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BMS 2 > ECM > Flashcards

ECM Flashcards

1
Q

Structural Proteins

A

Colalgen-strength

Elastin-resilience

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2
Q

Glycosaminoglycans

A

complex sugars that bind water and resist compression

Negatively charged

in joints/eye

Binds to proteoglycans

GAG

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3
Q

Proteoglycans

A

Proteints that vacantly bind to GAG

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4
Q

Adhesive glycoproteins

A

fibronectin, laminin, etactcin

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5
Q

Ground substance

A

Macromoleuclar compoentts-

structural proteins, glycosaminoglycans, proteoglycans, adhesive glycoproteins

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6
Q

Ground subtance+ cells

A

connective tissue

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7
Q

What is under the epithelium

A

basal lamina then connective tissue

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8
Q

Parenchyma

A

specialized epithelium

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9
Q

2 main regions of basal laminia + under that

=total is basement membrane

A

electron dense region underlying epithelial laer (rara/lucida/interna)-this part binds to hemidosmosomes

Much more electron dense under that-lamina densa

lamnia reticularis-made by fibroblasts, type 3 collagen

can only see difference in basement membrane with EM

under that is the stroma

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10
Q

what mediates continuum between cell surface and ecm

A

syndecans and integrins

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11
Q

Basement membrane

Basement membrane at EM and whats inside them

A

Can see with LM

Basal-laminin, fibronectin, coallagen, proteoglycans, enactin

Reticular-type 3 collagen (reticular fibers)

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12
Q

type 3 collagen is known as

A

reticular fibers

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13
Q

Stroma characteristic

A

fell cells, lots of matrix, dense irregular connective tissue

some tissues have specialized fibroblasts that secrete in stroma-secrete bone/cartledge

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14
Q

Collagen structure + facts

A

most abundant protein in body

individual collagen form triple helix, extensive, and can bind to other triple helixes to make huge molecule

Gly-x-y-gly-h atom (h is in middle of helix) side chain-repeats and fits inside helix
-X,Y s often P or K and can be hydroxylated-contributes to hydrogen binding or can be deaminited

K-contributes to cross linking to produce fibrils

mutation in glycine-disease

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15
Q

Fibril

A

Many triple helixes of collagen

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16
Q

Type 1, 2, 3 collagens

A

All form fibrils

1-bone , skin tendons-90% of body collagen

2-carledge

3-skin, blood vessels-exppand and contract-in stroma

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17
Q

type 7 collagen

A

anchors fibrils

beneath stratified squamous epithelia

stroma/blistering

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18
Q

collagen synthesis pathway

A

synthesized in city, bind SRP, ER, secreted

  • hydroxlate some proteins and lysine
  • glycoslate selected hydroxylysines
  • extension peptides keep from multimerizing in cell-but does a little enough to be exerted through sec vesicle
  • triplex forms-seceded out of cell as pro collagen
  • made into tropocollagen by removing extension peptides
  • self assemble into huge fibers
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19
Q

what hydroxylates glycine and prolines in collagen

A

vitamin c

can’t replace weak collagen with stronger-scurvy-teeth fall out

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20
Q

lysyl oxidase

A

cross-links tropocollagen molecules

DRAW SLIDE 10

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21
Q

Collagen type 3

A

Reticular-silver stain

in lymph nodes

more carbs thiner fibrils, more branches, fewer bundles

IMMUNE STRUCTURES

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22
Q

fibril associated collagen

A

ex-typle 9

interruption of triple helix-less rigid-form hinge

extensio peptides generally retained

Decorates outside of type 2 collagen (in cartilage)-9 is on outside

Join integrity

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23
Q

collagen type 4

A

network forming

major component of basement membrane+ basal lamina

extensio peptides are never cleaved-c and N termini interact=form dimer

N terminus has origination out of plane-vertical extensions-multilayer

  • chicken wire array
  • many of these form stacked network of sheets
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24
Q

Type 7 collagen

A

if mutated blistering-between epithelium and basement membrane

monomers make dimer, interact between stroma and lamina dense, keep storm attached to lamina densa

basement membrane NOT intact

BELOW LAMINA DENSA

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25
Q

type 12 collagen

A

transmembrane protein

anchors fibrils=monomers interact via c-terminal disulfide bonds-interacts with later densa
-N nd C not cleaved-interact to make anchoring fibrils

interacts with lamina densa

if this is messed up-blistering disease, epithelial cells peel away-basement membrane intact

ABOVE LAMINA DENSA

26
Q

Mutants with shortened C-termini

A

cannot associate-blistering below BM

27
Q

type 4 aka

A

lamina densa

28
Q

Which collegians retain extension peptides during assembly

A

network forming

29
Q

Which collagens form fibrils

A

1,2,3

30
Q

which collagen stains dif and why

A

3 b/c increased CHO

31
Q

elastin

A

highly cross linked monomers

  • assembed extracellularly
  • provide resillence
  • elsatin fibers are surrounded by microfibrils composed of fibrilin
32
Q

marfan sydnrome

A

mutation in fibrilin 1

overgrown lengthening of limbs

weak elastic fibers

distended aorta-prone to rupture

33
Q

ECM disorders

  • hyperextendable skin
  • altered eslastin
  • epidermolysis bullosa
A
  • too much type 3 collagen-skin very stretchy
  • no recoil
  • epithelium and basement membrane peeled away
    - type 7 collagen anchoring fibrils are disrupted
34
Q

GAGs

A

glycosaminoglycans

negatively charged, bind to water, resist compression

molecules repel each her at negative charge, but attract water-fill a lot of space

can be sulfated or not sulfated + attached to protein or not

35
Q

Aggrecan

A

aggrecan+type ii collagen+type 9+linker proteins

exist in chrdrocyte matrix-cartledge

Make up a lot of space

Forms aggregates with hylarunic acid

36
Q

hyaluronic acid

A

gag that is non sulfated and not attached to protein

37
Q

Perlecan-functions

A

basal laminae, strucural and filteing fucntion in basal lamina

38
Q

Syndecan 1

A

fibroblast and epithelial cell surface

cell adhesion-co receptor
-bind to growth factors and present to dif receptors

connection between ECM and internal signaling pathway

39
Q

Adhesive glycoproteins

A

attach to ECM, specific sequences-RGD, can interact with specific reports on cell (integrins)

laminas and fibronectins can bind many different molecules

has regions that bind to collagen/otehr components of ECM

Laminin’s and fibronectins

40
Q

Integrin alpha6beta1

A

binds laminin

41
Q

Laminin

A

major component of basal lamina

bind to cell surface receptors (integrins)-via RGD, type 4 collagen, and other adhesive proteins

42
Q

Fibronectin

A

reduced in tumor cells-can allow uncontrolled growth

integrin alpha5 beta1-cell attachment site

two binding sites for interns, collagen, heparin, and fibrin

Modular domains

43
Q

ECM componenets interacting

A

everyone interacts with everyone-bile network of different interactions depending on tissue type

44
Q

Integrin binding

A

both to collagen and laminin

45
Q

Are all gags bound to proteins?

A

no-hyalurnic acid is not

46
Q

Lamin and fibronectin can only bind to oneanotehr molecome?

A

no-they have several modular domains

47
Q

which collagens are found in ECM

A

aggrean, 2 , and 9

48
Q

What is found in basement membrane

A

Perlecan (proteoglycan) and laminin

49
Q

Integrins

A

Mediate communication between ECM and internal cell signaling by interacting with cytskeleton

dimers-not always active-help wbc/clots enter cell-would be bad if could enter whenever it wanted

both subunits involve din binding substrate via RGD sequences

beta subunts binds cytoskeleton (actin usually) that can initiate formation of signaling comeplexes

50
Q

Focal adhesion complex

A

Acts with actin and itegrin to send signal into cell

51
Q

integrins 2

A

Organize cytoskeleton-bind actin bdining proteins and the actin

focal accession forms at site of bounds intern via Rho GTPase

Recurits signalling moleculees
-focal adhesion kinase

Two transmembrane subunits

52
Q

focal adhesion kinase

A

focadhesion kinase is signalling molecule that when active can phosphoryalte tyrosine residue-different signaling molecule form focal adhesion complex
-integrins active, assemble actin cytoskeleton, and organize signaling molecules

53
Q

Major classes of interns

A

beta 1-bind ECM to fibronectin or laminin

beta 2-white blood cells

3-platelets

40desmosomes, bind specific laminin type

54
Q

what are integrins important for

and what diseases are there

A

important for entry of abc into tissue, mediated by beta2

beta 2 mut in these leads to leukocyte adhesion deficeincy-no adhere to endothelium

beta 3 ingretins-glanzmans disease-inability to bind fibrinogen during clotting

55
Q

Integrins and syndecans

A

cell membrane proteins that both interact with ECM components

intern with fibronectin-which is moldular-can bind other stuff like collagen/proteoglycans

interns can also bind to laminins along with syndecans

b1 integrins

56
Q

b4 integrin

A

hemidesmosomes

just one of man systems involved in keeping epithelium bound to underlying tissue

mutation in beta 4-integrin can’t assemble-cant bind laminin 5 or collagen 12-epithelium peels away

pachorning filaments bind surface of epithelia to lamina dens

57
Q

Intracellular signallinga nd integrins

A

Intergrin binding regulates intracellular signaling but other intracellular pathways can also regulate intern activity

things can go out to in and in to out
-done by conformational chages

58
Q

integrin activation

A

something binds to signal receptor, receptor activates integrin through intracellular signaling events, integrin then binds to matrix
-activation is conformational change

-lymphocyte binding to endothelium (b2) and platelet bindign to fibrinogen (b3)

59
Q

endothelium and platelet bindign to fibrinogen

A

(b2) and (b3)

60
Q

lympho binding to endothelium via selectin

A

b2 integrin conormation changes allowing binding to endothelial surface receptors

during roll of lympho-integrins are activated-straighten up and spread out chains

selectins not only sow WBC down, but initiate signal needed to convert intern beta 2 on WBC to active, so can move into tissue

the integrins are on lympho

BMS 2 (41 decks)

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