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Biochem block 3 > CT 2 > Flashcards

CT 2 Flashcards

1
Q

❂ Laminins

A

(basal laminae) (GP)

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2
Q

fibronectin

A

widely distributed GP

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3
Q

Collagens

A

most widely distributed protein in the body(GP)

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4
Q

Tf Glycoproteins have covalently-bound carbohydrate.

A

t Glycoproteins have covalently-bound carbohydrate.

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5
Q

the hydroxyl group ( -OH ) of serine or threonine • the hydroxyl group ( -OH ) of hydroxylysine

A

called “O-linked” in GP

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6
Q

(only in collagens)

A

hydroxylysine in GP

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7
Q

the amide group [-NH2] of asparagine -

A

called “N-linked”.

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8
Q

tf sugar residue Render glycoproteins more hydrophilic

A

t

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9
Q

sugar residues stabilize against —– and ——- binding to some components

A

Sugar stabilize against hydrolysis and modulate binding to some components

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10
Q

Linker Proteins

A

Fibronectins

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11
Q

Interlink collagens, proteoglycans with cell surface receptors

A

Fibronectins

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12
Q

Fibronectin

A

Enable cells to interact with the extracellular matrix

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13
Q

Adhesion ❂ Differentiation

A

Fibronectin purpose

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14
Q

Fibronectin purpose

A

Embryonic cell migration

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15
Q

Fibronectin Determine —-, ——- organization

A

Determine cell shape, cytoskeletal organization

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16
Q

Wound healing

A

Fibronectin

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17
Q

cancer cells lose the ability to synthesize ———

A

cancer cells lose the ability to synthesize fibronectin

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18
Q

In OC, fibronectin regulates

A

Dental mesenchyme differentiating into odontoblasts

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19
Q

Carbohydrate accounts for —– of the weight of fibronectin

A

5%

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20
Q

2 peptides connected in V like shape

A

Fibronectin

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21
Q

fibronectin —> 2 x 250 kDa chains linked by disulfide bond near the C-terminus.

A

2 x —– kDa chains linked by disulfide bond near the — -terminus.

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22
Q

Fibronectin

A

specialized domains for binding cell surface receptors and the extracellular matrix

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23
Q

links the outer components of the cell to the cell itself.

A

Fibronectin

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24
Q

RGD or RGDS

A

cell surface receptor-binding domain

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25
Q

disulfide bonds connect fibronectin at

A

C terminal

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26
Q

on the fibronectin structure which binding domain is most near N terminal

A

Heparin and Fibrin binding domain

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27
Q

binding domain next to cell surface receptor bidning domain and near N terminal

A

fibrin binding domain

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28
Q

fibrin heparin binding domain

A

most near c terminal of fibronectin (N to C)

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29
Q

cell surface receptor binding domain

A

contains RGD or RGDS

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30
Q

Laminin

A

linker proteins

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31
Q

Enable epithelial cells to interact with the extracellular matrix

A

Laminin

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32
Q

Laminin

A

high affinity for Type IV collagen

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33
Q

diff ,adhesion

A

Laminin

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34
Q

Embryonic nerve axonal outgrowth

Nerve regeneration after injury

A

laminin

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35
Q

Laminin in OC

A

contributing to terminal differentiation of ameloblasts and

in enamel matrix formation.

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36
Q

may also contribute to the growth of ameloblastomas

A

Laminin

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37
Q

Expression of α2 and β2 of laminin

A

in fetal oral squamous epithelium

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38
Q

α2 and β2 of laminin

A

Re-expression of these in adult oral squamous cell carcinomas

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39
Q

low Carbohydrate(13%)

A

Laminin

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40
Q

Laminin

A

Specialized domains bind cell surface receptors and the extracellular matrix i.e.

links outer components of the cell to the cell surface.

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41
Q

disulfide-linked heterotrimer

A

Laminin

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42
Q

α, β and γ chains

A

Laminin

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43
Q

cruciform shape

A

Laminin

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44
Q

Laminin molecules ——associate to form ——.

A

Laminin molecules self-associate to form aggregates.

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45
Q

For laminin

A

Nomenclature indicates chain composition

46
Q

Laminin network formation involve

A

Ca

47
Q

type 4 collagen and perlecan (extracelllar molecules)

A

bind laminin

48
Q

integrin

A

bind laminin and fibronectin

binding site for the linker proteins

49
Q

transmembrane proteins

and GP

A

integrin

50
Q

The cytoplasmic side of integrins binds to —– components.

The extracellular domain of integrins binds to —– and —–

A

The cytoplasmic side of integrins binds to cytoskeletal components. ❂ The extracellular domain of integrins binds to fibronectins and laminins

51
Q

binds ECM and transmembrane proteins

A

fibronectins and laminins

52
Q

linker protein-mediated “communication”.

A

fibronectins and laminins

53
Q

alpha beta subunit

A

integrin

54
Q

tf

Cells can have 1 integrin receptors that link the cell to only one component of the extracellular matrix.

A

Cells can have multiple integrin receptors that link the cell to more than one component of the extracellular matrix.

55
Q

The ——/—– sequence on the linker proteins binds specifically to the integrin receptors.

A

RGD/RGDS sequence on the linker proteins

56
Q

Activation of integrins can lead to their — and —— of focal adhesions

A

Activation of integrins can lead to their clustering and formation of focal adhesions

57
Q

C terminus of alpha and beta subunits of integrin

A

located in cytoplams

58
Q

alpha subunit split into 2 segments

A

and linked together by disulfide linkage

59
Q

disulfide rich repeats exist in

A

beta subunit of integrin

60
Q

integrin binds to actin on

A

cytoskeleton side

61
Q

out to in signal of integrin

A

ligand binds from ECM

62
Q

Out to in signal in integrin

A

cell polarity

surviva;

proliferation

cytoskeletal structure

gene expression

63
Q

Talin

A

involved in in to out signaling with integrin

64
Q

cell migration

cell adhesion

ECM assembly

A

In to Out signaling with integrin

65
Q

regulation of the extracellular binding activity of a cell’s integrins from within.

A
66
Q

collagen

A

GP

67
Q

Chemotaxis

A

Collagen

68
Q

(major stress-bearing component

A

Colagen

69
Q

Collagens form —– fibers with high —- strength; hold cells together in discrete units.

A

Collagens form insoluble fibers with high tensile strength; hold cells together in discrete units.

70
Q

By weight, —- of the protein in vertebrates is collagen

A

By weight, 1/4 of the protein in vertebrates is collagen

71
Q

cornea cartiledge

A

high percent collagen by weight

64 50

72
Q

highest percent collagen by weight

A

skin 74

73
Q

liver lung

A

small percent colagen by wieght

4 and 10

74
Q

cOrtical Bone

aOrta

A

23%

10-24%

% collagen by wieght

75
Q

after fibroblast make polypeptide system

A

OH and glycosylation occurs(collagen)

76
Q

Secretion of procolllagen is followed by

A

hydrolysis of peptide bond to form tropocollagen

77
Q

self assembly of tropocolagen to form

A

collagen fibers

78
Q

crosslink in colagen fiber leads to

A

mature collagen fiber

79
Q

tf collagen fber is made in between

procolagen and tropocollagen

A

F after tropocollagen

80
Q

tf collagenis product of few genes

and few types

A

F over 40 genes

28 types

81
Q

types 2 and 3 collagen

A

homotrimers

82
Q

collagen 1,4,5

A

heterotrimers

83
Q

polppetide in collegen

A

alpha

84
Q

placenta skin

A

type 5 collagen

85
Q

basment membrane

A

type 4 collagen

86
Q

cartildge IVD

A

collagen 2

87
Q

skin tendon

A

type 1 collagen

88
Q

bone dentin

A

type 1 collagen

89
Q

BV uterus reticular fibers

A

type 3 collagen

90
Q

triple helical rod

A

collagen

91
Q

Remarkably strong

Forms an insoluble fiber with high tensile strength

A

collagen

92
Q

collagen

A

3000 Å long and 15 Å diameter

93
Q

1/3 of the amino acids in collagen

A

Glycine

94
Q

Proline

4-Hydroxyproline (Hyp)

3-Hydroxyproline (Hyp)

A

collagen

95
Q

5-Hydroxylysine

A

collagen

96
Q

tf collgen has Charged (—) amino acids

A

F

Charged (positive) amino acids

97
Q

highest component in collagen and elastin

A

Gly

98
Q

5 hydroxylysine

A

not present in elastin

present in collagn

99
Q

desmosine and isodesmosine not in

A

collagen

100
Q

collagen primary structure

A

glu X Y

101
Q

X

A

Proline

102
Q

Y

A

hydroxyproline

103
Q

polar basic AA

A

also in collagen

104
Q

X

A

proline

105
Q

tf 3 hydroxylysine is in collagen

A

F

5 hydroxylysine

106
Q

Y

A

hydroxyproline

107
Q
A
108
Q

secondary structure of collagen

A

tropocollagen with left handed helical structure

109
Q

type 2 trans helix

A

2nd and tert structure of Collagen

110
Q

quat structure

A

type 2 transhelix twist around each other to form right handed helix(superhelix)

111
Q

triple helix of tropocollagen

A

has glycine in the middle

Biochem block 3 (12 decks)

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