Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases

作者：Guy S. Salvesen, DAVID L. FARLEY, Jon D. Shuman, Alan Przybyla, Christopher Reilly, James W. Travis · 发表于：Biochemistry · 年份：1987 · DOI：10.1021/bi00382a032 · 被引用次数：212 · 研究领域：Cell Adhesion Molecules Research、Protease and Inhibitor Mechanisms、Signaling Pathways in Disease

Human cathepsin G is a serine proteinase with chymotrypsin-like specificity found in both polymorphonuclear leukocytes (neutrophils) and the U937 leukemic cell line. Utilizing RNA from the latter, we have constructed a cDNA library in lambda gt11 and isolated a clone which apparently codes for the complete amino acid sequence of this enzyme. Analysis of the sequence reveals homology with rat mast cell proteinase II (47%) but a greater degree of identity (56%) with a product of activated mouse cytotoxic T lymphocytes. The close relationship between the three proteins indicates similarities in substrate specificity and in biosynthesis which we predict involves removal of a two amino acid activation peptide during or just before packaging into their respective storage granules.