Physiological factors controlling release of enterokinase from rat enterocytes

The quantitative release of enterokinase from isolated rat enterocytes following treatment with taurocholate-taurodeoxycholate, papain, chymotrypsin, elastase, carbamylcholine, and cholecystokinin-octapeptide was examined. Alkaline phosphatase and lactate dehydrogenase activities were evaluated simultaneously to check for specificity. Bile salts promoted a concentration-dependent release of all enzymes. Concomitantly, bile salts also led to cell destruction in proportion to the amount of enzymes released. Proteases caused the release of enterokinase and alkaline phosphatase with no concomitant increase of lactate dehydrogenase or cell lysis. At equal concentrations, papain released more enzymes than chymotrypsin and elastase. Chymotrypsin and elastase, however, led to higher ratios of enterokinase to alkaline phosphatase found in the media and suggested a selective release of enterokinase (EK) over that of alkaline phosphatase. Bile salts and pancreatic proteases together seem to have an additive effect of the release of EK. Carbamylcholine and cholecystokinin-octapeptide had no effect on enzyme release. These results suggested that pancreatic proteases are involved in the release of enterokinase by a selective action. Bile salts may also play a role through a nonselective detergent effect.