Cell matrix signal Flashcards

1
Q

extracellular matrix surround cells

A

chondrocytes - mesenchymal cell

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2
Q

cells sitting on matrix

A

epithelial, lining tube, skin

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3
Q

matrix

A

insoluble, amalgam of protein + proteoglycan = bed around cell
can be cell signalling molecules as well

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4
Q

dermis

A

below epithelial in skin

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5
Q

matrix function

A

for strength - tensile and compress - when pulled or pressed - returns back to original form

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6
Q

roles of matrix

A

integrate cells into tissue and limits it by setting boundaries
signal info to cells about surroundings

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7
Q

skin - dermis

A

loose connective tissue laid with many fibres

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8
Q

skin - dense connective tissue

A

laid - more defined regularly packed sheets

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9
Q

basement membrane

A

basal lamina between blood vessel, muscle, epithelium

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10
Q

basement membrane signalling function

A

migration - during development/ healing

cell survival and differentiation

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11
Q

basement membrane physical function

A

tissue border
strengthens
filter effect

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12
Q

basement membrane in ECM

A

structural protein
proteoglycan
cell adhesive protein

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13
Q

tensile strength by collagen

A

around 7 forms - act as fibrils/associated to fibrils or sheet

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14
Q

tensile strength characteristic

A

major structural protein and most abundant protein in body

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15
Q

collagen sequence

A

repeat of Gly-XY sequence 300-400 times

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16
Q

collagen helix

A

collagen sequence folds
LH helix than alpha
stable

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17
Q

trimeric collagen (TC)

A

3 helices wrap - RHS helix

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18
Q

RHS helix

A

right hand super helix

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19
Q

Gly-XY

A

XY - often lysine/ proline

modify to -OH form

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20
Q

fibrillar collagen

A

include collagen I, II, III

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21
Q

fibrillar collagen packing

A

loose connective - lots of collagen III

dense connective - more collagen 1 and 2

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22
Q

TC secreted

A

in ECM in regular array - places in off set array system

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23
Q

TC region

A

at high dense and less protein = bands in TEM and SEM

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24
Q

TEM/SEM

A

transmission/scanning e- micrograph

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25
collagen formation | non-collagenous region (no GlyXY)
N and C terminal ends
26
collagenous repeat
at the centre
27
collagen formation
produced in ER and secreted
28
some XY
hydroxylated and other (selected hydroxylysines) - glycosylated
29
trimeric Shelix
3 chains (pro alpha chains) weaved at C-terminus to N which is then placed in secreted vacuole for secretion out of Golgi
30
shift base
used to form covalent linkage between trimeric collagen fibril
31
collagen formation on secretion
C and N terminal non-collagenous region is remove = mature collagen molecule - able to lay down in arrays into fibrils cleaved by enzyme out of the cells
32
C and N terminal non-collagenous
prevent fibril forming inside cell | if removed inside cell - insoluble in Golgi and vacuole therefore kills the cell
33
collagen molecules characteristics
long half life | degraded/reformed at stress, healing, cell infiltration etc
34
mutation of enzyme used to cleave
can't form fibrils | detect in collagen deposition therefore weakens it
35
MMP
matrix metalloproteinase
36
MMP function
released as they migrate through CT | regulate breakdown of collagenous matrix in its modelling
37
disease - ascorbic acid deficiency
scurvy - in absence collagen trimer and fibrils less stable - weaker acid - cofactor for XY hydroxylase - for collagen crosslink
38
elastin
fibres formed of polymer elastic | monomeric tropoelastin
39
cross linkage
between elastin by hydroxy linkages | increase linkage over time
40
returning to original of elastin
lacks defined structure | highly HP = random coil which returns back
41
properties of elastin in tissues of
blood vessels lungs elastic cartilage
42
synthesis of elastin
during foetus and childhood | but very limited in later life = wrinkles
43
elastase
secreted by neutrophils destroyed elastin replaced with collagen after fibres are broken down by inflammation = fibrosis and scarring
44
proteoglycan
give compressive strength by water retention | core has highly charged sugar attached and attract H2O and Na+ = hydrated porous gel
45
hydrated porous gel
allow motion of nutrient and waste products about isolated cell e.g. chondrocytes
46
sugar and GAG
repeated sequence of disaccharides (tetrasaccharide link) and GAG sequence
47
GAG sequence
glycosaminoglycan sequence
48
proteoglycan function - resistant to compression
alter charge density on pressure | charged chains repel and water gel like
49
proteoglycan function - highly charged
binding site for many molecules - GF(FGF) and cytokines (TGFb) released on proteoglycan damage
50
proteoglycan function coreceptor
inducer for GF
51
cell adhesion molecule
fibronectin | laminin
52
fibronectin
in loose connective tissue | disulphide linked - dimer
53
6 domain in fibronectin
``` self association collagen binding cell binding heparin binding C-terminus ```
54
function of 6 domain in fibronectin
interact with different ECM molecules
55
C-terminus of 6 domain
small (RGD) and synergy region
56
RGD
Arg, Gly, Asp | bind to integrin - fibronectin act as link to surface and matrix
57
collagen binding and self-association - 6 domain
bind multiple fibronectin
58
heparin binding region
within heparin sulphate
59
cell binding of fibronectin via specific integrin receptor induces
remodelling of cytoskeleton cell migration proliferation
60
remodelling of cytoskeleton
signal cell to attach
61
cell migration
move - attach to surrounding - transport
62
proliferation of integrin receptor
in healing as example
63
laminin
a, b and y chain = trimer
64
laminin - G-domain
bind to receptor and integrin receptor and other receptors
65
sheet of laminin
trimer interacts in presence of Ca2+
66
self assemble mesh
centre go down and bind to receptor on cell surface | interacting with proteoglycans, collagen and cell receptors
67
basement membrane signals
migration, cell survival and differentiation
68
losing receptor in mesh
cell has tendency to die
69
integrin families matrix receptor
heterodimeric receptor - ab subunit separate
70
matrix receptor has transmembrane region
bind to linker and attach to part of cytoskeleton
71
specific integrin - function
bind to specific ECM components especially laminin and fibronectin
72
integrin
nucleation site for actin polymerisation = stable contact between contractile machinery and ECM linkage from cytoskeleton - in cell and matrix out of cell
73
cell contract and movement
pull on actin filament and transfer force ECM | allow cell to generate traction
74
traction of cells for movement
lamellipodia | filopodia
75
lamellipodia (Lp)
push | large amounts of integrins
76
filopodia (Fp)
spike | extension
77
cell contraction and movement - migration
heals wounds | immune cell and metastasis (tumour)
78
moving forwards - in terms of Lp and Fp
Fp interacts with matrix and convert to Lp to move
79
focal adhesion
area of clustering integrin binds to specific sequence on ECM e.g. RGD receptor or more complex site
80
roles of focal adhesion
anchor cells to ECM migration signal from ECM
81
focal adhesion - actin filaments
comes in from cytosol and linker protein attach to integrin receptor - sits through membrane and binds to ECM
82
linker proteins on actin filments
vinculin | alpha-actinin
83
assembly of focal adhesion
has many fibre therefore huge cluster of integrins
84
hemidesmosomes
specific integrin bind laminin in BM to intermediate filaments (keratin) via plectin
85
BM
basement membrane
86
desmosomes
similar to hemidesmosomes | only has keratin filaments
87
difference between hemidesmosomes and desmosomes - function
act as interaction between keratin filaments between cells | while hemidesmosomes - intermediate filaments and BM
88
defect in molecule producing hemidesmosome/receptor/laminin
weak attraction from ECM to BM therefore when force added on cell - pull away = Epidermolysis bullosa
89
integrin clustering causes | with example
other signalling molecules bind to focal adhesion sites concentrated at site e.g. FAK - at high conc - function activate
90
ECM attached to integrins pathways
actin organisation cell spreading cell motility survival proliferation
91
FAK
focal adhesion kinase