Extracellular Matrix Flashcards

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1
Q

Collection of extracellular molecules secreted by cells that provides structural and biochemical support to surrounding cells

A

extracellular matrix

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2
Q

Where is the EM found?

A

epithelium, endothelium, connective tissue

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3
Q

Cells contained in EM

A
  • fibroblasts
  • immune cells
  • fat cells
  • bone cells
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4
Q

macromolecules contained in EM

A
  • collagen
  • elastins
  • proteoglycans
  • hyaluronan
  • adhesive glycoproteins
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5
Q

two groups of cells in EM

A

indigenous cells and immigrant cells

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6
Q

4 indigenous cells

A

Primitive mesenchymal cells
Fibroblasts
White fat
Brown fat

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7
Q

immigrant cells

A

blood cells (immune system cells) —- plasma cells, monocytes, lymphocytes, etc.

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8
Q

Undifferentiated multipotential stem cells that proliferate and differentiate to give rise to all indigenous cells of connective tissue

A

primitive mesenchymal cells

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9
Q

main cell of em, secretes most of the macromolecules, spindle shaped reticular cells (can be other shapes)

A

fibroblasts

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10
Q
  • Distributed in the CT of ECM
  • energy reserve
  • calories (energy) in the form of lipid droplets
  • Only vertebrates have specialized cells recognizable as these
A

fat cells

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11
Q

master regulator of energy balance and nutritional homeostasis (most important function)

A

adipose tissue

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12
Q

types of fat cells

A

white, brown, and beige

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13
Q
  • Contain a single large lipid droplet full of triglycerides
  • Secrete hormones such as leptin,
  • Most common fat cell
A

white fat

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14
Q
  • Color refers to the large number of mitochondria

- Specialized fat that dissipates stored energy in the form of heat

A

brown fat

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15
Q
  • Emerge in rodents upon prolonged cold exposure or adrenergic signaling
  • Have both overlapping and distinct gene expression form brown fat
A

beige fat

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16
Q

which cell has a different linegae

A

brown fat - has the same lineage as a myoblasts

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17
Q

immune system cells

A

CT — blood and lymph, the interstitial space in the ECM

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18
Q

most abundant protein in human body, formation of a rod composed of a triple helix of polypeptides

A

collagen

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19
Q

tendons, ligaments, bones, dense CT

A

fibrillar collagens

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20
Q

polymerize into sheets, found in tissue surrounding organs, epithelial or in some cases a whole animal

A

sheet forming collagens

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21
Q

example that forms the basal lamina

A

type IV collagen

22
Q

fibrillar and sheet collagens, provide and anchor for type IV collagen to the basal lamina

A

linking collagens

23
Q

collagen amino acid seuqence

A

Gly-X-Y

24
Q

part of the repeating sequence, found in 3rd position of the polypeptide chain, fits into the restricted spaces where the three chains of the helix come together

A

glycine

25
Q

frequently proline

A

X

26
Q

facilitate the formation of helical conformation of α- chain, because its ring structure causes kink in the peptide chain.

A

proline

27
Q

hydroxy proline and hyroxy lysine

A

Y

28
Q

residues after their incorporation into the polypeptide chains.

  • post translational modification
  • stabilizes
  • requires oxygen and Vitamin C
  • mediated by prolyl and lysol hydroxyls in the rER
A

hydroxyporline and lysine

29
Q

vitamin C deficiency

A

scurvy

30
Q

swelling and bleeding of the gums, sick, bruised and bleeding, pain and swelling, hair and tooth loss,

A

scurvy

31
Q

most prominent in skin and walls of arteries, consists of fibrillar microfibrils

A

elastic fibers

32
Q

consists of tandem repeats of hydrophilic and hydrophobic domains

A

elastin molecules

33
Q

responsible for the elasticity

A

hydrophobic domain

34
Q

responsible for the rubbery elastin

A

desmosine

35
Q

stretched elastin are

A

organized

36
Q

heavily glycosylated proteins

A

proteoglycans

37
Q

one or more covalently attached glycosaminoglycan chain

A

core protein

38
Q

long polysaccharides made of repeating disaccharide units (hexuronic acid and hexoasmine)

A

glycosaminoglycans

39
Q

Function as adaptor proteins to facilitate attachment between different ECM proteins and ECM proteins and sugars

A

adhesive glycoproteins

40
Q

Participate in providing cells with signals required for the development and repair of tissues

A

adhesive glycoproteins (fibronectin and tenacin)

41
Q

Thin planar assembly of ECM proteins that supports epithelia, muscle cells and nerve cells outside of the central nervous system

A

basal lamina

42
Q

Regulated degradation of ECM is essential for several physiological processes such as

A

tissue remodeling, wound healing, organ involution

43
Q

three classes of Zn-dependent proteases

A
  1. MMPs - Matrix metalloproteases
  2. ADAMS (a disintigrin and mellaoprotease)
  3. ADAMTs (ADAMs with a thrombospondin domain)
44
Q

what are metalloproteases regulated with

A

TIMPS (tissue inhibitors of metalloproteases)

45
Q

Genetic bone disorder
Poorly formed and fragile bones
Caused by abnormalities of collagen I structure or synthesis

A

osteogenesis imperfecta

46
Q

Disturbance in the development of cartilage

Mild, severe arrested growth and dwarfism, to congenital lethal

A

chondrodysplasia

47
Q

Inherited disorder with long bone overgrowth, defects of the heart valve and aorta
Mutations in fibrillin 1

A

marfan syndrome

48
Q

Inherited mutations in the production or processing of collagen
Classical form is autosomal domoninat
Characterized by overly flexible joints, stretchy fragile skin.
More severe forms, blood vessel walls, or intestine will rupture
No cure, only manage symptoms

A

ehlers-danlos syndrome

49
Q

two types of adhesive glycoproteins

A

fibronectin and tenacin

50
Q

the basal lamina contains

A

nidogen, laminin, TIV collagen, and perfect that makes a floor”

51
Q

regulated degradation of ECM (type 1 collagen and elastin)

A

MMPS