Fibrillar Proteins Flashcards

1
Q

Fibrillar Proteins

A

insoluble protein that makes up the principal structural proteins of the body. High content of secondary structures that form rod-shaped microfibers (fibrils)

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2
Q

Abnormal Collagen cause dysfunction of ….

A
cardiovascular organs
bone
skin
joints
eyes
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3
Q

Amino acid composition of collagen

A

33% Gly, 10-13% Pro, 10% OH-Pro and 1% OH-Lys + other stuff

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4
Q

Enzymes needed to catalyze hydroxilation of Pro and Lys

A

Lyslyl hydroxylase
Prolyl-4-hydroxylase
Prolyl-3-hydroxylase

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5
Q

Hydroxilation enzymes require ….

A

Fe2+, O2, Vit C, and Alpha-ketoglutatrate

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6
Q

Collagen - primary composition, effects of primary composition

A

involve repeats of -Gly-Pro-Y and -Gly-X-Hyp

  • Gly (smallest AA) : will fit into small places
  • Pro : helix breaker : No Alpha Helix
  • Cross links can be formed
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7
Q

Scurvy - cause, symptoms

A

Ascorbic acid deficiency (Vit C) - poor synthesis of collagen without Co-factor to support collagen enzymes, symptoms diverse

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8
Q

Polyproline type II helix

A

One strand of collagen

Loose, left-handed helix, with three residues per turn

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9
Q

Alpha helix

A

Right-hand coiled or spiral confirmation. Every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier
Secondary structure proteins - Hydrogen bonds hold together

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10
Q

Right handed triple helix

A

Right handed

Low bulkiness of Gly allows COLLAGEN to from

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11
Q

Collagen - secondary/tertiary sturtures

A

Polyprolive type II helix
Right handed triple helix (three member superhelix)
Fibrils

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12
Q

How to collagen for fibrils

A

they can aggregate in quater staggered parallel arrays and cross-link to form fibrils

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13
Q

Telopeptides

A

N and C terminal segmetns of the triple helical region

sites for crosslinking

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14
Q

lysyle amono oxidase

A

Convert Lys groups to ALLYSINE (an aldehyde)
COPPER dependent
collagen + elastin

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15
Q

Steps in Biosynth of Collagen

A
Ribosomes in RER
3 alpha chains translation
Peptide chain a.k.a PRECOLLAGEN
Lumen of RER
Cleavage by signal peptidase
PROCOLLAGEN
Hydroxylation of lysine.proline by hydroxylysine residues
Glycosylation begins
Disulfide bond formation
RER - Triple helical structure
PROCOLLAGEN
Shipped to GA
Glycosylation complete
Secretion by exocytosis (into ECM)
Propeptides cleaved
TROPOCOLLAGEN together form COLLAGEN FIBRILS together form COLLAGEN FIBERS
Maturation (intra/inter crosslinks)
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16
Q

Collagenases - def, action

A
Matrix metalloprotienases (MMP's) that catalyze hydrolysis of collagens, which typically have long half lives
Clips collagen, triple helix unwinds and further degrades by gelatinases
17
Q

Collagen - types

A

Fibrillar : I-III, V, XI
Network Forming : IV
Fibirl associated : IX, XII

18
Q

Ostegensis Imperfecta - def., types (severity)

A

genetic disorder of collagen type I (mutation in chain alpha 1 or alpha 2)
OI type 1 - mild and common (type IA and IB)
OI type II - most severe - death in utero
OI type III - progressively deforming - most severe past infancy
OI type IV - moderately severe - variety

19
Q

Ehlers-Danlos Syndrome

A

Group of connective tissue disorders

20
Q

Elastin - def., compostion, sturcture

A

Provides elasticity to tissues, fibrous, insoluble to water
Lacks regular secondary structure but contains an UNORDERED coiled structure
Composed of allysines (secondary)
Desmosine and Isodesmosine (tertiary)- covalently crosslink chains

21
Q

Cytoskeleton - composed of

A

microtubles, intermediate filaments and microfilaments

22
Q

Microfilament - composed of,

A

Actin

Myosin

23
Q

Microtubles - composed of, affected by (action)

A

alpha and beta tubilin
Colchine - dissaemble microtubules
Taxol - inhibit microtuble formation through binding (cell cylce specific)
Vince Alkaloids - Inhibit microtubles formation
Taxanes and Epothilones - Enhance microtuble stability

24
Q

Kinesin and Dyenins

A

K - move vesicles to the + end of microtubules

D - move vesicles to the - end of microtubules

25
Q

Intermediary filament - def., e.g.

A

Exclusively structural

Keratin (hard and soft)

26
Q

Keratin - structure

A

Coiled coils - a dimer of alpha helices

27
Q

OI type I

A

few to 100 fractures, no bone deformity, normal stature, , normal teeth, blue scelra

28
Q

OI type II

A

Perinatal, lethal, dark blue sclera

29
Q

OI type III

A

Severe, lots of bone deformity, short stature, bad teeth, blue sclera, frequent hearing loss

30
Q

OI type IV

A

moderate to mild, some bone deformity, some hearing loss, some short stature, normal to gret sclera

31
Q

Types of OI mutations - explanations

A

Null allele = nulceotide deletion of frameshift = incorrect mRNA = low alpha 1 collagen = OI type 1
Structural mutation - single nucleotide change for Gly = new AA = variying problems = OI type II, III, IV