Digestion Lecture Flashcards

1
Q

Cell types in the small intestine

enterocytes

A

respon. for digestion, absorption, secretion

turnover rate 3-6 days

susceptible to irradiation and chemotherapy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Cell types in the small intestine

goblet cells

A

mucous secreting

produce physical, chemical and immunological barrier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Cell types in the small intestine

patneth cells

A

part of defense, secrete agents that destroy bacteria

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

forms of enterocyte membrane control

A

pinocytosis (at base of microvilli)
passive diffusion
active diffusion
facilitated diffusion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

transporters on the apical membrane of the enterocyte designed for taking in monosaccharides via _____transport

A

SGLT 1 is a Glucose-Na cotransporter, Galactose-Na cotransporter; uses secondary transport (duh)

GLUT2 is a fructose transporter

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

transporters on the basolateral membrane of the enterocyte designed for taking in monosaccharides via _____transport

A

Glut2, it takes in everything (glucose, galactose, fructose)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

where is lactase located

A

on the brush boarder. deficiency causes osmotic diarrhea

undigested lactose is fermented into methane and hydrogen gas, causing excess flatulence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Stomach: protein digesting enzymes

“endopeptidases”

A

pepsin, typsin, chymotrypsin, elastase

“endopeptidases”

degrade peptides from interior peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Stomach: protein digesting enzymes

“exopeptidases”

A

carboxypeptidase A
carboxypeptidase B

degrade peptides beginning at C terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Trypsinogen

A

converted to trypsin by ENTEROpeptidase

trypsin converts the ENDOpeptidases into their active form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are the inactive/active form of the endopeptidases?

A

trypsinogen—> trypsin
chymotrypsinogen –> chymotrypsin
Proelastase —> elastase
Pro-carboxypeptidase A and B –> A and B carboxypeptidase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

where are proteases actives?

A

in the stomach AND the SI

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

autocatalysis

A

trypsin’s conversion of trypsinogen into trypsin

pancreatic enzymes digest one another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Protein in the stomach is digested to ___ by ____

A

amino acids and oligopeptides by pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

protein in the small intestines is digested to ______ by ______

A

amino acids, dipeptides, tripeptides, oligopeptides

oligopeptides are further degraded by peptidase on the brush border to amino acids, dipeptides and tripeptides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Amino acid transporters in the small intestine in the apical membrane

A

secondary a.a.-Na cotransporter

there are four: one for acidic a.a., neutral a.a., imino a.a.s, basic a.a’s

dipeptides/tripeptides have an H-Di/Tri cotransporter as well

17
Q

Amino acid transporters in the small intestine in the basolateral surface

A

four transporters for each group of amino acids using facilitated diffusion

internally there’s a peptidase to degrade dipeptides and tripeptides to a.a.s

dipeptides and tripeptides can diffuse out of the cell

18
Q

pancreatic preteases

A

trypsin, chymotrypsin, elastase, caeboxypeptidase A and carboxypeptidase B

19
Q

after degrading proteins, what happens to pancreatic enzymes?

A

they degrade one another and are reabsorbed

20
Q

cystinuria

A

defect or absence of Na-amino acid cotransporters

transporter for di-basic amino acids (cystine, lysine, arginine, and ornithine) are absent from small intestine and kidney

genetic disorder

amino acids are secreted into feces

21
Q

Hartnup Disease

A

Cannot absorb neutral amino acids e.g. tryptophan

recessive genetic disorder

symptoms resemble those cause by pellagra
deficiency of niacin)

symptoms: diarrhea, mood changes, neurologic problems, 
res scaly skin
photosensitivity 
short stature 
uncoordinated movements 

urine has high concentration of neutral amino acids

22
Q

Cystic fibrosis transporter mutations

A

associated with deficiency of amino acid transporters
CFTR transporter in the apical region of duct cells in pancreas

CFTR secretes chlorine, which moves back into the cell down a gradient, and pushing HCO3 into the duct lumen

CFTR mutations decrease bicarbonate secretion

pH elevation prevents activated trypsin from catalyzing the trypsinogen to trypsin conversion

ability to flush active enzymes from the duct may be lost

result– acute or recurrent peancreatits

23
Q

Where are lipids digested?

A

in the stomach and small intestine

24
Q

Triglycerides are digested via 3 enzymes

A

lingual lipase, gastric and prancreatic lipase

25
Q

cholesterol esters are degrade by one important enzyme

A

cholesterol esterase hydrolase

26
Q

phospholipids are degraded by

A

phospholipase A2

phospholipid —> lysolecithin-FA

27
Q

what must occur initially for lipid digestion

A

solubilized, formed into micelles by bile and transported to the apical region of the enterocytes

28
Q

pancreatic lipase

A

cholesterol ester hydrolase, phospholipase A2, and pancreatic lipase