title: Peptic ulcer: the many proteinases of aggression.
abstract: Peptic activity has long been recognized as an essential factor in the pathogenesis of peptic ulcer and related diseases, but only recently has it become clear that this activity is derived from a remarkable diversity of enzymes, all of which belong to the aspartic proteinase family of enzymes. These include two types of pepsinogens and two types of cathepsins. In recent years, considerable progress has been made in characterizing these proteinases and in applying this information to the study of a number of gastrointestinal disorders. The intent of this article is to update recent basic and clinical information on these topics and to suggest several areas that merit further investigation.
authors.affiliation: Veterans Administration Medical Center, Sepulveda, California.
authors.forename: I M
authors.initials: IM
authors.lastname: Samloff
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002403:Cathepsins / Q000378:metabolism; D004381:Duodenal Ulcer / Q000201:enzymology* / Q000235:genetics; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D010435:Pepsinogens / Q000378:metabolism; D011110:Polymorphism, Genetic; D013276:Stomach Ulcer / Q000201:enzymology* / Q000235:genetics
chemical_list: D010435:Pepsinogens; D002403:Cathepsins; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases