BIOM20002 Lecture Notes - Lecture 43: Lingual Lipase, Brush Border, Enteropeptidase

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8 Sep 2018
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Pepsin just breaks down cellular structure to make it easier for duodenum enzymes. Exopeptidases: break off the amino acids on each end. Very inefficient because they need to be broken down one by one. Primary products are free amino acids, dipeptides and tripeptides. Pepsin is secreted in stomach by chief cells. Active at acid ph (about 2) produced in stomach by h+ secretion from parietal cells - stimulated by both gastrin and vagal activity (due to local reflexes and feed forward pathway due to cephalic release). Trypsin is secreted by pancreas as inactive protrypsin (zymogen) in response to cck released from duodenum enteroendocrine (ee) cells (due to some fat + amino acids). Chymotrypsinogen and procarboxypeptidase released from pancreas in response to cck. Amino acids cross apical membrane via na+ coupled cotransporters. In brush border membrane, more enzymes are still breaking down short peptides. Di- and tripeptides cross via h+ coupled transporters (since lumen is more acidic due to stomach acid)

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