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CPZ  -  carboxypeptidase Z

Homo sapiens

Synonyms: Carboxypeptidase Z
 
 
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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].

References

  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]
 
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