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

CPA4  -  carboxypeptidase A4

Homo sapiens

Synonyms: CPA3, Carboxypeptidase A3, Carboxypeptidase A4, UNQ694/PRO1339
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 CPA4

  • Because CPA4 was originally identified as a protein induced in a prostate cancer cell line (PC-3) by histone deacetylase inhibitors, and was located at the putative prostate cancer-aggressiveness locus at 7q32, we investigated its imprinting status in fetal tissues and in adult benign hypertrophic prostate (BPH) [1].

High impact information on CPA4

  • Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin [2].
  • The consistent induction of CPA3 by NaBu in several prostate cancer cell lines led us to investigate the signaling pathway involved in the induction of CPA3 mRNA [3].
  • Trichostatin A, a potent and specific inhibitor of histone deacetylase, also induced CPA3 mRNA expression, suggesting that CPA3 gene induction is mediated by histone hyperacetylation [3].
  • The structural similarity between CPA3 and its closest homologues indicates that the putative CPA3 protein contains a 16-residue signal peptide sequence, a 95-residue NH2-terminal activation segment, and a 310-residue CP enzyme domain [3].
  • However, analysis of ten SRS patients revealed no mutations in CPA4 [1].

Biological context of CPA4

  • As CPA4 has a potential role in cell proliferation and differentiation, two preferentially expressed copies in mUPD patients with SRS syndrome would result in excess expression and could alter the growth profiles of these subjects and give rise to intrauterine growth restriction [4].

Anatomical context of CPA4

  • RT-PCR using four intragenic polymorphisms as markers showed that CPA4 was expressed preferentially from the maternal allele in the fetal heart, lung, liver, intestine, kidney, adrenal gland, and spleen, but not in the fetal brain [1].

Associations of CPA4 with chemical compounds

  • We demonstrated that CPA3 induction was a downstream effect of the treatment with butyrate or trichostatin A, but that the induction of p21(WAF1/CIP1) occurred immediately after these treatments [3].

Physical interactions of CPA4

  • Such an inhibitory mode is evocative of the recently reported structure of the human inhibitor latexin in its complex with hCPA4 [5].


  1. The novel imprinted carboxypeptidase A4 gene ( CPA4) in the 7q32 imprinting domain. Kayashima, T., Yamasaki, K., Yamada, T., Sakai, H., Miwa, N., Ohta, T., Yoshiura, K., Matsumoto, N., Nakane, Y., Kanetake, H., Ishino, F., Niikawa, N., Kishino, T. Hum. Genet. (2003) [Pubmed]
  2. Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin. Pallarès, I., Bonet, R., García-Castellanos, R., Ventura, S., Avilés, F.X., Vendrell, J., Gomis-Rüth, F.X. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. Huang, H., Reed, C.P., Zhang, J.S., Shridhar, V., Wang, L., Smith, D.I. Cancer Res. (1999) [Pubmed]
  4. The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate for Silver-Russell syndrome. Bentley, L., Nakabayashi, K., Monk, D., Beechey, C., Peters, J., Birjandi, Z., Khayat, F.E., Patel, M., Preece, M.A., Stanier, P., Scherer, S.W., Moore, G.E. J. Med. Genet. (2003) [Pubmed]
  5. Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin. García-Castellanos, R., Bonet-Figueredo, R., Pallarés, I., Ventura, S., Avilés, F.X., Vendrell, J., Gomis-Rütha, F.X. Cell. Mol. Life Sci. (2005) [Pubmed]
WikiGenes - Universities