Genes, cloned cDNAs, and proteins of human trypsinogens and pancreatitis-associated cationic trypsinogen mutations

Abstract

Historically, trypsinogens/trypsins have been one of the most extensively studied enzyme models of protein structure and function. They have received renewed attention after the identification of mutations in the cationic trypsinogen gene as being associated with hereditary pancreatitis. A survey of the literature revealed five cloned cDNAs, but only three protein products of human trypsinogens, and their nomenclature has been confusing. The availability of the complete genomic sequencing of the human trypsinogen gene family made it possible to provide a systematic review of the genes, cDNAs, and protein products of human trypsinogens and to clarify some controversial issues. Further, the confusing coexistence of two systems for naming the cationic trypsinogen mutations is addressed.