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{{Infobox_gene}}
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'''Meprin A subunit beta''' is a [[protein]] that in humans is encoded by the ''MEP1B'' [[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 | pmc =  | 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/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4225| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Meprin A, beta
| HGNCid = 7020
| Symbol = MEP1B
| AltSymbols =;
| OMIM = 600389
| ECnumber = 
| Homologene = 48382
| MGIid = 96964
| GeneAtlas_image1 = PBB_GE_MEP1B_207251_at_tn.png
| Function = {{GNF_GO|id=GO:0004238 |text = meprin A activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008533 |text = astacin activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007586 |text = digestion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4225
    | Hs_Ensembl = ENSG00000141434
    | Hs_RefseqProtein = NP_005916
    | Hs_RefseqmRNA = NM_005925
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 28023985
    | Hs_GenLoc_end = 28054362
    | Hs_Uniprot = Q16820
    | Mm_EntrezGene = 17288
    | Mm_Ensembl = ENSMUSG00000024313
    | Mm_RefseqmRNA = NM_008586
    | Mm_RefseqProtein = NP_032612
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 21215384
    | Mm_GenLoc_end = 21240502
    | Mm_Uniprot = Q059K0
  }}
}}
'''Meprin A, beta''', also known as '''MEP1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MEP1B meprin A, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4225| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: MEP1B meprin A, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4225| accessdate = }}</ref>
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: MEP1B meprin A, beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4225| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Yamaguchi T, Fukase M, Sugimoto T, ''et al.'' |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 |doi=  }}
*{{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 |doi=  }}
*{{cite journal  | author=Bond JS, Rojas K, Overhauser J, ''et al.'' |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 |year= 1995 |pmid= 7774936 |doi=  }}
*{{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  | author=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=  }}
*{{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 }}
*{{cite journal | author=Dumermuth E, Eldering JA, Grünberg J, ''et al.'' |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=  }}
*{{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  | author=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= | pmc=1217546 }}
*{{cite journal  | author=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 ( Pt 3) |issue=  |pages= 731-8 |year= 1996 |pmid= 8760356 |doi=  }}
*{{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 }}
*{{cite journal  | author=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=  }}
*{{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 }}
*{{cite journal | author=Eldering JA, Grünberg J, Hahn D, ''et al.'' |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=  }}
*{{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 }}
*{{cite journal | author=Lottaz D, Hahn D, Müller S, ''et al.'' |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=  }}
*{{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  | author=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=  }}
*{{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 }}
*{{cite journal | author=Bertenshaw GP, Turk BE, Hubbard SJ, ''et al.'' |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 }}
*{{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 }}
*{{cite journal  | author=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 }}
*{{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 | author=Leuenberger B, Hahn D, Pischitzis A, ''et al.'' |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 }}
*{{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 }}
*{{cite journal  | author=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 }}
*{{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 | author=Norman LP, Jiang W, Han X, ''et al.'' |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=  }}
*{{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 }}
*{{cite journal | author=Hahn D, Pischitzis A, Roesmann S, ''et al.'' |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 }}
*{{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  | author=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 }}
*{{cite journal | author=Becker-Pauly C, Höwel M, Walker T, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 06:23, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Meprin A subunit beta is a protein that in humans is encoded by the MEP1B gene.[1][2]

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][2]

References

  1. ↑ 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. PMID 7774936.
  2. ↑ 2.0 2.1 "Entrez Gene: MEP1B meprin A, beta".

Further reading



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