tailieunhanh - Báo cáo khoa học: Human anionic trypsinogen Properties of autocatalytic activation and degradation and implications in pancreatic diseases

Humanpancreatic secretions contain twomajor trypsinogen isoforms, cationic and anionic trypsinogen, normally at a ratio of 2 : 1. Pancreatitis, pancreatic cancer and chronic alcoholism lead to a characteristic reversal of the isoform ratio, and anionic trypsinogen becomes the predominant zymogen secreted. To understand the biochemical conse-quences of these alterations, we recombinantly expressed and purified both human trypsinogens and documented characteristics of autoactivation, autocatalytic degradation and Ca 2+ -dependence | Eur. J. Biochem. 270 2047-2058 2003 FEBS 2003 doi Human anionic trypsinogen Properties of autocatalytic activation and degradation and implications in pancreatic diseases Zoltán Kukor Miklos Tilth and Miklos Sahin-Toth Department of Molecular and Cell Biology Goldman School of Dental Medicine Boston University Boston USA Human pancreatic secretions contain two major trypsinogen isoforms cationic and anionic trypsinogen normally at a ratio of 2 1. Pancreatitis pancreatic cancer and chronic alcoholism lead to a characteristic reversal of the isoform ratio and anionic trypsinogen becomes the predominant zymogen secreted. To understand the biochemical consequences of these alterations we recombinantly expressed and purified both human trypsinogens and documented characteristics of autoactivation autocatalytic degradation and Ca2 -dependence. Even though the two trypsinogens are w 90 identical in their primary structure we found that human anionic trypsinogen and trypsin exhibited a significantly increased 10-20-fold propensity for autocatalytic degradation relative to cationic trypsinogen and trypsin. Furthermore in contrast to the characteristic stimulation of the cationic proenzyme acidic pH inhibited autoactivation of anionic trypsinogen. In mixtures of cationic and anionic trypsinogen an increase in the proportion of the anionic proenzyme had no significant effect on the levels of trypsin generated by autoactivation or by enterokinase at pH in 1 mM Ca2 - conditions that were characteristic of the pancreatic juice. In contrast rates of trypsinogen activation were markedly reduced with increasing ratios of anionic trypsinogen under conditions that were typical of potential sites of pathological intra-acinar trypsinogen activation. Thus at low Ca2 concentrations at pH selective degradation of anionic trypsinogen and trypsin caused diminished trypsin production while at pH inhibition of anionic trypsinogen activation .

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