Lecture 2 - Insulin and Friends Flashcards

1
Q

what can goldfish convert lactate into

A

ethanol

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1
Q

insulin is synthesised as a pre-pro-peptide, what is this

A

small protein

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2
Q

what is the pre sequence in insulin responsible for

A

the export from the cytosol of the cell
- in this case to secretory granules

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3
Q

what does the pro-sequence of insulin seem to be important for (and what happens to it)

A

proper folding of insulin and it is removed

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4
Q

what bonds and structure interactions does insulin have

A

disulfide bonds (C-C) as well as secondary and tertiary structure interactions (covalent linkages)

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5
Q

where is insulin made

A

made in the islets of Langerhans in the pancreas (B cells)

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6
Q

what do alpha cells in the pancreas produce

A

glucagon

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7
Q

what are two of the endocrine hormones produced in the pancreas

A

insulin and glucagon

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8
Q

insulin typically forms hexamers with what in B cells and what does this mean

A

Zn = causes insulin to be packed very tightly together and held into hexamers

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9
Q

insulin forms what in the blood

A

monomers in blood

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10
Q

circulating insulin interacts with what

A

receptors on some tissues (fat, muscle and liver etc)

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11
Q

the insulin receptor is synthesised as one protein and then what happens for its full function form (what does it form)

A

it is cleaved (modified) for full function (forms a dimer)

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12
Q

what gives rise to different insulin receptor isoforms

A

splicing variants during mRNA processing

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13
Q

how many splices is the insulin receptor split into

A

3

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14
Q

where does the largest splice (A chain) of the insulin receptor sit

A

sits outside the cell and folds

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15
Q

where does the B chain of the insulin receptor sit

A

the first part of B chain is in the membrane, other part is inside the cell

16
Q

insulin is a what on the surface of the cell

A

dimer

17
Q

what are the three domains of the insulin receptor

A
  • extracellular domain
  • transcellular domain
  • cytosolic domain
18
Q

what will activate the insulin receptor

A

insulin binding

19
Q

when there is no ligand (insulin) present at the receptor what does the receptor do

A

remains inactive

20
Q

what does binding of insulin cause to the receptor

A

structural changes and activates the receptor

21
Q

specifically what part of the receptor is changes when insulin binds

A

tyrosine kinase domain

22
Q

in a normal body insulin is released from where and in response to what

A

insulin is released from B cells in response to blood glucose

23
Q

in a normal body when the insulin receptor is stimulated what happens

A

receptor is stimulated, GLUT4 moves to the cell surface to transport glucose

glucose is taken up by the cell

24
Q

what is the problem with insulin in type 1 diabetics and what is the cause of this

A

no functional insulin, autoimmune disease or variant insulin

25
Q

what is the problem with insulin in type 2 diabetics and what is the cause of this

A

reduced receptor sensitivity, obesity or rare genetic receptor variants

(receptor not responding to insulin)

26
Q

what does the uptake of glucose stimulate

A

oxidative metabolism and ATP production

27
Q

increased metabolic activity stimulates the conversion of what and the release of insulin

A

conversion of proinsulin and release of insulin

28
Q

what is the function of GLUT4 and where is it found

A

insulin-dependent glucose uptake, found in striated muscle and adipose tissue

29
Q

what is the broad process called that GLUT4 does

A

endo and exocytosis

30
Q

what is the function of GLUT2 and where is it found

A

largely responsible for insulin-independent uptake of glucose (it happens on its own)

found in kidney, liver, pancreatic B cells, basolateral membrane of small intestine

31
Q

what is endocytosis

A

internalising molecules, particles, or fluids from the external environment by engulfing them into membrane-bound vesicles

32
Q

what is exocytosis

A

cells release molecules, particles, or fluids from internal vesicles into the extracellular environment