Carboxypeptidase M is an enzyme that in humans is encoded by the CPMgene.[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
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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. PMID10426564.
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. PMID10849748.
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. PMID2753907.
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. PMID2914904.
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. PMID7615511.
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. PMID7620164.
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. PMID7797563.
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. PMID8338689.
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. doi:10.1161/01.res.78.4.635. PMID8635221.
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. PMID8796265.
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. PMID8889548.
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. PMID9701794.
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. PMID10222261.
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. PMID11147789.
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. PMID11444929.