The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CPZ  -  carboxypeptidase Z

Homo sapiens

Synonyms: Carboxypeptidase Z
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CPZ

  • In luteinizing hormone/follicle-stimulating hormone (LH/FSH)-producing gonadotroph adenomas, which do not require carboxypeptidases to produce gonadotropins, only CPZ immunostaining was demonstrated [1].
  • This study evaluated the expression patterns of CPE, CPD, and CPZ immunoreactivity in 48 pituitary adenomas [1].
  • The 641-amino acid form of CPZ expressed in the baculovirus system cleaves 5-dimethylaminonaphthalene-1-sulfonyl (dansyl)-Phe-Ala-Arg, although the level of enzyme activity was approximately 10-fold lower than either carboxypeptidase E or D expressed using the same viral system [2].
  • A human adenocarcinoma of the colon shows expression of CPZ in the extracellular matrix adjacent to malignant cells [3].
  • Endogenous CPZ in the PC12 rat pheochromocytoma cell line is also associated with the extracellular matrix [3].

High impact information on CPZ

  • Carboxypeptidase Z (CPZ) is a newly reported member of the metallocarboxypeptidase gene family, but unlike other members of this family, CPZ contains an N-terminal domain that has amino acid sequence similarity to Wnt-binding proteins [3].
  • CPZ is also present in amnion cells, but is not readily apparent in the extracellular matrix of this cell type [3].
  • In human placenta, CPZ is present within invasive trophoblasts and in the surrounding extracellular space, indicating an association with extracellular matrix [3].
  • Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues [3].

Biological context of CPZ


Anatomical context of CPZ

  • In null-cell adenomas, CPE immunoreactivity was detected in the majority of tumors, but CPD and CPZ were identified only in a minority of cases [1].
  • When expressed in the AtT-20 mouse pituitary cell line, CPZ protein is routed to the regulated secretory pathway and secreted upon stimulation [3].
  • Mild to moderate immunoreactivities for CPE and CPZ were distributed relatively uniformly in the majority of the anterior pituitary cells and basophil invasion [5].
  • Northern blot analysis showed rat CPZ mRNA to be abundant in the placenta, with low to moderate levels in the brain, lung, thymus, and kidney [6].
  • The BRL3A rat liver cell line and the PC12 rat adrenal cell line express high levels of CPZ mRNA [6].

Associations of CPZ with chemical compounds

  • In addition to containing a metallocarboxypeptidase domain, CPZ also contains a Cys-rich domain that has homology to Wnt-binding proteins; Wnts are important signaling molecules during development [4].

Physical interactions of CPZ

  • CPZ binds myristoylated as well as non-myristoylated NCS-1 in Ca(2+)-dependent manner, with dynamic interaction to myristoylated protein [7].

Other interactions of CPZ


Analytical, diagnostic and therapeutic context of CPZ

  • In order to gain insights as to the potential function of CPZ, the intracellular localization of this protein was determined in cell culture and in human tissues [3].
  • In situ hybridization analysis indicated that CPZ is expressed only in specific cell types [6].
  • Sequence analysis showed rat and human CPZ to be highly conserved within the frizzled domain (77% amino acid identity), the carboxypeptidase domain (91%), and the C-terminal 28 residues (78%) [6].
  • Early subjective response and symptom change at twenty-four and forty-eight hours following initiation of drug therapy with either CPZ or haloperidol were the only variables that significantly related to therapeutic outcome [9].
  • Increase in activity for the C-terminal Pro-X bond by site-directed mutagenesis of Gly137 to Ala in carboxypeptidase Z [10].


  1. Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary. Fan, X., Olson, S.J., Blevins, L.S., Allen, G.S., Johnson, M.D. J. Histochem. Cytochem. (2002) [Pubmed]
  2. Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase. Song, L., Fricker, L.D. J. Biol. Chem. (1997) [Pubmed]
  3. Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues. Novikova, E.G., Reznik, S.E., Varlamov, O., Fricker, L.D. J. Biol. Chem. (2000) [Pubmed]
  4. Carboxypeptidases from A to z: implications in embryonic development and Wnt binding. Reznik, S.E., Fricker, L.D. Cell. Mol. Life Sci. (2001) [Pubmed]
  5. Immunohistochemical localization and comparison of carboxypeptidases D, E, and Z, alpha-MSH, ACTH, and MIB-1 between human anterior and corticotroph cell "basophil invasion" of the posterior pituitary. Fan, X., Olson, S.J., Johnson, M.D. J. Histochem. Cytochem. (2001) [Pubmed]
  6. Cloning, sequence analysis, and distribution of rat metallocarboxypeptidase Z. Xin, X., Day, R., Dong, W., Lei, Y., Fricker, L.D. DNA Cell Biol. (1998) [Pubmed]
  7. Calcium and chlorpromazine binding to the EF-hand peptides of neuronal calcium sensor-1. Muralidhar, D., Kunjachen Jobby, M., Jeromin, A., Roder, J., Thomas, F., Sharma, Y. Peptides (2004) [Pubmed]
  8. Molecular cloning and sequence analysis of the scpZ gene encoding the serine carboxypeptidase of Absidia zychae. Lee, B.R., Takeuchi, M., Kobayashi, Y. Curr. Genet. (1995) [Pubmed]
  9. Early treatment events and prediction of response to neuroleptics in schizophrenia. Awad, A.G., Hogan, T.P. Prog. Neuropsychopharmacol. Biol. Psychiatry (1985) [Pubmed]
  10. Increase in activity for the C-terminal Pro-X bond by site-directed mutagenesis of Gly137 to Ala in carboxypeptidase Z. Ratanakhanokchai, K., Lee, B.R., Kobayashi, Y., Takeuchi, M. Biosci. Biotechnol. Biochem. (1996) [Pubmed]
WikiGenes - Universities