CPM (gene)

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Carboxypeptidase M
Protein CPM PDB 1uwy.png
PDB rendering based on 1uwy.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol CPM
External IDs OMIM114860 MGI1917824 HomoloGene35367 ChEMBL: 3038 GeneCards: CPM Gene
EC number 3.4.17.12
RNA expression pattern
PBB GE CPM 206100 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1368 70574
Ensembl ENSG00000135678 ENSMUSG00000020183
UniProt P14384 Q80V42
RefSeq (mRNA) NM_001005502 NM_027468
RefSeq (protein) NP_001005502 NP_081744
Location (UCSC) Chr 12:
69.24 – 69.37 Mb
Chr 10:
117.63 – 117.69 Mb
PubMed search [1] [2]

Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene.[1][2]

The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.[2]

References[edit]

  1. ^ Kas K, Schoenmakers EF, Van de Ven WJ (Mar 1996). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics 30 (2): 403–5. PMID 8586455. 
  2. ^ a b "Entrez Gene: CPM carboxypeptidase M". 

Further reading[edit]

  • Fujiwara H, Imai K, Inoue T, et al. (1999). "Membrane-bound cell surface peptidases in reproductive organs.". Endocr. J. 46 (1): 11–25. doi:10.1507/endocrj.46.11. PMID 10426564. 
  • Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo.". Adv. Exp. Med. Biol. 477: 205–16. doi:10.1007/0-306-46826-3_23. PMID 10849748. 
  • Nagae A, Deddish PA, Becker RP, et al. (1992). "Carboxypeptidase M in brain and peripheral nerves.". J. Neurochem. 59 (6): 2201–12. doi:10.1111/j.1471-4159.1992.tb10112.x. PMID 1431901. 
  • Tan F, Chan SJ, Steiner DF, et al. (1989). "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N.". J. Biol. Chem. 264 (22): 13165–70. PMID 2753907. 
  • Skidgel RA, Davis RM, Tan F (1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones.". J. Biol. Chem. 264 (4): 2236–41. PMID 2914904. 
  • McGwire GB, Skidgel RA (1995). "Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M.". J. Biol. Chem. 270 (29): 17154–8. doi:10.1074/jbc.270.29.17154. PMID 7615511. 
  • de Saint-Vis B, Cupillard L, Pandrau-Garcia D, et al. (1995). "Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13.". Blood 86 (3): 1098–105. PMID 7620164. 
  • Rehli M, Krause SW, Kreutz M, Andreesen R (1995). "Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation.". J. Biol. Chem. 270 (26): 15644–9. doi:10.1074/jbc.270.26.15644. PMID 7797563. 
  • Nagae A, Abe M, Becker RP, et al. (1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells.". Am. J. Respir. Cell Mol. Biol. 9 (2): 221–9. doi:10.1165/ajrcmb/9.2.221. PMID 8338689. 
  • Michel B, Igić R, Leray V, et al. (1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M.". Circ. Res. 78 (4): 635–42. PMID 8635221. 
  • Skidgel RA, McGwire GB, Li XY (1997). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones.". Immunopharmacology 32 (1–3): 48–52. doi:10.1016/0162-3109(96)00008-2. PMID 8796265. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
  • Yoshioka S, Fujiwara H, Yamada S, et al. (1998). "Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy". Mol. Hum. Reprod. 4 (7): 709–17. doi:10.1093/molehr/4.7.709. PMID 9701794. 
  • Li XY, Skidgel RA (1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochem. Biophys. Res. Commun. 258 (1): 204–10. doi:10.1006/bbrc.1999.0619. PMID 10222261. 
  • Bektas A, Hughes JN, Warram JH, et al. (2001). "Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes". Diabetes 50 (1): 204–8. doi:10.2337/diabetes.50.1.204. PMID 11147789. 
  • Suzuki Y, Taira H, Tsunoda T, et al. (2001). "Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites". EMBO Rep. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929. 
  • Lendeckel U, Arndt M, Wrenger S, et al. (2001). "Expression and activity of ectopeptidases in fibrillating human atria". J. Mol. Cell. Cardiol. 33 (6): 1273–81. doi:10.1006/jmcc.2001.1389. PMID 11444929.