Chapter 14 Flashcards

(57 cards)

1
Q

Signal transduction

A

the pathway that converts the information from a molecular signal to a physiological response

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2
Q

Steps in a standard signal transduction pathways:

A
  1. Signal release
  2. A membrane-bound receptor on another cell binds the ligand and makes an intracellular conformational change
  3. An intracellular secondary messenger is generated to amplify the signal
  4. The cell responds to the secondary messenger by activating pumps, pathways, gene expression, etc
  5. The signal must be terminated after the response
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3
Q

Signal release

A

. A diffusable extracellular primary messenger or “ligand” is released.

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4
Q

ligand

A

extracellular primary messenger

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5
Q

Often in signal transduction there are (multiple) stages

A

amplification

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6
Q

Epinephrine + B-Adrenergic receptor

A

Energy-store mobilization

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7
Q

Insulin + insulin receptor

A

increased glucose uptake

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8
Q

Epidermal growth factor (EGF) + EGF receptor

A

Expression of growth-promoting genes

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9
Q

Examples of secondary messengers

A

cAMP, cGMP, C+, IP3, DAG

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10
Q

Example of signal or primary messenger

A

epinephrine

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11
Q

epinephrine

A

a hormone released by the adrenal gland in response to stress

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12
Q

Does epinephrine enter the cell?

A

No, instead it “pushes the doorbell” of a specific 7TM receptor protein to effect the “fight or flight” responses (second messengers are produced inside the cell)

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12
Q

largest family of receptors

A

7TM helix receptor family

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13
Q

How many 7TM receptors do humans have

A

800

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14
Q

7TM receptors are important for the

A

senses

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15
Q

What flavors are mediated by 7TM receptors

A

sweet, bitter, and umami flavors (NOT sour or salty)

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16
Q

Vision works with

A

rhodopsin, another 7TM protein

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17
Q

Smell is mediated by hundreds

A

olfactory receptors, also 7TM receptors

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18
Q

The 𝛽AR receptor acts as

A

GNEF

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19
Q

carazolol

A

epinephrine blocker

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20
Q

G-proteins

A

3 subunit complexes activated by GTP

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21
Q

Cyclic amp (cAMP) exerts its effects through

A

protein kinase A (PKA)

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22
Q

Phosphorylate proteins with the aa sequence

23
Q

growth-regulating kinases

A

PKA, PKB, PKC

24
PKA is a four-subunit enzyme
2 catalytic and 2 regulatory
25
Each PKA regulatory subunit functions as
kinase inhibitor by binding the catalytic site with a non-functional pseudosubstrate domain
26
After each PKA binds 2 cAMP each
the R subunits dissociate from the C subunits so they are active
27
Parts of the G protein
-α subunit -Beta subunit -GDP -fatty acid -Y subunit
28
Which of the subunits, when activated, associates with adenylyl cyclase (adenylate cyclase) and enables it to assume a more catalytically active conformation
29
Glucagon is a hormone that is released when
glucose in the blood is low
30
Glucagon uses a G protein signaling to
promote glycogenolysis
31
Glucagon released into the blood which will
1. Glucagon binds G Protein 2. G protein releases GDP and binds GTP which activates protein 3. Activated G protein activates adenylate (adenyly) cyclase 4. adenylate cyclase converts ATP to cAMP 5. Cyclic AMP activates protein kinase A (PKA) 6. kinase A phosphorylates glycogen phosphorylase 7. Glycogenolysis is promoted.
32
adenylate cyclase converts ATP to
cAMP
33
free catalytic PKA subunits interact with proteins to
phosphoryate Ser or THR residues
34
termination of a response in the GPCR, or 7TM receptor
1. The G𝛼s subunit turns itself “off” by hydrolysis of GTP->GDP. This allows it to re-associate with the inhibitory 𝛽𝛾 subunits. 2. The ligand dissociates from the receptor, which resumes its inactive conformation. 3. The receptor is inactivated by phosphorylation of Ser or other residues on its intracellular domain. 4. The receptor itself is turned off by dissociation of epinephrine
35
phosphorylates
introduce a phosphate group into (a molecule or compound).
36
One of calmodulin’s main roles is to
to activate calmodulin-dependent protein kinases (CaM kinases).
37
How is (CaM kinases) activated
Ca2+ induces calmodulin to bind a specific peptide on CaM kinase 1
38
The binding of insulin to the insulin receptor alters
conformation of the two 𝛽 subunits in the cytoplasm
39
tyrosine kinases
𝛽 subunits altered by insulin+insulin receptor
40
phosphotyrosines are recongized by
“SH2” domain proteins
41
SH2 domains are known to
bind phospho-tyrosine residues
42
Insulin-receptor substrates (IRS) bind
phospho-tyrosines adjacent to phosphoinositides
43
Because Akt is not achored to the membrane
it can diffuse to cytoplasmic targets proteins that traffic GLUT4 receptors to plasma membrane and stimulate glycogen synthesis
44
RGF pathway is turned off by
GTP hydrolysis by Ras
45
Needed to terminate EGF pathway
Phosphatases of the activated Raf, MEK, and ERK kinases
46
Signal transduction and cancer
Src tyrosine kinase and Abl tyrosine kinase
47
Gleevec or Imatinib
drug that specifically inhibits the abl tyrosine kinase by binding near the ATP binding site to competitively inhibit the kinase
48
Abl tyrosine kinase causes
chronic myelogenous leukemia (CML)
49
IP3 ->
Ca+
50
PIP2 and PLC ->
DAG and IP3
51
cAMP ->
PKA
52
Ca2+
PKC
53
ATP and adenyly cyclase
cAMP
54
DAG ->
PKC
55
In the context of smooth muscle contraction, which second messenger would be a direct antagonist of
IP3
56
antibody targeting receptor
herceptin and erbitux