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Topics to be covered
Digestion of proteins and enzymes
involved
Uptake of amino acids by cells
The -glutamyl cycle
Lecture objectives
To elucidate the enzymatic digestion of
dietary proteins
To describe the different enzymes involved
in the digestion of proteins
To analyze the way amino acids are taken
up by cells
To comprehend the -glutamyl cycle
Digestion of Proteins
Entry of dietary protein into the stomach
stimulates the gastric mucosa to secrete the
hormone gastrin.
Gastrin stimulates the secretion of HCl by the
parietal cells and pepsinogen by the chief cells
of the gastric glands.
HCl has antiseptic property and denatures
proteins rendering internal parts accessible for
enzymatic hydrolysis.
Digestion of Proteins
Pepsinogen, an inactive precursor, or zymogen, is
converted to active pepsin by the enzymatic action of
pepsin itself.
In the stomach, pepsin hydrolyzes proteins at peptide
bonds on the amino-terminal side of the aromatic
amino acid residues (Phe, Trp, Tyr).
When stomach contents pass into the small intestine,
the low pH triggers secretion of the hormone secretin
into the blood.
Secretin stimulates the pancreas to secrete
bicarbonate into the small intestine to neutralize the
gastric HCl, abruptly increasing the pH to about 7.
Digestion of Proteins
Digestion of proteins now continues in the small
intestine through secretion of cholecystokinin,
which stimulates secretion of many peptidases.
These include Trypsinogen, Chemotrypsinogen,
and Procarboxypeptidase A and B (inactive forms)
Trypsinogen changed to trypsin by
enteropeptidase and trypsin further activates
itself and the other inactive precursors.
Synthesis of the enzymes as inactive forms
protects the exocrine cells from destructive
proteolytic attack (self digestion).
Digestion of Proteins
The pancreas further protects itself against selfdigestion by making a specific inhibitor, a
protein called pancreatic trypsin inhibitor.
Pepsin, trypsin, and chymotrypsin have
different amino acid specificities.
Trypsin cleaves peptide bonds from the
carboxyl termini of basic amino acids (Lys,Arg)
Chemotrypsin cleaves peptide bonds from the
carboxyl ends of aromatic amino acids.
Gastric glands
stomach
Parietal cells
Chief cells
pancreas
Low pH
Pepsinogen
Pancreatic duct
pepsin
pH 7
Small intestine
Exocrine cells
Of pancreas
Rough ER
Zymogen
granules
Villi of small
intestine
Digestion of Proteins
Degradation of the short peptides in the small
intestine is then completed by other entestinal
peptidases.
Carboxypeptidases A and B (both of which are
zinc-containing enzymes), remove successive
carboxyl-terminal residues from peptides, and
an aminopeptidase that hydrolyzes
successive amino-terminal residues from short
peptides.
The resulting mixture of free amino acids is
transported into the epithelial cells lining the
small intestine.