Molecular Cloning and Characterization of Mouse Mast Cell Chymases
Document Type
Article
Publication Date
5-22-1992
Description
Mouse mast cell chymases are granule-associated serine proteinases with chymotrypsin-like substrate specificities. cDNAs for two new chymases were isolated from a cDNA library constructec using mRNA from ABFTL-6 mouse mast cells by screening with a rat mast cell proteinase cDNA. The deduced amino acid sequence of mouse cymase 1 consists fo a 226 amino acid catalytic portion and a 21 amino acid preprosequence. Chymase 1 is unusual in that an Asn occurs in the substrate binding pocket, a feature that has not been observed in any other serine proteinase. Also, chymase 1 is expected to have a large positive charge (+13) at physiological pH. A partial cDNA for chymase 2 encodes 177 residues of the carboxy terminal portion of a second proteinase distinct from chymase 1. Chymase 2 cDNA contains highly conserved intron/exon junction, a high positive charge (+17) and a novel, second potential N-glycosylation site. Transcripts for both chymases are found in ABFTL-6 mast cells, but only chymase 2 mRNA is in mouse connective tissue mast cells. These data suggest that these chymases have distinct enzymatic properties and tissue-specific patterns of gene expression.
Citation Information
Chu, Wei; Johnson, David A.; and Musich, Phillip R.. 1992. Molecular Cloning and Characterization of Mouse Mast Cell Chymases. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. Vol.1121(1-2). 83-87. https://doi.org/10.1016/0167-4838(92)90340-J PMID: 1376147 ISSN: 0167-4838