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Pancreatology. 2001;1(5):461-5.

The pathobiochemistry of hereditary pancreatitis: studies on recombinant human cationic trypsinogen.

Author information

1
Department of Physiology, University of California Los Angeles, Calif., USA. miklos@hhmi.ucla.edu

Abstract

BACKGROUND/AIMS:

This study attempts to identify the biochemical alterations in human cationic trypsinogen and trypsin caused by the hereditary pancreatitis-associated mutations Arg117-->His and Asn21-->Ile.

METHODS:

Recombinant wild-type and mutant human cationic trypsinogens were expressed in Escherichia coli and purified to homogeneity, and trypsin autolysis and trypsinogen autoactivation were characterized.

RESULTS:

Both mutations significantly enhanced the autoactivation of human cationic trypsinogen. In addition, the Arg117-->His mutation inhibited autocatalytic inactivation of trypsin, while the Asn21-->Ile mutation had no such effect.

CONCLUSIONS:

The findings support the notion that enhanced trypsinogen activation in the pancreas is the common initiating step in hereditary pancreatitis, whereas trypsin stabilization plays a role in cases associated with the Arg117-->His mutation.

PMID:
12120225
DOI:
10.1159/000055848
[Indexed for MEDLINE]
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