Please use this identifier to cite or link to this item:
Title: Molecular structure and alternative splicing of the human carboxypeptidase M gene
Authors: Pessoa, L. G.
Silva, IDG da
Baptista, H. A.
Pesquero, J. L.
Paiva, ACM
Bader, M.
Pesquero, J. B.
Max Delbruck Ctr Mol Med
Universidade Federal de São Paulo (UNIFESP)
Universidade Federal de Minas Gerais (UFMG)
Keywords: carboxypeptidases
gene structure
kininase I
Issue Date: 1-Feb-2002
Publisher: Walter de Gruyter & Co
Citation: Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 383, n. 2, p. 263-269, 2002.
Abstract: Using RACE technology the 5' and 31 ends of human carboxypeptidase M (CPM) mRNA were determined and found to be divergent from the published sequence. With these results the complete structure of the human CPM gene was established based on the human genome sequence in the GenBank database. the gene was shown to contain 9 exons comprising at least 75 kb of genomic sequence. A novel first exon of 30 bp was identified and an upstream promoter sequence containing several transcription factor binding sites was found by computer analysis. Furthermore, the ATG starting codon was detected defining an open reading frame of 1329 bp that codes for a protein of 443 residues. Additionally, the polyadenylation site was discovered, determining a 31 noncoding region of 2000 nucleotides. the exon-intron boundaries diverged substantially compared to those of the other basic carboxypeptidases, CPD, CPE, CPN, and AEBP1. Cloning and sequencing of RT-PCR products from different tissues revealed alternative splicing of exons 3 and 5, which results in the generation of four different mRNA isoforms. RNA extracted from tumor tissues contained more CPM mRNA than control tissue, suggesting an upregulation of CPM expression in tumors and raising the question of the role of this enzyme in cancer.
ISSN: 1431-6730
Other Identifiers:
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.