Carboxypeptidase A3 (CPA3)

Carboxypeptidase A3 (CPA3) is a mast cell-specific zinc-dependent metalloprotease stored in secretory granules and released during mast cell activation[1][2][3]. It plays major roles in proteolytic degradation of proteins and peptides in the extracellular matrix and participates in inactivation of toxins or pathogenic peptides, including snake venom and endothelin-1[1][2]. CPA3 is essential for mast cell biology, including maturation and function, and is involved in regulating innate immune responses, tissue remodeling, and angiogenesis[1][2][3]. Expression of CPA3 increases in conditions such as asthma and chronic inflammation, making it a valuable biomarker for mast cell activity and inflammation[2][3]. Genetic models show that CPA3 is necessary for proper mast cell maturation, and its deficiency impairs mast cell function[2]. There is no evidence of known drugs directly targeting CPA3 currently in clinical use, but its central role in inflammatory and immune processes makes it a candidate for future therapeutic modulation[1][2][3].

Other names

Mast cell carboxypeptidase AMC-CPAtissue carboxypeptidase ACBPA3_HUMAN

Proteolytic cleavage of target peptides or proteins, including bioactive peptides such as endothelin-1, neurotensin, kinetensin, neuromedin N, angiotensin I, and venom factors[1][2].