Lt. Pitkanen et al., Expression of a novel human ornithine decarboxylase-like protein in the central nervous system and testes, BIOC BIOP R, 287(5), 2001, pp. 1051-1057
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Ornithine decarboxylase (ODC) is the key enzyme of polyamine synthesis. The
physiological activity of ODC is associated with cell proliferation, and h
igh ODC activities are encountered in rapidly growing cancer cells. We have
cloned a cDNA for a novel human protein that is 54% identical to ODC and 4
5% identical to antizyme inhibitor (AZI). mRNA for ODC-paralogue (ODC-p) wa
s found only in the central nervous system and testes, suggesting a role in
terminal differentiation rather than cell proliferation. ODC-p occurs at l
east in eight alternatively spliced forms. In vitro translated ODC-p did no
t decarboxylate ornithine, whereas, in vivo, one splice variant exerted mod
est ODC-like activity upon expression in COS-7 cells. ODC-p has a unique mu
tation in cysteine 360, where this ornithine decarboxylase reaction-directi
ng residue is substituted by a valine. This substitution might lead to an e
nzymatic reaction that differs from typical ODC activity. ODC-p might also
function as a brain- and testis-specific AZI. (C) 2001 Academic Press.