L1 : amino acid metabolism Flashcards

1
Q

what is kwashiorkor?

A

a severe form of protein malnutrition

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2
Q

what is kwashiorkor caused by?

A

insufficient protein consumption

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3
Q

what happens as a result of insufficient protein consumption?

A

osmotic imbalance in the GI system which leads to gut swelling

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4
Q

what is gut swelling also known as?

A

edema or water retention

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5
Q

gut swelling decreases the body’s ability to produce:

A
  1. new intestinal epithelial cells

2. digestive enzymes

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6
Q

what is the aim of digesting dietary proteins?

A

hydrolyzing proteins into di- and tri- peptides and free amino acids

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7
Q

where does the digestion of proteins begin?

A

the stomach

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8
Q

where does the digestion of proteins end?

A

the small intestine

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9
Q

where are proteolytic enzymes produced?

A
  1. stomach
  2. small intestine
  3. pancreas
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10
Q

what is secreted by parietal cells?

A

HCl

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11
Q

what does HCl do?

A

denatures proteins and kills some bacteria because its too dilute to hydrolyze the proteins

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12
Q

what is secreted by chief cells?

A

pepsin; as an inactive zymogen (pepsinogen)

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13
Q

what is pepsin?

A

an endopeptidase

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14
Q

how is pepsinogen activated to pepsin?

A
  1. low pH of HCl

2. autocatalytic activation by other pepsin molecules

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15
Q

what is the type of mechanism in which autocatalytic activation runs?

A

positive feedback mechanism

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16
Q

what is the function of pepsin?

A

release peptides and a few amino acids

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17
Q

what is the release of zymogens in the pancreas mediated by?

A

two hormones; cholecystokinin and secretin

18
Q

how are zymogens activated in the pancreas?

A

a duodenal enteropeptidase converts trypsinogen to trypsin

19
Q

how are all pancreatic zymogens activated?

A

by trypsin

20
Q

what is the specificity of trypsin?

A

cleaving only after arginine and lysine

21
Q

how is digestion done in the small intestine?

A

by aminopeptidases

22
Q

what is the classification of aminopeptidases?

A

exopeptidase

23
Q

where are aminopeptidases found?

A

the luminal surface of the intestine

24
Q

what do aminopeptidases do?

A

repeatedly cleaves the N-terminal residue from oligopeptides

25
when oligopeptides are cleaved what do they form?
smaller peptides and free amino acids
26
how are free amino acids absorbed?
intestinal enterocytes by Na+ linked secondary transport system
27
how are the di and tri peptides absorbed?
H+ linked transport system
28
how does the Na+ leave the cell?
Na/K pump
29
how are free amino acids RELEASED?
facilitated transporters; to be metabolized by the liver
30
how many transporters have overlapping specificity?
at least 7
31
what do the small intestine and proximal tubule of the kidney share?
common transport systems for AA uptake
32
which amino acid do the small intestine and proximal tubule of the kidney have an affinity to, and what disease may it lead to?
cystine; cystinuria
33
what is cystinuria?
its an inborn error of metabolism characterized by a genetic defect in the transport system which leads to an accumulation in the amino acids
34
what is the role of HCl in digestion?
denatures proteins
35
what initiates protein digestion in the stomach?
pepsin
36
which hormone stimulates the release of pancreatic zymogens?
cholecystokinin
37
which cells produce pepsin?
chief cells
38
where does the enzymatic digestion of proteins start?
stomach
39
what is a characteristic of pepsin?
autocatalytic
40
what is a characteristic of trypsin?
synthesized as a zymogen (trypsinogen)
41
what secretes gastric HCl?
parietal cells
42
how is pepsinogen activated?
positive feedback