MEP1A

From Wikipedia, the free encyclopedia

Meprin A, alpha (PABA peptide hydrolase)

Identifiers

External IDs

OMIM: 600388 MGI: 96963 HomoloGene: 31323

Gene ontology
Molecular Function:	• meprin A activity • metallopeptidase activity • zinc ion binding • astacin activity • metal ion binding
Cellular Component:	• extracellular space • soluble fraction • integral to plasma membrane • microvillus • membrane
Biological Process:	• proteolysis • digestion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005588 (mRNA)
NP_005579 (protein)

NM_008585 (mRNA)
NP_032611 (protein)

Location

Chr 6: 46.87 - 46.92 Mb

Chr 17: 42.94 - 42.97 Mb

Pubmed search

[1]

[2]

Meprin A, alpha (PABA peptide hydrolase), also known as MEP1A, is a human gene.^[1]

[edit] References

^ Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase).

[edit] Further reading

Dumermuth E, Sterchi EE, Jiang WP, et al. (1991). "The astacin family of metalloendopeptidases.". J. Biol. Chem. 266 (32): 21381–5. PMID 1939172.
Kärgel HJ, Dettmer R, Etzold G, et al. (1982). "Action of rat liver cathepsin L on glucagon.". Acta Biol. Med. Ger. 40 (9): 1139–43. PMID 7340337.
Bond JS, Rojas K, Overhauser J, et al. (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. PMID 7774936.
Kaushal GP, Walker PD, Shah SV (1994). "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.". J. Cell Biol. 126 (5): 1319–27. PMID 8063866.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Dumermuth E, Eldering JA, Grünberg J, et al. (1994). "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells.". FEBS Lett. 335 (3): 367–75. PMID 8262185.
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. PMID 8660687.
Chevallier S, Ahn J, Boileau G, Crine P (1996). "Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin.". Biochem. J. 317 ( Pt 3): 731–8. PMID 8760356.
Eldering JA, Grünberg J, Hahn D, et al. (1997). "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.". Eur. J. Biochem. 247 (3): 920–32. PMID 9288916.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Lottaz D, Hahn D, Müller S, et al. (1999). "Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits.". Eur. J. Biochem. 259 (1-2): 496–504. PMID 9914532.
Richter R, Schulz-Knappe P, Schrader M, et al. (1999). "Composition of the peptide fraction in human blood plasma: database of circulating human peptides.". J. Chromatogr. B Biomed. Sci. Appl. 726 (1-2): 25–35. PMID 10348167.
Köhler D, Kruse M, Stöcker W, Sterchi EE (2000). "Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro.". FEBS Lett. 465 (1): 2–7. PMID 10620696.
Jiang W, Le B (2000). "Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase meprin A.". Arch. Biochem. Biophys. 379 (2): 183–7. doi:10.1006/abbi.2000.1873. PMID 10898933.
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. PMID 11267665.
Bertenshaw GP, Turk BE, Hubbard SJ, et al. (2001). "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity.". J. Biol. Chem. 276 (16): 13248–55. doi:10.1074/jbc.M011414200. PMID 11278902.
Ishmael FT, Norcum MT, Benkovic SJ, Bond JS (2001). "Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer.". J. Biol. Chem. 276 (25): 23207–11. doi:10.1074/jbc.M102654200. PMID 11301339.
Rösmann S, Hahn D, Lottaz D, et al. (2002). "Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system.". J. Biol. Chem. 277 (43): 40650–8. doi:10.1074/jbc.M206203200. PMID 12189145.
Norman LP, Jiang W, Han X, et al. (2003). "Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles.". Mol. Cell. Biol. 23 (4): 1221–30. PMID 12556482.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.