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SIGNAL TRANSDUCTION Flashcards

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1
Q

MAJOR CLASSES OF CELL SURFACE RECEPTOR

A
  1. G-PROTEIN COUPLED RECEPTOR
  2. LIGAND ION CHANNEL RECEPTOR
  3. TYROSINE KINASE RECEPTOR
  4. ENZYMATIC RECEPTOR
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2
Q

SIGNALING MOLECULE RESPONSIBLE FOR CELL INHIBITION/ STIMULATION

A

LIGAND

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3
Q

A SPECIFIC PROTEIN RESPONSIBLE IN BINDING OF SIGNALLING MOLECULE`

A

RECEPTOR

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4
Q

LIPOPHILIC RECEPTOR FOUND WITHIN THE CELL

A

INTRACELLULAR RECEPTOR

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5
Q

LIPOPHOBIC / HYDROPHILIC RECEPTOR FOUND OUTSIDE THE CELL

A

CELL-SURFACE RECEPTOR

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6
Q

HORMONES ARE THE SIGNALLING MOLECULE WHEREIN CELL SEND SIGNALS FROM FAR TARGET CELL

A

ENDOCRINE SIGNALING

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7
Q

SIGNALING MOLECULES RELEASED BY THE CELL ONLT TO AFFECT CLOSE PROXIMITY

A

PARACRINE SIGNALING

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8
Q

CELL RELEASE SIGNALING MOLECULE WITHIN THEMSELVES. IT IS ALSO OBSERVABLE ON TUMOR CELLS

A

AUTOCRINE SIGNALING

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9
Q

HOW DOES SIGNAL TRANSDUCTION OCCUR

A
  1. CELL WILL SYNTHESIS ITS SIGNALING MOLECULE
  2. IT WILL THEN NOW BE RELEASED BY THE SIGNALING CELL
  3. AND TRANSFER THE SIGNALING MOLECULE TO THE TARGET CELL
  4. THE TARGET CELL WILL THEN DETECT THE SIGNALING MOLECULE BY A SPECIFIC RECEPTOR PROTEIN
  5. A CHANGE WILL OCCUR WITHIN THE CELL RESULTING TO A TRIGGERED EFFECT (EITHER STIMULATE/ INHIBITED)
  6. AFTER THE RESPONSE IS GIVEN THEIR WILL NOW BE A TERMINATION OF SIGNAL WHERE THE SIGNALING MOLECULE WILL BE REMOVED FROM THE RECEPTOR
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10
Q

DETERMINES THE SPECIFICITY OF THE LIGAND TO ITS RECEPTOR

A

LIGAND BINDING SPECIFICITY

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11
Q

DETERMINES THE SPECIFIC CELLULAR RESPONSE OF THE CELL

A

EFFECTOR SPECIFICITY

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12
Q

DIFFERENT CLASSIFICATION OF HORMONES

A
  1. SMALL LIPOPHILIC MOLECULE
  2. WATER SOLUBLE HORMONES
  3. SMALL CHARGED MOLECULE
    4 LIPOPHILIC MOLECULE WITH HIGH MOLECULAR WEIGHT
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13
Q

A SPECIFIC LIGAND BINDING TO A G-PROTEIN RECEPTOR WOULD LEAD TO ACTIVATION OF?

A

G PROTEIN

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14
Q

BINDING OF LIGAND WOULD EITHER CHANGE THE CONFORMATION OF THE RECEPTOR ALLOWING EITHER ION EFFLUX OR INFLUX

A

LIGAND ION CHANNEL RECEPTOR

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15
Q

EXAMPLE OF LIGAND ION CHANEL

A

ACETYLCHOLINE

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16
Q

EXAMPLE OF G-PROTEIN

A

SEROTONIN, GLUCAGON, EPINEPHRINE

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17
Q

THESE RECEPTORS DO NOT EXHIBIT INTRINSIC CATALYTIC ACTIVITY, BINDING TO IT WILL TURN THE RECEPTOR INTO DIMERIC

A

TYROSINE KINASE RECEPTOR

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18
Q

WHAT WILL HAPPEN IF THE TYROSINE KINASE RECEPTOR ACTIVATES

A

THERE WILL BE A SUCCESSIVE ACTIVATION OF TYROSINE KINAE DOWNSTREAM

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19
Q

EXAMPLE OF TYROSINE KINASE RECEPTOR

A

GROWTH FACTOR, CYTOKINE, INTERFERON

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20
Q

EXAMPLE OF ENZYMATIC RECEPTOR

A

GROWTH FACTOR AND INSULIN

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21
Q

LIGAND ACTIVATES THIS RECEPTOR’S INTRINSIC ENZYMATIC ACTIVITY

A

ENZYMATIC RECEPTOR

THIS RECEPTOR IS AN ENZYME AWAITING ACTIVATION BY A LIGAND

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22
Q

SECOND MESSENGERS:

A
  1. Inositol phospholipids (phosphoinositides)
  2. Inositol 1,4,5 triphosphate (IP3)
  3. 1,2 diacylglycerol (DAG)
  4. 3’ 5’ cyclic AMP (cAMP)
  5. 3’ 5’ cyclic GMP (cGMP)
  6. Calcium
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23
Q

OTHER SIGNALING PROTEINS

A
  1. GTPASE SWITCH PROTEIN

2. PROTEIN KINASE

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24
Q

2 TYPES OF GTPASE SWITCH PROTEIN

A
  1. TRIMERIC G PROTEIN

2. MONOMERIC RAS AND RAS LIKE PROTEIN

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25
A G-PROTEIN THAT IS DIRECTLY ASSOCIATED WITH RECEPTORS
TRIMERIC G PROTEIN
26
A SWITCH PROTEIN THAT IS INDIRECTLY ASSOCIATED WITH THE RECEPTOR
MONOMERIC RAS AND RAS LIKE PROTEIN
27
AN ENZYME THAT BINDS GTP TO RELEASE PHOSPHATE AS ENERGY SOURCE. THIS ALSO STANDS AS A MOLECULAR SWITCHES
GTPASE SWITCH PROTEIN
28
TYPE OF SWITCH PROTEIN THAT ACTIVATES REACTION
GTP
29
TYPE OF SWITCH PROTEIN THAT INHIBITS REACTION
GDP
30
A SIGNALING PROTEIN THAT ACTIVATES IN RESPONSE TO STIMULATION OF SIGNALING PATHWAYS, IT ALSO CARRIES OUT PROCESS OF PHOSPHORYLATION
PROTEIN KINASE
31
A SIGNAL PROTEIN THAT DOES NOT PARTICIPATE IN CATALYTIC ACTIVITY BUT CONTAINS DOMAINS THAT ATTACH TO OTHER PROTEIN TO MAKE THEM FUINCTIONAL
ADAPTER PROTEINS
32
DIFFERENT TYPES OF SIGNALING PATHWAY
1. G-PROTEIN COUPLED RECEPTOR SIGNALING (GPCR) 2. RECEPTOR TYROSINE KINASE SIGNALING (RTK) AND RAS 3. MITOGEN ACTIVATED PROTEIN SIGNAL (MAP)
33
GPCR ARE LINKED IN WHAT TYPE OF G-PROTEIN
TRIMERIC G PROTEIN
34
HOW MANY TRANSMEMBRANE DOMAINS AN GPCR HAVE
7 TRANSMEMBRANE PROTEIN
35
WHY DOES TRANSMEMBRANE DOMAIN IMPORTANT IN GPCR
THE TRANSMEMBRANE DOMAINS OF GCPR BINDS TO LIGAND CAUSING FOR THE TRIMETRIC G PROTEIN TO BE ACTIVATED
36
WHAT ARE THE SUBUNITS OF TRIMERIC G PROTEINS
α, β, γ
37
DOES GTP INITIALLY ATTACHED TO INACTIVE FORM OF G PROTEIN TRUE OR FALSE
FALSE GDP INITIALLY ATTACHED TO THE INACTIVE FORM OF G-PROTEIN WHILE GTP ATTACHED TO THE ACTIVE FORM OF G-PROTEIN
38
WHAT HAPPENS IF TRIMERIC G-PROTEIN BINDS TO A LIGAND?
GDP WILL BE RELEASED CAUSING FOR GTP TO BIND ON THE ALPHA-G-PROTEIN
39
WHAT WILL HAPPENED IF ALPHA-G-PROTEIN IS ACTIVATED
GTP WILL HYDROLYZE FORMING PHOSPHATIDYL INOSITOL (Pi) WHICH WILL BE RELEASE RESULTING FOR THE GDP IN THE ALPHA SUBUNIT TO RETURN TO ITS FORMER POSITION WITH Gβ AND Gγ
40
GPCR ACTIVATES GENERATION OF THE FOLLOWING 2ND MESSENGERS
cAMP IP3 DAG Ca++
41
WHAT ENZYME FORMS cAMP FROM ATP
ADENYLY CYCLASE
42
A 2ND MESSENDGER PRODUCED FROM HYDROLYSIS OF PYROPHOSPHATE FROM ATP
cAMP
43
1. _____ A SECOND MESSENGER THAT REGULATES CARBOHYDRATE METABOLISM AND ACTIVATES 2. _______
1. cAMP | 2. ACTIVATES GLYCOGEN PHOSPHORYLASE PROMOTING GYCOGENOLYSIS
44
DIFFERENT CARBOHYDRATE METABOLISM OF cAMP
1. GLYCOGENOLYSIS - cAMP ACTIVATES GLYCOGEN PHOSPHORYLATION 2. GLYCOGENESIS - cAMP INHIBITS GLYCOGEN SYNTHASE 3. cAMP IS INHIBITED BY INSULIN 4. cAMP IS ACTIVATED BY EPINEPHRINE AND GLUCAGON
45
WHAT ACTIVATES cAMP
GLUCAGON AND EPINEPHRINE
46
WHAT SUBSTANCE INHIBITS cAMP
INSULIN
47
ENZYME CONVERTS PHOSPHATIDYL INOSITOL (Pi) INTO PHOSPHATIDYL TRIPHOSPHATE (PIP3) AND DIACYLGLYCEROL (DAG)
PHOSPHOLIPASE C β
48
SUBSTANCE RELEASE IN RESULT TO INCREASED IP3
CALCIUM
49
WHAT ACTIVATES KINASE C TO PHOSPHORYLATE
DAG AND CALCIUM
50
SUBSTANCES DERIVED FROM PHOSPHOINOSITIDES
1. PHOSPHATIDYL INOSITOL (Pi) 2. PHOSPHATIDYL PHOSPHATE (PIP) 3. PHOSPHATIDYL BI[HOS[HATE (PIP2) 4. PHOSPHATIDYL TRIPHOSPHATE (PIP3)
51
WHAT WOULD RELEASE CALCIUM FROM THE ENDOPLASMIC RETICULUM
PHOSPHATIDYL TRIPHOSPHATE (PIP3)
52
WHAT IS THE INACTIVATED AND ACTIVATED FORM OF RTK
MONOMER - INACTIVATED WITH GDP | DIMER - ACTIVATED WITH GTP
53
WHAT WILL HAPPEND IF A LIGAND BINDS TO RTK
AUTOPHOSPHORYLATION OF TYROSINE RESIDUE IN CYTOSOLIC DOMAIN WILL BE ACTIVATED
54
AN INTRACELLULAR MONOMERIC OF GTPASE
RAS
55
WHAT IS THE ACTIVATED AND INACTIVATED PROTEINS OF RAS
GEF - ACTIVATED PROTEIN BECAUSE OF GTP | GAP - INACTIVATED PROTEIN BECAUSE OF GDP
56
AN ADAPTER PROTEIN FOR RTK
GRB2
57
2 SUBTYPE GRB2
SH2 AND SH3 DOMAINS
58
GRB2 SUBTYPE THAT BINDS TO PHOSPHOTYROSINE RESIDUE
SH2 DOMAIN
59
GRB2 SUBTYPE THAT BINDS TO ACTIVATE SoS
SH3 DOMAIN
60
FUNCTIONS AS GEF (GUANINE NUCLEOTIDE EXCHANGE PROTEIN) OF RTK
SoS THIS CONVERTS GDP-RAS TO GTP-RAS
61
A SIGNALING PATHWAY THATTRANSLOCATES TO THE NUCLEUS TO PHOSPHOSRYLATE PROTEIN INVOLVED IN TRANSCRIPTION
MITOGEN ACTIVATED PATHWAY (MAP)
62
SEQUENCE OF PROTEIN THAT BINDS IN THE ACTIVE OF RAS IN ORDER TO BE ACTIVATED
1. RAF | 2. MEF
63
ACTIVATED BY RAS TO BE RECRUITED IN THE MEMBRANE AND IN ORDER TO ACTIVATE MEK
RAF ONCE RAS IS ACTIVATED, RAF WILL BE RECRUITED TO THE MEMBRANE AND WILL BE ACTIVATED. RAS WILL RETURN TO ITS INACTIVE STATE WILL RAF WILL ACTIVATE MEF IN ORDER TO ACTIVATE MAP KINASE
64
A PROTEIN THAT ACTIVATES MAP
MEF
65
A CIS ACTING DNA SEQUENCE IN GENE
cAMP RESPONSE ACTING ELEMENT (CRE)
66
cAMP RESPONSE ACTING ELEMENT IS ACTIVATED BY WHAT SECOND MESSENGER
cAMP
67
TRANSCRIPTION FACTOR WHERE CRE BIND
CRE-BINDING PROTEIN (CREB)
68
ALLOWS CREB TO STIMULATE TRANSCRIPTION
CBP/300
69
SEQUENCE F G-PROTEIN CAMP PATHWAY
1. cAMP DEPENDENT PROTEIN KINASE (cAPK) WILL BE ACTIVATED BY cAMP 2. cAPK WILL DIRECTLY GO TO THE NUCLEUS AND PHOSPHORYLATE CREB 3. CREB WILL NOW BIND TO CO-ACTIVATOR CBP/300

BIOCHEMISTRY (3 decks)

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