Multimeric Structure of the Secreted Meprin A Metalloproteinase and Characterization of the Functional Protomer

• Published in: The Journal of biological chemistry Vol. 276; no. 25; pp. 23207 - 23211
• Main Authors: Ishmael, Faoud T., Norcum, Mona T., Benkovic, Stephen J., Bond, Judith S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.06.2001; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biopolymers; Disulfides - chemistry; Humans; meprin A; Metalloendopeptidases - chemistry; Metalloendopeptidases - genetics; Mice; Microscopy, Electron; Molecular Weight; Promoter Regions, Genetic; Protein Conformation; Recombinant Proteins - chemistry; Recombinant Proteins - genetics

Meprin A secreted from kidney and intestinal epithelial cells is capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. The secreted form of meprin A is a homo-oligomer composed of α subunits, a multidomain protease of 582 amino acids coded for near the...