Signal receptors Flashcards

1
Q

Hormones

A

produced by glands and act on external bodies

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2
Q

polypeptide growth facotors

A

act locally, in the area in which they are produced

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3
Q

Ionotropic receptors

A

‐ ionchannel (gate through which ions can transfer)
‐ receptor, binding spot for ligand.
‐ Synapsis in central nervous system
‐ Acetylcholine receptor; nicotine acetylcholine receptor
- bound by neurotransmitters (acetylochine - nicotonic)
- binding results in changes in ion transport
- extra cellular lignand binding domain, intercellular domain with enzymatic function

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4
Q

G protein coupled receptors

A

‐ Bound by hormones and slow transmission
‐ 7 transmembrane helices
‐ Bound to G‐proteins which hydrolyse guanosine triphosphate (GTP)
to GDP

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5
Q

Kinase receptors

A

‐ Extracellular ligand binding domain
‐ Intracellular domain with enzymatic function
‐ Transfer phosphate from ATP to target peptide

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6
Q

nuclear receptors

A

‐ Present in cytoplasm
‐ After binding of ligand migrate into cell nucleus and bind DNA
‐ Estrogen receptor (often high expressed in breast cancer)
- present in cytoplasm
- migrate after lignand binding to nucleus and and bind DNA

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7
Q

estrogen receptor signaling

A

protein molecule found inside cells that are targets for estrogen

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8
Q

agonist

A

activates receptor and results in a strong biological effect; the maximum
respons by a natural ligand = full agonist

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9
Q

partial agonist

A

activates the receptor but not to its fullest capacity, even not after
maximum binding

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10
Q

antagonist

A

binds but does not activate

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11
Q

inverse agonist

A

results after binding in opposite effect (for example instead of activation
it gives repression)

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12
Q

tyrosine kinase receptors

A

‐ Phosphorylate tyrosine residues in proteins (not serine/threonine)
‐ Transfer phosphate from ATP to target peptide
‐ Extracellular ligand binding domain
‐ Intracellular domain with enzymatic function
‐ critical role in the development and progression of many types of cancer

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13
Q

ErbB 1

A

Upon ligand binding the receptor undergoes a conformational change
 The ligand binding domains are brought together and the cystein rich
region 1 is exposed

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14
Q

ErbB 2

A

no binding ligands, always in open configuration

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15
Q

ErbB 3

A

does not have tyrosine kinase domain

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16
Q

ErbBs

A

have different affinity for ligands

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17
Q

EGFR:EGFR

A

normal signal

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18
Q

ErbB3:ErbB3

A

no signal

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19
Q

ErbB4:ErbB4

A

normal signal

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20
Q

ErbB2:EGFR/ErbB3/ErbB4

A

strong signal

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21
Q

pertuzmab

A

antibody prevents dimerization by blocking CR1

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22
Q

cancer removal

A

‐ Surgical removal of tumors
‐ Chemotherapy: use cytostatic/cytotoxic drugs to remove tumors
‐ Radiotherapy: use radiation to remove tumors

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23
Q

targeted drugs

A

small organic molecules or biologicals, specific

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24
Q

active immunization

A

vaccination

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25
Q

passive immunization

A

rastuzumab  temporal immunization with antibodies that
are biologically made, generally used for treatment

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26
Q

general activation of t cells

A

he tumor generates molecules that deactivate T‐cells, so
these T‐cells will not target the tumor cells.

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27
Q

IGF1

A

produced in liver, enhances growth during puberty

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28
Q

IGF2

A

produced in liver, embyonal important, Scavenger receptor (opruim receptor), Everything that binds on the extracellular domain will be recruited in the
cell and degraded

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29
Q

insulin

A

produced by beta cells of pancreas, important for sugar and fat metabolism, diabetes
- sugar/ fat metabolism

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29
Q

IGF1R and insulin receptor featurs

A

+ 3 S‐S bridges and dimeric structure with L1, CR, L2
+ 4 chains: 2x alpha chain, 2x beta chain
+ activation by ligand binding, not by dimerization (as happens for EGF)
-cell growth

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30
Q

IGF2 features

A

+ Many extracellular domains to which ligands can bind:
 IGF2 binding
 Mannose‐6‐phosphate binding
+ No kinase activity
- everything that binds will be recruited in cell and degraded

31
Q

measure of DNA synthesis

A

labeled
thymidine is added and
amount of thymidine
incorporated in newly
synthesized DNA can be
measured

32
Q

TGFB receptors

A

homodimer connected by disulfate bridge, no tyrosine kinase activity but serine/theonine kinases,Serine/Threonine Kinase (STK) domain of
type II receptor: constitutive active, Joining two type II receptors does not
change activity in terms of signaling, can inhibit growth of poliferation cells but stimulates growth of of fiberblasts

33
Q

active TGFB

A

‐ Growth stimulation for non‐transformed fibroblasts (muscle and bone cells)
‐ Growth inhibition for most cells, including cancer cells!
also shuts down system so not ideal!
-TGFB induces genes for extracellular matrix proteins like collagen and
fibronectin via receptor signaling

34
Q

TGFB type 2

A

stk domains which phosphorilate he GS box in type 1

35
Q

TGFB 1

A

is activated by phosphorylation of Glycine/serine box (GS) afterwards the stk (phosphorylation) domain of type 1 receptors activate, signal sent

36
Q

trastuzumab

A

temporal immunization with ab that are biologically made

37
Q

ipilimumab

A

developed for treatment of melanoma and ab that prevents deactivation of T cells

38
Q

phosphatidylcholines PC

A

class of phospholipids that incorporate choline as a
headgroup. They are a major component of biological membranes

39
Q

enzymes that process PC

A

+ Phospholipase I will split the fatty acid a the first carbon atom of glycerol
+ Phospholipase II will do the same for the second carbon atom
+ PLC cuts at the polar head
+ PLD cut after the phosphate group
glycerophospholipid molecules: phosphatidylcholine
negative OH and positive N, so neutral

40
Q

PL1

A

splits the fatty acids a the first carbon atom of glycerol

41
Q

PL 2

A

splits the fatty acids at the second carbon atom of glycerol

42
Q

PLC

A

cuts the polar head of PC

43
Q

PLD

A

cuts after the phosphate group

44
Q

proteins with an SHw domain that can bind

A

‐ PLC: phospholipase C‐gamma
‐ PI3K: phosphatidyl‐inositol‐3‐kinase
‐ SHC: adaptor protein

45
Q

PI3K

A

converts PIP2 to PIP3 by phosphorelation of C3

46
Q

PLC gamma

A

converts PIP2 in DAG and IP3

47
Q

PIP 3

A

activates PKB/AKT (cytoplasmic STK) which inhibits aptosis

48
Q

DAG

A

activates PKC (cytoplasmic STK)

49
Q

STK

A

serine/theonin kinase

50
Q

PTEN

A

phosphatase, converts PIP3 back to PIP2

51
Q

PKB

A

protein kinase B

52
Q

PKC

A

protein kinase C

53
Q

IP3

A

increases ca+, temporal increase in cell division, muscle contraction

54
Q

RAS

A

G protein, needs GTP as energy and then converts it to GDP, when activated binds to RAF and activates STK activity, RAF will phosphorylate the kinase MEK, which phosphorylates ERK

55
Q

GEF (SOS) for RAS

A

GTP exchange factor, removes GDP and adds GTP

56
Q

GAP

A

GTPase activating protein, regulates activity of GTP ase -> RAS, catalyses the convertion into GDP

57
Q

GRB2

A

+ adaptor molecule between SHC and SOS
+ GRB2‐SOS complex in cytoplasm
+ After SHC activation recruitment to membrane and activation of RAS

58
Q

ERK

A

in a complex with MEK, ERk goes into the nucleus to activate genes, phosphorylates SRF

59
Q

nuclear recptors

A

‐ Present in cytoplasm
‐ After binding of ligand migrate into cell nucleus and bind DNA
‐ Estrogen receptor (often high expressed in breast cancer)

60
Q

promoter

A

+ Contains DNA binding elements for transcription factors (TF)
+ There is variation in DNA sequences, so not all transcription factors can
bind the same DNA element
+ A specific sequence that is bound by a specific transcription factor upon
an extracellular signal is called a response element (e.g. the estrogen
response element, ERE)

61
Q

SRF

A

phosphorylated by ERk, results in transcription of FOS and JUN, recruits RNA polymerase

62
Q

FOS and JUN

A

genes for cell division g0 to g1 phase, transcription factors which form a complex AP-1

63
Q

TPA

A

tumor-promoting agents, resembling DAG, can enter the cell easily because its apolar, it activates PKC

64
Q

growth factors

A

essential for cell growth, multiple gene programs need to be activated, present for up to 8 hours,ErbB, Ins PGF -> all have tyrosine tail phosphorilation

65
Q

PDGF

A

stimulates all three pathways too much, cell growth very harsh, growth factor

66
Q

EGF + Insuline

A

EGF and Insulin can stimulate downstream
pathways independently, but when together
they stimulate parallel pathways and give
synergistic effect

67
Q

GPCR

A
  • Bound to G‐proteins which hydrolyze guanosine triphosphate (GTP) to GDP
    ‐ Activate many different pathways (dependent on which GPCR is
    stimulated), cross membrane 7x, After ligand binding the complex becomes a GEF: GTP exchange factor, activator of G‐
    proteins. The GEF removes GDP from GDP and replace it with GTP
68
Q

Gs alpha/beta-gamma

A

+ stimulatory
+ stimulates ATP conversion to cAMP (cyclic AMP; a derivation of adenosine
monophosphate; its decay is inhibited by caffeine/red bull)
+ cAMP activates many processes, such as glycogen to glucose process
+ adrenergic receptors: adrenaline

69
Q

Gi alpha/beta-gamma

A

+ inhibitory
+ inhibits ATP conversion to cAMP
+ Cannabinoid receptors: cannabis

70
Q

Gq alpha/beta-gamma

A

+ activates PLC
+ converts PIP2 to DAG and IP3
+ Bradykinine receptors: bradykinine (lowers blood pressure)
 GPCRs can activate similar pathways as Tyrosine Kinase
receptors

71
Q

SMAD2-SMAD4 complex

A

binds to promoters of genes with SBE
(SMAD binding element)
+ matrix genes (fibronectin, collagen)
+ genes for growth(inhibition)

72
Q

SMAD2

A

phosphorylated by STK box in TGFB receptors, binds to SMAD4 and the complex enters the nucleus

73
Q

cytokines

A

especially important for the immune system,
interleukins, interferon
‐ Cytokines are bound by receptors without tyrosine or serine‐threonine kinase
activity
‐ However, the receptors are associated with the tyrosine kinase JAK: Just
Another Kinase; Janus Kinase

74
Q

JAK

A

when cytokines activate it activates and phosphorilates the receptor at tyrosine residues, this recruits STAT proteins form cytoplasm

75
Q

STAT

A

signal transducer and
activator of transcription
STAT proteins have SH2 domain which
bind phosphorylated tyrosines,phosphorylated STAT proteins
will move to nucleus, bind STAT
Response Elements and activate
gene transcription