IAS14 Flashcards

1
Q

AA digestion in stomach

A

pepsinogen secreted by stomach chief cell
self-cleaves & activates to form pepsin under low pH (HCl), hydrolyses AA

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2
Q

AA digestion in intestine

A

pancreas secretes zymogens (trypsinogen, etc.) -> enteropeptidase cleaves trypsinogen to form trypsin -> trypsin cleaves zymogens to form functioning proteins i.e. endopeptidases, e.g. chemotrypsin, elastase, carboxypeptidase
exopeptidase secreted by enterocytes & sit on brush border for digestion of short chain AA
pH rises due to bicarbonate -> start cleaving

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3
Q

AA absorption by enterocyte

A

take in AA, dipep, tripep
Na+ dependent carrier takes in AA along with Na -> Na+ pumped out for K+ by Na+/K+ ATPase pump
peptides cleaved to form AA
basolateral membrane: only free AA carried by facilitated transporter out down conc. gradient (secondary active transport)

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4
Q

polypeptide entering blood & clinical relevance

A

pinocytosis or slipping between enterocytes
can cause allergy to protein containing food in infants

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5
Q

endogenous source of proteins

A

protein turnover i.e. protein degradation in 2 methods: ubiquitin-proteasome, autophagy

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6
Q

ubiquitin proteasome method

A

protein covalently linked to ubiquitin -> interact w/ proteasome -> degrade protein to small peptides using ATP -> ubiquitin recycled

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7
Q

autophagy of proteins

A

unwanted IC components surrounded by membranes fuse with lysosome -> cathepsin cleaves proteins into AA

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8
Q

amino acid pool

A

free AA enter or leave AA pool
+: exogenous / endogenous AA sources, AA synthesis in body w/ N & glucose supply
-: new protein synthesis, biomolecule synthesis, AA degradation into N, AA used as fuel or through GNG, transamination & carbon skeleton removed for GNG

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9
Q

transamination

A

in liver, amino group transferred from AA to alpha keto acid, original AA -> alpha keto acid
coupled w/ AA transaminase & cofactors

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10
Q

fate of protein degradation & transamination products

A

C skeletons converted to glucose or TAG
TAG packaged, secreted from liver by VLDL -> long term fuel storage
glucose stored in glycogen or released to blood
alpha keto acid enter TCAC at diff. points as energy sources when glucose unavail.
N: disposed of

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11
Q

urea disposal & carriers

A

as equal amts of ingested & excreted N every day, waste product from AA -> NH3 sources & must be disposed of
all peripheral cells have N disposal -> transfer to liver for disposal as urea using Ala & Gln (major N carriers)
muscle, intestinal, kidney cells use Ala for carrier
muscle, lung, neuron use Gln for carrier

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12
Q

NH3 toxicity

A

hyperammonemia, neurotoxic to CNS
can occur in disorders of urea cycle

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13
Q

deamination Rx e.g.

A

amino group from Gln or other not taken up by alpha keto acid -> NH4+ & AKA (incl. pyruvate) forms

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14
Q

glucose-alanine cycle

A

during exercise or fasting when muscle use blood-borne glucose
AA degradation -> pyruvate gains N from Glu -> Ala -> travels to liver -> pyruvate -> glucose via GNG -> to peripheral tissue
i.e. backbone of Ala make glucose, amino group fed to urea cycle

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15
Q

alanine -> pyruvate Rx

A

AKG -> Glu, 2 fates
1. -> transaminated to AKG, OAA forming Asp -> enter urea cycle
2. -> deaminated to AKG by directly forming NH4+

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16
Q

glutamine in N disposal

A

inter-organ amino exchange in fasting -> AA use for fuel or biosynthesis of compounds / proteins
AKG -> Glu -> Gln (by accepting 2x NH4) -> travel in blood to liver -> AKG -> NH4 released into urea cycle

17
Q

urea cycle

A

in liver hepatocytes
converts harmful NH3 into harmless urea which can be excreted, maintain N balance & get rid of toxic NH3
takes 1x NH4 from deamination of glutamate, 1x NH4 from Asp

18
Q

excess AA fate in fed state

A

energy storage in lipid & glycogen
make proteins in liver or exported to peripheral cells
biosynth. of N-containing compounds

19
Q

AA metabolism in fasting state

A

net degradation of skeletal muscle proteins -> AA used to provide energy -> N deaminated by transport by Ala & Gln