CPM (gene)

From Wikipedia, the free encyclopedia

Carboxypeptidase M

PDB rendering based on 1uwy.

Available structures: 1uwy

Identifiers

Symbol(s)

CPM;

External IDs

OMIM: 114860 MGI: 1917824 HomoloGene: 35367

Gene ontology
Molecular Function:	• carboxypeptidase A activity • ferric iron binding • metallopeptidase activity • zinc ion binding • metal ion binding • GPI anchor binding
Cellular Component:	• plasma membrane
Biological Process:	• proteolysis • aromatic compound metabolic process • anatomical structure morphogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001005502 (mRNA)
NP_001005502 (protein)

XM_917914 (mRNA)
XP_923007 (protein)

Location

Chr 12: 67.53 - 67.61 Mb

Chr 10: 117.03 - 117.09 Mb

Pubmed search

[1]

[2]

Carboxypeptidase M, also known as CPM, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CPM carboxypeptidase M.

[edit] Further reading

Fujiwara H, Imai K, Inoue T, et al. (1999). "Membrane-bound cell surface peptidases in reproductive organs.". Endocr. J. 46 (1): 11–25. 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. PMID 10849748.
Nagae A, Deddish PA, Becker RP, et al. (1992). "Carboxypeptidase M in brain and peripheral nerves.". J. Neurochem. 59 (6): 2201–12. 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. 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. 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. PMID 8338689.
Kas K, Schoenmakers EF, Van de Ven WJ (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.
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. PMID 8796265.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. 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. 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. 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. 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.