Collagen structure and function 1 Flashcards

1
Q

What space is filled with a network of large macromolecules?

A

Extracellular Matrix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are specialized tissues in which ECM is more abundant than cells?

A

connective tissues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What types of oral and craniofacial tissues involve the ECM?

A
  • teeth/bone
  • cartilage
  • lamina propria
  • gingiva/periodontium
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is a stroma?

A

cells embedded in matrix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What are the major components of stormal matrix?

A

collagen embedded in polysaccharide ground substance of hyaluronan and proteoglycans

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What cells secrete ECM in most connective tissues?

A

fibroblasts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the specialized matrix at the interface between connective tissues stroma and epithelium?

A

basal lamina

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what type of collagen tethers the basal lamina to the CT?

A

type VII

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

basement membrane is comprised of what?

A

basal lamina and layer of collagen fibrils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the function of the ECM in bone?

A
  • Support and locomotion
  • Calcium homeostasis
  • Skeleton protects brain, internal organs
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the function of ECM in teeth?

A
  • Provides strength/structure to tooth
  • Resists shear and compression forces associated with chewing
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the function of ECM in cartilage?

A
  • Support and locomotion
  • Resilient - shock absorber for compressive forces associated with locomotion, mastication etc.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what are the roles of ECM not related to structure?

A

-embryonic development
-regulation of cell function
-tissue repair/wound healing
-angiogenesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The composition of ECM in each tissue is perfectly suited to ______________________

A

biomechanical/functional requirements of the tissue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what are the ECM components?

A

-collagen
-proteoglycans
-elastin
-fibrillin-1
-mineral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What property does collagen have?

A

tensile strength

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What property does proteoglycans?

A

resilience/resistance to compression

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What property does elastin have?

A

elasticity/resilience

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What property does fibrillin-1 have?

A

controlled elasticity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What property does mineral have?

A

strength, hardness, brittleness

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What are examples of structural fibrous proteins?

A

collagen, elastin, fibrillins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What are examples of adhesive fibrous proteins?

A

fibronectin, vitronectin, laminin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

28 different collagens identified, encoded by up to _____ different genes

A

42

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

All collagen molecules contain at least one ___________

A

triple helical region associated with glycine every third amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is the major structural component of ECM?

A

collagens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What are collagens structure?

A

trimeric molecules consisting of three identical or non-identical polypeptide chains

(long, stiff triple stranded helical structure with 3 a-chains wound around each other like a rope)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What are the major fibrillar collagens?

A

I, II, III

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

what are fibrils crosslinked between?

A

lysines of adjacent molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Which collagen type is found in tendon, bone, ligaments, dentin, skin?

A

Type I

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Which collagen type is found in cartilage matrix?

A

Type II

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What is the Type I collagen structure?

A

heterotrimer of two a1(I) chains and one a2(I) chain (genes COL1A1 and COL1A2)

32
Q

mutations in type I collagen genes (COL1A1 and COL1A2) are associated with what?

A

osteogenesis imperfecta

33
Q

What are the ways in which type I collagen fibrils vary in 3D arrays?

A
  • parallel bundles (tendons/ligaments)
  • orthogonal lattices (cornea)
  • concentric weaves (bone)
  • wickerwork pattern (skin)
  • swirling pattern (teeth)
34
Q

What is the major collagen type in cartilage, vitreous humor (eye), and inner ear?

A

Type II

35
Q

What is the structure of Type II collagen?

A

homotrimer of a1(II) chain (COL2A1)

36
Q

What do mutations in type II collagen cause?

A

chondrodysplasias

37
Q

structure of non-fibrillar collagen

A

triple helical domains shorter, interrupted by non-collagenous sequences-structure less rigid and more flexible

38
Q

What collagen types are important in basal lamina?

A

Type IV and VI

39
Q

What collagen type is key in anchoring fibrils that attach epithelia to underlying connective tissue?

A

Type VII

40
Q

In collagenous domains ______ is present every 3rd residue?

A

glycine (Gly-X-Y motif)

41
Q

what is the X in Gly-X-Y motif most commonly?

A

proline

42
Q

what is the Y in Gly-X-Y motif most commonly?

A

4-hydroxyproline

43
Q

is the collagen helix left or right-handed?

A

left-handed

44
Q

How is the collagen helix stabilized?

A

by static repulsion of pyrrolidone rings or proline and hydroxyproline residues

45
Q

Which amino acid has a 60 degree twist?

A

proline (disrupts other structures from forming beside a helix)

46
Q

What type of helix forms from 3 procollagen chains?

A

collagen right handed triple helix (quaternary structure)

47
Q

Which amino acid has the least bulky side chain?

A

glycine

48
Q

what stabilizes the triple helix of collagen?

A

hydrogen bonds

49
Q

Why is every 3rd residue glycine?

A

allows three helical alpha chains to pack together to form a triple helix

50
Q

What are some key steps in collagen biosynthesis and assembly?

A
  • post translational modifications
  • collagen crosslinking
51
Q

what are the post-translational modifications in collagen biosynthesis and assembly?

A

hydroxylation
glycosylation
protolytic processing of procollagen

52
Q

Where do collagens undergo extensive post translational modifications?

A

ER

53
Q

What does the post-translational modification prolyl hydroxylases and lysyl hydroxylase do?

A

hydroxylates prolines and lysines (needs vitamin C)

54
Q

What does the post-translational modification FKBP10 do?

A

accelerates protein folding

55
Q

What does the post-translational modification collagen glycosyltransferasesd do?

A

glycosylates selected hydroxylysines

56
Q

What does the post-translational modification protein disulphide isomerase (PDI) do?

A

catalyzes formation of interchain disulphide bonds between cysteines

57
Q

What does the post-translational modification Hsp47 do?

A

chaperone protein that binds to disulfide bonded collagen trimers

58
Q

What does the procollagen processing ADAMTS2, 3, 14 do?

A

N-proteases resonsible for cleaving off N-propeptide

59
Q

What does the procollagen processing BMP-1/tolloid proteinases do?

A

C-proteinase responsible for cleaving off C-propeptide

60
Q

The amount of crosslinking of collagen __________ with age

A

increases

61
Q

What is the key enzyme in collagen crosslinking with fibrils?

A

lysyl oxidases

62
Q

What is the major ECM component of dentin, cementum, and periodontal ligament?

A

Type I collagen

63
Q

What is the only calcified tissue that does not contain abundant collagen?

A

enamel

64
Q

what attaches the cementum layer of tooth root to alveolar bone?

A

collagen in PDL

65
Q

what attaches the gingiva to tooth and alveolar bone?

A

abundant collagen fibers in gingiva

66
Q

What are the five groups of collagen fibers in gingiva?

A
  • Dentinogingival and Alveogingival (calcified into cementum/bone at one end, free at other end)
  • Circumferential (encircle tooth)
  • Periosteal (hold attached gingiva
    against bone)
  • Transseptal (run between teeth)
67
Q

What is the portion of fibrils anchored into mineralized cementum or bone?

A

sharpey’s fibers

68
Q

What type of collagen in dentin?

A

Type I with trace amounts of III and V

69
Q

What type of collagen in enamel organic matrix at the DEJ?

A

Type IV and VII

70
Q

What collagen type is important in basal lamina?

A

Type IV

71
Q

What is the function of basal lamina in kidney glomerulus?

A

determines which molecules will pass into urine from blood

72
Q

What is the function of basal lamina in skin?

A

attaches epidermis to dermis

73
Q

What is the function of basal lamina in oral mucosa?

A

attaches epithelium to lamina propria

74
Q

What are the key components of basal lamina?

A

glycoproteins
collagens (Type IV collagen)
proteoglycans

75
Q

What mutation and collagen type is involved in dystrophic epidermis bullosa?

A

COL7A1
Type VII