Meprin A subunit beta is a protein that in humans is encoded by the MEP1Bgene.[5][6]
Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes and in leukocytes and certain cancer cells. Mature meprins are oligomers of evolutionarily related, separately encoded alpha and/or beta subunits. Homooligomers of meprin-alpha (MEP1A; MIM 600388) are secreted; oligomers containing meprin-beta are associated with the plasma membrane. Substrates include bioactive peptides and extracellular matrix proteins. See MIM 600388 for further information on meprins.[supplied by OMIM][6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Bond JS, Rojas K, Overhauser J, Zoghbi HY, Jiang W (Jul 1995). "The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively". Genomics. 25 (1): 300–3. doi:10.1016/0888-7543(95)80142-9. PMID7774936.
Yamaguchi T, Fukase M, Sugimoto T, et al. (1995). "Purification of meprin from human kidney and its role in parathyroid hormone degradation". Biol. Chem. Hoppe-Seyler. 375 (12): 821–4. PMID7710697.
Bankus JM, Bond JS (1996). "Expression and distribution of meprin protease subunits in mouse intestine". Arch. Biochem. Biophys. 331 (1): 87–94. doi:10.1006/abbi.1996.0286. PMID8660687.
Kumar JM, Bond JS (2001). "Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning". Biochim. Biophys. Acta. 1518 (1–2): 106–14. doi:10.1016/S0167-4781(01)00188-9. PMID11267665.
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