This Article Order Full text via Infotrieve Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rao, K. N. Articles by Lombardi, B. Search for Related Content PubMed PubMed Citation Articles by Rao, K. N. Articles by Lombardi, B.

American Journal of Pathology, Vol 98, 45-59, Copyright © 1980 by American Society for Investigative Pathology

REGULAR ARTICLES

Acute hemorrhagic pancreatic necrosis in mice: the activity of lysosomal enzymes in the pancreas and the liver

KN Rao, MF Zuretti, FM Baccino and B Lombardi

The activity of lysosomal enzymes of the pancreas and the liver has been studied during induction and onset of acute hemorrhagic pancreatic necrosis with fat necrosis (AHPN) in mice. We induced AHPN by feeding the animals a choline-deficient (CD) diet containing 0.5% DL-ethionine (CDE). Control animals were fed either laboratory chow or a plain CD DIET. Increased total activities of cathespin B1, beta-galactosidase, and acid phosphatase were found to occur in pancreas homogenates of mice fed the CDE diet for 2 and 3 days. Release of cathespin B1 into pancreas cytosol was observed after 1 day of feeding. beta- galactosidase and acid phosphatase were increased in pancreas cytosol after 2 and 3 days of feeding. Changes in total activity and location of the lysosomal enzymes did not occur in the liver. Feeding the CD and CDE diets resulted in an increase in the free activity of lysosomal enzymes of both the pancreas and the liver, suggesting the existence of alterations in the lysosomal membrane. Pancreas and liver homogenates were stored on ice up to 3 hours, and the free activity of acid phosphatase and beta-galactosidase were determined at various time intervals. The free activity of both enzymes increased progressively for 3 hours in the pancreas but not in the liver. It is concluded that: 1) induction of AHPN in mice is accompanied by an increase in the activity of lysosomal enzymes of the acinar cells of the pancreas; 2) cathepsin B1 may be responsible for triggering an intraparenchymal activation of zymogens, and 3) pancreatic lysosomes are labilized more easily than liver lysosomes.

This article has been cited by other articles:

				P. Chowdhury, S. MacLeod, K. B. Udupa, and P. L. Rayford Pathophysiological Effects of Nicotine on the Pancreas: An Update Experimental Biology and Medicine, July 1, 2002; 227(7): 445 - 454. [Abstract] [Full Text] [PDF]