Identification and molecular cloning of a novel mouse mucosal mast cell serine protease.

A novel 28,000 Mr serine protease, designated mouse mast cell protease-2 (MMCP-2), that is stored in the secretory granules of Kirsten sarcoma virus-immortalized mouse mast cells (KiSV-MC) has been identified and its NH2-terminal amino acid sequence has been determined. Analysis of a 953-base pair cDNA that encodes MMCP-2 revealed that this serine protease is a basically charged protein, possessing the histidine-aspartic acid-serine charge relay system that is characteristic of other serine proteases. DNA blot analysis using the full-length MMCP-2 cDNA indicated the existence of a family of highly related serine protease genes in the mouse genome. When the same DNA blot was probed with the 149-base pair KpnI----3' fragment of the cDNA, the probe hybridized to a single DNA fragment, thereby demonstrating that this 3' fragment could be used as a gene-specific probe. The presence of high levels of the MMCP-2 mRNA transcript in the intestines of nematode-infected mice, and its absence in mouse bone marrow-derived mast cells and peritoneal cavity-derived connective tissue mast cells, suggest that this member of the mouse mast cell protease family is preferentially expressed late in the differentiation of mucosal mast cells.