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CPM (gene)

Introduction

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

Function

Function

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

References

  1. ↑ Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). “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. ↑ 2.0 2.1 “Entrez Gene: CPM carboxypeptidase M”.
External links
Further reading

Further reading

  • Fujiwara H, Imai K, Inoue T, Maeda M, Fujii S (February 1999). “Membrane-bound cell surface peptidases in reproductive organs”. Endocrine Journal. 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”. Advances in Experimental Medicine and Biology. 477: 205–16. doi:10.1007/0-306-46826-3_23. PMID 10849748.
  • Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). “Carboxypeptidase M in brain and peripheral nerves”. Journal of Neurochemistry. 59 (6): 2201–12. doi:10.1111/j.1471-4159.1992.tb10112.x. PMID 1431901.
  • Tan F, Chan SJ, Steiner DF, Schilling JW, Skidgel RA (August 1989). “Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N”. The Journal of Biological Chemistry. 264 (22): 13165–70. PMID 2753907.
  • Skidgel RA, Davis RM, Tan F (February 1989). “Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones”. The Journal of Biological Chemistry. 264 (4): 2236–41. PMID 2914904.
  • McGwire GB, Skidgel RA (July 1995). “Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M”. The Journal of Biological Chemistry. 270 (29): 17154–8. doi:10.1074/jbc.270.29.17154. PMID 7615511.
  • de Saint-Vis B, Cupillard L, Pandrau-Garcia D, Ho S, Renard N, Grouard G, Duvert V, Thomas X, Galizzi JP, Banchereau J (August 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 (June 1995). “Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation”. The Journal of Biological Chemistry. 270 (26): 15644–9. doi:10.1074/jbc.270.26.15644. PMID 7797563.
  • Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG (August 1993). “High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells”. American Journal of Respiratory Cell and Molecular Biology. 9 (2): 221–9. doi:10.1165/ajrcmb/9.2.221. PMID 8338689.
  • Michel B, Igić R, Leray V, Deddish PA, Erdös EG (April 1996). “Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M”. Circulation Research. 78 (4): 635–42. doi:10.1161/01.res.78.4.635. PMID 8635221.
  • Skidgel RA, McGwire GB, Li XY (May 1996). “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 (September 1996). “Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Yoshioka S, Fujiwara H, Yamada S, Nakayama T, Higuchi T, Inoue T, Mori T, Maeda M (July 1998). “Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy”. Molecular Human Reproduction. 4 (7): 709–17. doi:10.1093/molehr/4.7.709. PMID 9701794.
  • Li XY, Skidgel RA (April 1999). “Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis”. Biochemical and Biophysical Research Communications. 258 (1): 204–10. doi:10.1006/bbrc.1999.0619. PMID 10222261.
  • Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A (January 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, Mizushima-Sugano J, Sese J, Hata H, Ota T, Isogai T, Tanaka T, Morishita S, Okubo K, Sakaki Y, Nakamura Y, Suyama A, Sugano S (May 2001). “Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites”. EMBO Reports. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929.
  • Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A (June 2001). “Expression and activity of ectopeptidases in fibrillating human atria”. Journal of Molecular and Cellular Cardiology. 33 (6): 1273–81. doi:10.1006/jmcc.2001.1389. PMID 11444929.