4: 1 Flashcards

1
Q

define mechanotransduction

A

the molecular mechanism by which cells sense and respond to mechanical signals.

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2
Q

How does myocardial infarction demonstrate tissue mechanics

A

o Portion dies and replaced by collagen (blue)

o Tissue mechanics change, i.e. collagen makes cardio stiffer

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3
Q

3 types of molecules in the ECMs

A
  1. Proteoglycans and GAGs
  2. Fibrous proteins
  3. Glycoproteins
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4
Q

What is a GAG

A
  • (sugarchain) unbranched polysaccharide chains
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5
Q

What are the four groups of GAG

A

1) Hyaluronan
2) Chondroitinsulfate
3) Dermatansulfate
4) Keratansulfate

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6
Q

What are some features of a GAG

A
  • Too stiff to fold into globular structures & Strongly hydrophilic
    o High volume relative to the mass - space filler (not flexible enough to fold into small)
    o Form hydrated gels even at the low concentrations (can hold high amount of water)
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7
Q

What attaches to GAG and what is this combinatorial molecule called

A

proteins attached =proteoglycans

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8
Q

what is a proteoglycan

A

GAG (sugar/polysaccharide) with a protein covalently attached

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9
Q

What GAG cannot add a protein

A

hyaluronan

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10
Q

difference between proteoglycan + glycoprotein

A

Proteo= mostly sugar + small protein

Glycopro= - mostly protein + small sugar

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11
Q

name two Common Proteoglycans: both core protein but different side chain of GAG number

A
  1. Decorin <10 GAG chains

2. Aggrecan >100 GAG chains

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12
Q

describe aggrecan

A
  • proteoglycan
  • • 100 aggrecans non-covalently bound to a single hyaluronan
    • found in cartilage
    • = high compression load bearing
    • i.e knee joint
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13
Q

What are the major component of ECM

A

Fibrous protein= collagen

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14
Q

Describe the structure of collagen

A
  • Gly-X-Y - ⍺ chain (usually X: proline and Y: hydroxyproline)
  • Three together= Triple-stranded helical rod (B)
  • Small glycine - interior of the triple helix // compact rod tightly
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15
Q

how many genes coding for different collagen ⍺ chains + how many types of collagen

A

human genome contains 42 distinct genes coding for different collagen ⍺ chains but only ~40 types of collagen (as triple helices)
= • Lot of gene coding but less combination

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16
Q

Models of fibrillar collagen assmebly

A

amino acid sequence > a chain > triple helix > collagen molecule > collagen fibril > collagen fiber

17
Q

what are the types of collagen + function

A
  • Type I is by far the most common collagen of skin and bone
  • 90% of your body: types I to IV
  • Types IX and XII are called fibril- associated collagens
18
Q

what force does collagen resist

A

TENSILE force

19
Q

Name 2 glycoproteins

A

Fibronectin

Laminin

20
Q

how many genes codes fibronectin + how many types

A

• 1 gene codes it, (50 kb) but 20 different types

21
Q

How many, and what’s inside the domains of fibronectin

A

• 3 domains within the protein (12 type I, 2 type II, 15-17 type III)

22
Q

2 types of fibronectin

A

A. Plasma Fibronectin (soluble)

B. Cellular Fibronectin (insoluble)

23
Q

Tension sensing function of fribronectin

A
  • Cells can pull fribronectin and stretch a little
  • insoluble fibronectin assemble into fibrils only on the surface of cells with appropriate fibronectin-binding proteins, integrin (whereas collagen that can self- assemble into fibrils in a test tube)
  • some type III fn unfold (when stretched) to expose cryptic binding sites that interact with other fb resulting fn filaments formation
24
Q

what is basal laminin and major compnents

A
  • Specialised type of ECM called basal lamina (basement membrane)
  • Laminin and type IV collagen, nidogen, perelman, integrin
25
Q

is laminin a glycoprotein

A

yes

26
Q

describe structure + number of combinations of laminin

A
  • Trimeric structure with alpha, beta, and gamma chains (3 chains)
  • 16 combinations found in vivo
27
Q

how to name laminin

A

•3 chains= If have alpha 1, gamma 1, beta 1 // = laminin111

28
Q

what degrades the matrix

A

• Degradation by MMPs (matrix metaloproteases)