Biology:CPD (gene)
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Carboxypeptidase D is an enzyme that in humans is encoded by the CPD gene.[1][2][3]
Function
The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities: the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene.[3]
References
- ↑ "Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1)". Genomics 50 (1): 105–8. May 1998. doi:10.1006/geno.1998.5295. PMID 9628828.
- ↑ "Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains". The Biochemical Journal 327 ( Pt 1) (Pt 1): 81–7. Oct 1997. doi:10.1042/bj3270081. PMID 9355738.
- ↑ 3.0 3.1 "Entrez Gene: CPD carboxypeptidase D". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1362.
Further reading
- "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry 236 (1): 107–13. Apr 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein". Life Sciences 60 (10): 715–24. 1997. doi:10.1016/S0024-3205(96)00642-X. PMID 9064476.
- "Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface". Journal of Cell Science 111 ( Pt 7) (7): 877–85. Apr 1998. doi:10.1242/jcs.111.7.877. PMID 9490632.
- "Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme". Gene 215 (2): 361–70. Jul 1998. doi:10.1016/S0378-1119(98)00270-4. PMID 9714835.
- "Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord". The Journal of Histochemistry and Cytochemistry 46 (12): 1359–68. Dec 1998. doi:10.1177/002215549804601204. PMID 9815277.
- "Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium". Molecular Pharmacology 59 (5): 1324–32. May 2001. doi:10.1124/mol.59.5.1324. PMID 11306718.
- "Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary". The Journal of Histochemistry and Cytochemistry 50 (11): 1509–16. Nov 2002. doi:10.1177/002215540205001111. PMID 12417617.
- "Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking". The Journal of Biological Chemistry 278 (11): 9244–9. Mar 2003. doi:10.1074/jbc.M209379200. PMID 12643288.
- "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nature Biotechnology 21 (6): 660–6. Jun 2003. doi:10.1038/nbt827. PMID 12754519.
- "Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells". The Biochemical Journal 390 (Pt 3): 665–73. Sep 2005. doi:10.1042/BJ20050025. PMID 15918796.
External links
- Human CPD genome location and CPD gene details page in the UCSC Genome Browser.
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