Functional, chemical, and clinical aspects of proteolytic enzymes in the alimentary canal.
Knowledge of the structure and catalytic function of the pancreatic proteases has increased rapidly in recent years. These advances have been less spectacular in the case of pepsin, and information concerning mucosal enzymes of the small intestine and colon has not even reached the point where one can be certain of their number, far less their nature. The role of these enzymes in disease processes is probably not significant so far as the alimentary tract is concerned, and it is not even certain that the pancreatic proteases influence the course of acute pancreatitis -- they are of more interest to the clinician as diagnostic aids. Since undesirable consequences result from their deficient output, future research should be directed towards improving replacement therapy.
D002403:Cathepsins / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism; D003106:Colon / Q000201:enzymology*; D005243:Feces / Q000201:enzymology; D006801:Humans; D007421:Intestine, Small / Q000201:enzymology*; D010179:Pancreas / Q000201:enzymology*; D010434:Pepsin A / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D012007:Rectum / Q000201:enzymology*; D013270:Stomach / Q000201:enzymology*; D014357:Trypsin / Q000378:metabolism
D002403:Cathepsins; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin; D010434:Pepsin A