Meprin A subunit alpha (MEP1A)

Meprin A subunit alpha (MEP1A) is a zinc-dependent metalloprotease that is mainly expressed in the brush border of proximal tubule epithelial cells in the kidney and in enterocytes of the intestine and colon. It is secreted into the extracellular space, where it forms large oligomeric enzyme assemblies that participate in proteolytic processing of pro-collagens, growth factors, cytokines, and components of the extracellular matrix. MEP1A is important for extracellular matrix remodeling, immunity, inflammation, and epithelial homeostasis. Dysregulation of MEP1A is associated with several diseases including acute kidney injury, colorectal cancer, sepsis, and inflammatory bowel disease. It is a target for drug discovery due to its pathological roles and has been explored as a biomarker, especially in cancers. MEP1A enzyme activity can be blocked by selective small molecule inhibitors and endogenous regulatory proteins, such as fetuin-B.

Other names

Meprin A subunit alphaMEP1APPHAEndopeptidase-2N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alphaPABA peptide hydrolasePPH alphabA268F1.1meprin A alpha (PABA peptide hydrolase)meprin A, alpha (PABA peptide hydrolase)

Inhibition of metalloprotease activity; small molecule inhibitors and endogenous proteins (e.g., fetuin-B) bind and block enzyme function