Lecture 2 - Insulin and Friends Flashcards

(33 cards)

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

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
what is the problem with insulin in type 1 diabetics and what is the cause of this
no functional insulin, autoimmune disease or variant insulin
25
what is the problem with insulin in type 2 diabetics and what is the cause of this
reduced receptor sensitivity, obesity or rare genetic receptor variants (receptor not responding to insulin)
26
what does the uptake of glucose stimulate
oxidative metabolism and ATP production
27
increased metabolic activity stimulates the conversion of what and the release of insulin
conversion of proinsulin and release of insulin
28
what is the function of GLUT4 and where is it found
insulin-dependent glucose uptake, found in striated muscle and adipose tissue
29
what is the broad process called that GLUT4 does
endo and exocytosis
30
what is the function of GLUT2 and where is it found
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
what is endocytosis
internalising molecules, particles, or fluids from the external environment by engulfing them into membrane-bound vesicles
32
what is exocytosis
cells release molecules, particles, or fluids from internal vesicles into the extracellular environment