MEP1A

Revision as of 19:17, 4 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Meprin A, alpha (PABA peptide hydrolase)
Identifiers
Symbols MEP1A ; PPHA
External IDs Template:OMIM5 Template:MGI HomoloGene31323
RNA expression pattern
File:PBB GE MEP1A 206000 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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


References

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

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.

Template:WikiDoc Sources