Mast cells are connective tissue cells derived from blood-forming tissues that line arterial walls and secrete substances, which mediate inflammatory and immune responses. Mast cell chymase, known as CMA1, is a major secreted serine protease that is involved in vasoactive peptide generation, extracellular matrix degradation and regulation of gland secretion. The human chymase gene, which maps to human chromosome 14q11.2, encodes a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide and a 226-amino acid catalytic domain. Tryptases comprise a family of trypsin-like serine proteases that are enzymatically active as heparin-stabilized tetramers. There are four functional genes for tryptase: α I, β I, β II and γ I, which map to human chromosome 16p13.3, with β tryptases representing the main isoenzymes expressed in mast cells. Mast cell proteases are a family of rodent protein homologs to human tryptases that are specifically expressed in mast cells and may serve as highly specific markers in the analysis of mast cell heterogeneity, differentiation and function.
