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MGD > Collagen Synthesis > Flashcards

Collagen Synthesis Flashcards

1
Q

In collagen, what are the X and Y amino acids most often?

A

Proline- X

Hydroxylisine/Hydroxyproline- Y

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2
Q

How many alpha chains are present in collagen?

A

3

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3
Q

What formation of chains does collagen form?

A

Triple helix

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4
Q

In collagen, which is every 3rd amino acid?

A

Glycine

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5
Q

Which types of collagen, out of I, II, III, form fibrils and which form fibres?

A

All 3 form fibrils

Only type I and II form fibres

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6
Q

Characteristics of type I collagen and where it’s found

A

High tensile strength

Bone, skin, tendons, BV’s

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7
Q

Characteristics of type II collagen and where it’s found

A

Cartilagenous
Don’t form fibres
Forms elastic and hyaline cartilage

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8
Q

Name and characteristics of type III collagen and where it’s found

A

Reticullin
Forms fibres
Skin, BV’s, lymphatic system

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9
Q

What is the name of collagen when it is initially synthesised?

A

Preprocollagen

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10
Q

Where is collagen precursor synthesised and secreted from?

A

Fibroblasts

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11
Q

Is the signal sequence on collagen precursor cleaved or retained? If so by what?

A

Cleaved

Signal peptidase

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12
Q

After cleavage of signal peptide, what is collagen precursor chains called?

A

Pro α Chains

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13
Q

Why is it important that the collagen chains are hydroxylated?

A

More OH- groups
TF more H bonds form
TF stronger structure

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14
Q

What modifications occur to collagen in the RER? (In brief)

A

Hydroxylation (of selected proline + lysine)
Addition of Galactose
N-linked glycosylation

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15
Q

Where does O linked glycosylation of collagen occur?

A

Golgi body

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16
Q

What is the final thing that happens to collagen in RER, before exocytosis?

A

Chains align and disulphide bonds form

Forms a triple helix

17
Q

What is N-linked glycosylation?

A

Where a sugar (glucose) is linked onto a chain by forming a bond with the nitrogen in the sugar ring

18
Q

What is O-linked glycosylation?

A

Where sugar (glucose) is added to chain by forming a bond with the oxygen present in the sugar

19
Q

Which residues in collagen α chains are selectively hydroxylated? What are they then called?

A

Proline- Hydroxyproline

Lysine- hydroxylysine

20
Q

What enzyme catalyses hydroxylation in collagen synthesis?

A

Prolyl hydroxylase

21
Q

Which enzyme catalyses the formation of covalent cross link between collagen fibrils?

A

Lysyl Oxidase

22
Q

What co-factors are required for the enzyme that catalyses hydroxylation of collagen residues? Name the enzyme too

A

Prolyl hydroxylase
Vitamin C
Fe2+ ions

23
Q

What is the general/basic structure of alpha collagen chains?

A

Glycine-X-Y

24
Q

What is tropocollagen?

A

Collagen FIBRILS that have had their N&C terminal propeptides removed?

25
Q

Once finished in the Golgi, what happens to procollagen?

A

Transported out of Golgi by transport vesicle
N&C terminal peptides removed
To form tropocollagen
Collagen FIBRILS aggregate to form FIBRES
Lysyl oxidase catalyses formation of covalent bonds

26
Q

Which residues are selectively N-linked glycosylated and have galactose added to?

A

Hydrolysine

Proline

27
Q

Which enzyme catalyses the removal of N&C terminal propeptides?

A

Procollagen peptidase

28
Q

What modification to collagen occurs in the Golgi?

A

O-linked glycosylation

29
Q

Once tropocollagen has formed, what happens?

A

Lysyl oxidase catalyses formation of covalent cross links between collagen FIBRILS to form collagen FIBRES

30
Q

Which enzyme catalyses the formation of covalent cross links between collagen fibrils forming collagen fibres?

A

Lysyl oxidase

31
Q

What does CHANDPORC stand for?

A

Cleavage, hydroxylation, addition of galactose, n-linked glycosylation, disulphide bond formation, procollagen, o-linked glycosylation, removal of N + C propeptides chains, covalent bond formation

MGD (9 decks)

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