# MEP1B

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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Meprin A subunit beta''' is a [protein](/source/protein) that in humans is encoded by the ''MEP1B'' [gene](/source/gene).<ref name="pmid7774936">{{cite journal |vauthors=Bond JS, Rojas K, Overhauser J, Zoghbi HY, Jiang W | title = The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively | journal = Genomics | volume = 25 | issue = 1 | pages = 300–3 |date=Jul 1995 | pmid = 7774936 | doi =10.1016/0888-7543(95)80142-9  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MEP1B meprin A, beta| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4225}}</ref>

Meprins are multidomain zinc metalloproteases that are highly expressed in [mammalian kidney](/source/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]<ref name="entrez">{{cite web | title = Entrez Gene: MEP1B meprin A, beta| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4225}}</ref>

==References==
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==Further reading==
{{refbegin | 2}}
*{{cite journal   |vauthors=Yamaguchi T, Fukase M, Sugimoto T, etal |title=Purification of meprin from human kidney and its role in parathyroid hormone degradation. |journal=Biol. Chem. Hoppe-Seyler |volume=375 |issue= 12 |pages= 821–4 |year= 1995 |pmid= 7710697 }}
*{{cite journal  |vauthors=Kaushal GP, Walker PD, Shah SV |title=An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin. |journal=J. Cell Biol. |volume=126 |issue= 5 |pages= 1319–27 |year= 1994 |pmid= 8063866 |doi=10.1083/jcb.126.5.1319  | pmc=2120165  }}
*{{cite journal   |vauthors=Dumermuth E, Eldering JA, Grünberg J, etal |title=Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells. |journal=FEBS Lett. |volume=335 |issue= 3 |pages= 367–75 |year= 1994 |pmid= 8262185 |doi=10.1016/0014-5793(93)80421-P  |s2cid=32599035 |doi-access=free }}
*{{cite journal  |vauthors=Bankus JM, Bond JS |title=Expression and distribution of meprin protease subunits in mouse intestine. |journal=Arch. Biochem. Biophys. |volume=331 |issue= 1 |pages= 87–94 |year= 1996 |pmid= 8660687 |doi= 10.1006/abbi.1996.0286 }}
*{{cite journal  |vauthors=Chevallier S, Ahn J, Boileau G, Crine P |title=Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin. |journal=Biochem. J. |volume=317 |issue=  3|pages= 731–8 |year= 1996 |pmid= 8760356 |doi=  10.1042/bj3170731| pmc=1217546  }}
*{{cite journal  |vauthors=Chestukhin A, Muradov K, Litovchick L, Shaltiel S |title=The cleavage of protein kinase A by the kinase-splitting membranal proteinase is reproduced by meprin beta. |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 30272–80 |year= 1997 |pmid= 8939981 |doi=10.1074/jbc.271.47.30272  |doi-access=free }}
*{{cite journal   |vauthors=Eldering JA, Grünberg J, Hahn D, etal |title=Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells. |journal=Eur. J. Biochem. |volume=247 |issue= 3 |pages= 920–32 |year= 1997 |pmid= 9288916 |doi=10.1111/j.1432-1033.1997.00920.x  |doi-access=free }}
*{{cite journal   |vauthors=Lottaz D, Hahn D, Müller S, etal |title=Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits. |journal=Eur. J. Biochem. |volume=259 |issue= 1–2 |pages= 496–504 |year= 1999 |pmid= 9914532 |doi=10.1046/j.1432-1327.1999.00071.x  |doi-access=free }}
*{{cite journal  |vauthors=Kumar JM, Bond JS |title=Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning. |journal=Biochim. Biophys. Acta |volume=1518 |issue= 1–2 |pages= 106–14 |year= 2001 |pmid= 11267665 |doi=  10.1016/S0167-4781(01)00188-9}}
*{{cite journal   |vauthors=Bertenshaw GP, Turk BE, Hubbard SJ, etal |title=Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13248–55 |year= 2001 |pmid= 11278902 |doi= 10.1074/jbc.M011414200 |doi-access= free }}
*{{cite journal  |vauthors=Litovchick L, Friedmann E, Shaltiel S |title=A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34413–23 |year= 2002 |pmid= 12093806 |doi= 10.1074/jbc.M203986200 |doi-access= free }}
*{{cite journal   |vauthors=Leuenberger B, Hahn D, Pischitzis A, etal |title=Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion. |journal=Biochem. J. |volume=369 |issue= Pt 3 |pages= 659–65 |year= 2003 |pmid= 12387727 |doi= 10.1042/BJ20021398  | pmc=1223113 }}
*{{cite journal  |vauthors=Bertenshaw GP, Norcum MT, Bond JS |title=Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2522–32 |year= 2003 |pmid= 12399461 |doi= 10.1074/jbc.M208808200 |doi-access= free }}
*{{cite journal   |vauthors=Norman LP, Jiang W, Han X, etal |title=Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. |journal=Mol. Cell. Biol. |volume=23 |issue= 4 |pages= 1221–30 |year= 2003 |pmid= 12556482 |doi=10.1128/MCB.23.4.1221-1230.2003  | pmc=141138  }}
*{{cite journal   |vauthors=Hahn D, Pischitzis A, Roesmann S, etal |title=Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 42829–39 |year= 2003 |pmid= 12941954 |doi= 10.1074/jbc.M211169200 |doi-access= free }}
*{{cite journal  |vauthors=Herzog C, Kaushal GP, Haun RS |title=Generation of biologically active interleukin-1beta by meprin B. |journal=Cytokine |volume=31 |issue= 5 |pages= 394–403 |year= 2005 |pmid= 16095909 |doi= 10.1016/j.cyto.2005.06.012 }}
*{{cite journal   |vauthors=Becker-Pauly C, Höwel M, Walker T, etal |title=The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. |journal=J. Invest. Dermatol. |volume=127 |issue= 5 |pages= 1115–25 |year= 2007 |pmid= 17195012 |doi= 10.1038/sj.jid.5700675 |doi-access= free }}
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{{gene-18-stub}}

Category:Genes on human chromosome 18

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Adapted from the Wikipedia article [MEP1B](https://en.wikipedia.org/wiki/MEP1B) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MEP1B?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.
