Biochemical Signaling Flashcards

1
Q

What do target cells have to respond to the hormone?

A

a specific receptor for the hormone.

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2
Q

What kind of hormones are pancreatic islet hormones?

A

peptide hormones

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3
Q

What do pancreatic islet hormones do?

A

peptides that regulate glucose metabolism: insulin.

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4
Q

What do catecholamines control?

A

controls glucose and lipid metabolisms.

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5
Q

What hormone controls lipid metabolism and controls glucose?

A

catecholamines

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6
Q

What are catecholamines?

A

Derivatives of tyrosine.

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7
Q

What are catecholamines targets?

A

alpha and beta adrenergic receptors.

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8
Q

What hormone regulates muscle function?

A

catecholamines.

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9
Q

What are steroid hormones?

A

derivatives of cholesterol.

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10
Q

What do steroid hormones include?

A

glucocorticoids, mineralocorticoids, and sex hormones.

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11
Q

Which major class of hormones slip right through the membrane and don’t need help?

A

steroid hormones

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12
Q

What are growth hormones?

A

peptide hormones targeting receptors on the bone, muscle, and connective tissue.

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13
Q

Growth hormones are what kind of hormones?

A

peptides

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14
Q

What hormones control the rate of growth?

A

growth hormone.

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15
Q

What are the two hormonally active catecholamines that adrenal medulla synthesizes?

A

Norepinephrine (Noradrenalin) and Epinephrine (Adrenalin)

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16
Q

What do adrenergic receptors contain?

A

Agonist and Antagonist?

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17
Q

An agonist replicates what?

A

the effect of a hormone.

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18
Q

What effect will an antagonist replicate?

A

bind on to the hormone and compete for the substrate.

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19
Q

What occurs to the growth hormone receptor upon hormone binding?

A

dimerizes

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20
Q

What does hormone binding induce?

A

receptor dimerization that is necessary for signal transduction.

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21
Q

Describe the structure of the growth hormone?

A

a 4 helix bundle. 191 amine acids comprises it

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22
Q

How does the hormone receptor get the signal across?

A

has to get transduce through the membrane inside the cell.

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23
Q

What occurs in the autophosphorylation activates insulin receptor?

A

dimerization may or may not require ligand bonding and one subunit phosphorylates the other.

24
Q

What occurs to the loops in the Tyrosine Kinase Domain of Insulin Receptor?

A

Tyrosines flanking the active site and they must phosphorylate to remove inhibitory loop.

25
Q

What occurs once tyrosines phosphorylate to remove inhibitory loop?

A

the loop opens up, is free to phosphorylate other substrates.

26
Q

What are autoinhibited?

A

Unphosphorylated kinases

27
Q

What moves out the way upon phosphorylation?

A

activation loop.

28
Q

What is SH2 (Sark)?

A

a kinase involved in a signal transduction.

29
Q

SH2 binds to what?

A

Phospho-Tyr Residues

30
Q

What kind of mechanisms occur between P-Tyr and other proteins?

A

Docking mechanism

31
Q

What does SH3 do? (Sark Homology 3)?

A

Binds polyprotein sequences and other proteins. These signaling cascades get turned on this manner.

32
Q

Where is the signal amplified in the Ras Signaling Cascade?

A

amplified through this cascade of phosphorylation.

33
Q

What is the end results in RAS signaling Cascade?

A

phosphorylation and activation of transcription factors that turn on genes to alter the phenotype of the cell.

34
Q

How do you prevent promiscuous cross talk?

A

Location, Localize kinases to sites in the cell where their function is needed.

35
Q

What are crosstalks?

A

Intermingling pathways of signal transduction between pathways.

36
Q

What does the Src Structure reveal?

A

mechanism for autoinhibition.

37
Q

What relaxes the structure of the Kinase domain to open its substrate binding pocket?

A

binding of SH2 or SH3 domains to their ligands in another proteins or the dephosphorylation of Tyr527.

38
Q

What allows phosphorylation of Tyr 416?

A

The relaxation of the kinase domain to open its substrate binding pocket.

39
Q

What doe Tyr-PO4 of Tyr 416 form?

A

A salt bridge to Arg409.

40
Q

Why does a salt bridge form to Arg409?

A

to relax the activation loop to its unblocked conformation.

41
Q

What allows Glu 310 to form catalytically important salt bridge with Lys295?

A

The Arg409 relaxation of the activation loop to its unblocked conformation

42
Q

What is step 1 in the Src Activation?

A

Binding to phosphoprotein partner or dephosphorylation of Tyr527.

43
Q

Binding to the phosphorylation partner or dephosphorylation of Tyr527 does what?

A

opens the substrate binding cleft of Src.

44
Q

What is step 2 in the Src Activation?

A

Tyr 416 is phosphorylated to free activation loop of the active site of the enzyme.

45
Q

What do protein kinases often have?

A

inhibitory domains (loops) that occupy the active site when not phophorylated.

46
Q

In the activation of protein kinases the phosphorylation of the loop results in what?

A

in its conformation out of the active site of the enzyme allowing substrate access.

47
Q

What enzymes are equally important as kinases?

A

protein tyrosine phosphatases

48
Q

What isn’t possible without reversal of modifications?

A

regulation

49
Q

Dephosphorylation of Src where is important for what?

A

At Tyr527 for its activation.

50
Q

Active site residue form what?

A

covalent bond to phosphate hydrolyzed.

51
Q

Ser/Thr phosphotases are similar except that?

A

their substrate binding pockets are more shallow due to reduced size of the substrate.

52
Q

What is important to know about the domains N-SH2 and C-SH2 in protein tyrosine phosphatase SHP-2?

A

These domains are autoinhibitory until bound to a substrate.

53
Q

What occurs when the domain N-SH2 and C-SH2 move?

A

the inhibitory D’E loop moves out of the active site.

54
Q

What comprises 1% of the total cellular proteins?

A

Protein phosphatase PP2A.

55
Q

What are hormones?

A

Molecules secreted by specialized glands of vertebrates and plants designed to signal specific target tissues of the body.