Studies on the activation of canine trypsinogens in vitro.
The activation of canine anionic and cationic trypsinogen by enterokinase, trypsin, thrombin, plasmin and extracts from canine granulocytes were studied in vitro. Enterokinase activates both trypsinogens about 1000 times faster than trypsin. The enterokinase-catalyzed activation is not inhibited by the main serum protease inhibitors, alpha-macroglobulin and alpha 1-antitrypsin. alpha-Macroglobulin cannot inhibit the activation of the trypsinogens by trypsin but this reaction is completely inhibited by alpha 1-antitrypsin. The results are discussed in relation to the pathogenesis of acute pancreatitis.
D000818:Animals; D004285:Dogs; D004765:Enteropeptidase / Q000494:pharmacology; D005341:Fibrinolysin / Q000494:pharmacology; D006098:Granulocytes / Q000378:metabolism; D066298:In Vitro Techniques; D014357:Trypsin / Q000494:pharmacology; D014362:Trypsinogen / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000515:alpha 1-Antitrypsin / Q000494:pharmacology; D000511:alpha-Macroglobulins / Q000494:pharmacology
D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins; D014362:Trypsinogen; D014357:Trypsin; D005341:Fibrinolysin; D004765:Enteropeptidase