, bone
2: cartilage
3: reticular CT
4: forms basal lamina, epithelium secreted layer of basement membrane
5: cell surfaces, liver, cornea, mucosa

21
Q

list the types of non-fibrillar collagens

A
  • network forming (4, 8, 10)
  • facit (9, 12, 14, 16, 19)
  • anchoring collagens (7)
  • short chains (8, 10)
  • multiplexin (15, 18)
  • macit (13, 17)
22
Q

how are type 1 collagens structured

A

each triple helix is displaced by 1/4 length (35nm) from its neighbour This is called a quarter staggered array. This helps form the banded pattern of collagen.

23
Q

how are type 1 collagen fibrils assembled?

A

it is determined by chain recognition sequence in the C - propeptide

24
Q

descemets membrane in the cornea is made of what type of collagen

A

VIII

25
Q

the basement membrane of glomerulus of kidney is formed by

A

type IV

26
Q

anchoring collagens connect x to y

A

epithelium to stroma

27
Q

beaded filament forming collagens form

A

structural links with cells, are type VI, it is crosslinked into tetramers that assemble into microfibrils

28
Q

elastin is found in what tissues

A

arteries, lungs, bladder, skin, elastic ligaments, cartilage

29
Q

how many genes are present for elastin

A

one, it contains Gly, Val, modified Ala and Pro. tropoelastin does not contain hydroxylysine nor is it glycosylated

30
Q

note

A

The lysines are involved in intermolecular crosslinking, while the week interactions between valine residues in the hydrophobic domains impart elasticity to the molecule.
• Tropoelastin is highly cross-linked to form insoluble complexes.

31
Q

what does lysyl oxidase do

A

converts amine groups of lysine to form reactive aldehydes, this results in spontaneous formation of desmosine cross links

32
Q

structure of elastin

A

is made of elastin fibers (made of a core region enriched in elastin proteins surrounded by microfiber sheath)

Biochemistry Year 2 (11 decks)

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