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Biochem block 3 > CT 3 > Flashcards

CT 3 Flashcards

1
Q

signals from the outside of the cell to stimulate gene transcription of Collagen

A

tgf beta il 1b

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2
Q

tnf alpha

A

signals from the outside of the cell to inhibit gene transcription of Collagen

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3
Q

TGF beta binds to

A

ser thre kinase activity

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4
Q

after ser thre kinase activity is triggered by TGF beta

A

SMAD 2 and 3 phosphorylate

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5
Q

phosphorylated SMAD 2 and 3

A

agg with SMAD 4 to form heterometric complex

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6
Q

heterometric complex

A

go to nucleus and act transcription of collagen

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7
Q

SMAD 7,8 inh

A

phos of SMAD 2 and 3

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8
Q

heterometric complex made from SMAD 2 and 3

A

binds CIS-elements in the 5′-flanking region for the regulation of transcription of the COL1A2 gene

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9
Q

collagen gene

A

repressors and enhancers

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10
Q

COL1 a1 controlled by

A

TGF beta act. protein

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11
Q

ColagenMolecule is to be secreted; it’s synthesized on —- —– ribosomes as larger precursor

A

Collagen Molecule is to be secreted; it’s synthesized on membrane-bound ribosomes as larger precursor

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12
Q

pre pro alpha chain (collagen)

A

hydrophobic and can be thread thru lumen of ER

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13
Q

pre pro alpha chain (collagen)

A

cotransltionally cleaved

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14
Q

signal peptidase

A

cleave N and C terminal

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15
Q

cleaveage of N and C terminal

A

leaves a telopeptide

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16
Q

contains intrachain disulfides

A

pN; N-terminal propeptide

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17
Q

contains interchain disulfides

A

pC; C-terminal propeptide

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18
Q

Collagens are modified

A

Collagens are modified after the amino acids are incorporated into the growing polypeptide chain

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19
Q

prolyl residues and lysyl residues

A

are hydroxylated

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20
Q

Glycosylation of—– residues

A

Glycosylation of hydroxylysyl residues

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21
Q

Prolyl hydroxylase has — ion at its active site

A

Prolyl hydroxylase has Fe++ ion at its active site

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22
Q

Prolyl hydroxylase

A

Prolyl hydroxylase is a dioxygenase

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23
Q

requires ascorbate

A

Prolyl hydroxylase

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24
Q

prolyl residue is added with —– —

and —to be hydrozylated

A

alpha ketogluterate and O2

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25
Q

Prolyl hydroxylase

A

act O2

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26
Q

Proline is hydroxylated at —-

by the action of prolyl hydroxylase

A

Proline is hydroxylated at C-4

by the action of prolyl hydroxylase

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27
Q

TF Free proline is a substrate

A

Free proline is NOT a substrate

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28
Q

Hydroxylation at C-4 only if Pro is on the —– side of a Gly residue in the (Gly-XY)n sequence in collagen

A

Hydroxylation at C-4 only if Pro is on the amino side of a Gly residue in the (Gly-XY)n sequence in collagen

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29
Q

Different enzyme; hydroxylation at —- if Pro is on the carboxyl side of a Gly in the (Gly-X-Y)n sequence in collagen

A

Different enzyme; hydroxylation at C-3 if Pro is on the carboxyl side of a Gly in the (Gly-X-Y)n sequence in collagen

3-prolyl hydroxylase

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30
Q

Dietary deficiency of vitamin C

A

Scurvy

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31
Q

Poor wound healing

Poor calcification of developing teeth

A

Vit C

32
Q

Fragile blood vessels

Suppressed bone growth

A

Scurvy

33
Q

gingival bleeding and

Skin lesions

A

deficiency of vitamin C

34
Q

Hydroxylation of lysine only if it’s on the amino side of a glycine residue

A

Specificity of lysyl hydroxylase

35
Q

O2 and ascorbate

A

needed for lysyl hydroxylase to work

36
Q

α ketoglutarate; succinate

A

reactant and substrtae for lysyl hydroxylase and prolyl hydroxylase

37
Q

Ehlers-Danlos Syndrome,

A

Deficiency of lysyl hydroxylase

38
Q

❂ Hyperextensibility of skin and joints

A

Ehlers-Danlos Syndrome,

39
Q

tf Ehlers-Danlos Syndrome, has inc crossliking of collagen

A

F

lowered

40
Q

Poor wound healing

and Musculoskeletal deformities

A

Ehler danslos

41
Q

Hyp

A

CANNOT be incorporated into a growing polypeptide chain so addition of [14C] Hyp will not result in formation of [14C] collagen

42
Q

Proline and hydroxyproline are both radioactive but

A

Hyp CANNOT be incorporated into a growing polypeptide chain

43
Q

Unique to collagens;

A

Unique to collagens; glycosylated hydroxylysyl residues

44
Q

2 types of O linked glycosylations

A

serine and 5 hydroxylysine

45
Q

asparagine

A

N glycosyl Linkage

46
Q

glycosylations of

A

glucose and galactose

47
Q

After post-translational modification, the 3 polypeptides associate to form the procollagen molecule.

A

After post-translational modification, the 3 polypeptides associate to form the procollagen (Type I procollagen) molecule.

48
Q

where is procollagen made

A

in the ER lumen

49
Q

Extension peptides

A

help guide the formation of the triple helix.

50
Q

Each polypeptide is —- through a large portion of the molecule and stabilized partly by —— of the pyrrolidone rings of proline.

A

Each polypeptide is helical through a large portion of the molecule and stabilized partly by steric repulsion of the pyrrolidone rings of proline.

51
Q

3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains

A

3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains

procollagen

52
Q

Residues in each chain are —— staggered such that a gly, an X and a Y from ——chains are on the same level along the helix axis.

A

Residues in each chain are vertically staggered such that a gly, an X and a Y from different chains are on the same level along the helix axis.

53
Q

procollagen

A

stiff cable

54
Q

H-bonds form between —- and —- in procollagen

A

H-bonds form between the N-H of Gly and O in procollagen

55
Q

procollagen C terminal

A

disulfide linkage

56
Q

cooperative interactions

A

determines stability of collagen molecules

57
Q

-NH of Gly and the C=O of second residue in triplet of neighboring chain

A

have a h bond

58
Q

Gly as every third amino acid

Hyp content

Total imino acid content

A

determine stability of collagen molecule

59
Q

inc temp

A

collagen loses its rodlike shape, the viscosity of the solution drops

helical structure destroyed

60
Q

after TM

A

collagen is a random coil

61
Q

Tm is the temperature at

A

temperature at which 1/2 of the helical structure is lost

62
Q

abruptness of the transition indicates that the stability of collagen molecules depends upon—- cooperative interactions

A

abruptness of the transition indicates that the stability of collagen molecules depends upon weak cooperative interactions

63
Q

abnormal collagen

A

smaller Tm

64
Q

Hyp cntent

A

inc the TM and stabilizes the collagen triple helix

65
Q

pro and hyp inc with

A

warm blooded animals

Tm also increases

66
Q

H bonding in collagen occur

A

between peptide -NH of Gly and the C=O of second residue in triplet of neighboring chain

OH groups of Hyp also participate in Hbonding

67
Q

Mutation of a single gly

A

can be lethal

68
Q

close packing and stabilization of triple helix

A

Glycine

69
Q

OI

A

Mutation of a single T for a G

70
Q

glycine to cysteine mutation

A

OI

71
Q

Skeletal deformities, brittle bones

A

OI

72
Q

Triple helix is disrupted

A

OI

73
Q

Rupture arteries

Rupture uterus

A

Ehlers-Danlos Syndrome, Type IV

74
Q

Thin, translucent skin ,Bruise easily

A

Ehlers-Danlos Syndrome, Type IV

75
Q

Perforate intestines

A

Ehlers-Danlos Syndrome, Type IV

76
Q

Defects in type III collagen

A

Ehlers-Danlos Syndrome, Type IV

77
Q

Gly , Skip exon

A

Ehlers-Danlos Syndrome, Type IV

Biochem block 3 (12 decks)

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