The mechanisms of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH 3T3 cells - PubMed (original) (raw)
. 1988 Mar 25;263(9):4500-7.
Affiliations
- PMID: 3279036
Free article
The mechanisms of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH 3T3 cells
E Hölttä et al. J Biol Chem. 1988.
Free article
Abstract
NIH 3T3 cells transformed with the human c-Ha-rasVal-12 oncogene showed markedly enhanced activity of ornithine decarboxylase (ODC), the key enzyme of polyamine biosynthesis, as compared with their nontransformed counterparts. While in normal and in c-Ha-ras proto-oncogene-transfected cells stimulation with serum caused a transient induction of ODC, in cells transfected with the mutant c-Ha-ras oncogene the activity of ODC persisted at high levels for greatly extended periods of time. The amounts of immunoreactive ODC protein roughly paralleled the changes in the enzyme activity. The augmentation of ODC content by transformation could be largely, but not solely, accounted for by an enhanced accumulation of ODC mRNA. Nuclear run-off transcription assays demonstrated that in transformed cells the rate of transcription of the ODC gene was increased but to a much lower extent than the increase in the level of ODC mRNA. The turnover of ODC mRNA, as measured after actinomycin D treatment, was negligible in transformed cells for up to 8 h, whereas in normal cells the messenger content was initially decreased, by 40% within 4 h, and then remained constant. In normal cells, however, actinomycin D depressed the expression of ODC by more than 80%, while in transformed cells the activity of ODC was slightly superinduced, corresponding to the changes of ODC mRNA. These findings suggest that labile proteins may be involved in the regulation of both the stability and translatability of the ODC mRNA. Transformation led also to about 3-fold stabilization of ODC as determined by an exposure of the cells to cycloheximide. The results thus suggest ODC deregulation at multiple levels in the ras-oncogene-transformed cells.
Similar articles
- The cellular response to induction of the p21 c-Ha-ras oncoprotein includes stimulation of jun gene expression.
Sistonen L, Hölttä E, Mäkelä TP, Keski-Oja J, Alitalo K. Sistonen L, et al. EMBO J. 1989 Mar;8(3):815-22. doi: 10.1002/j.1460-2075.1989.tb03442.x. EMBO J. 1989. PMID: 2498084 Free PMC article. - Ornithine decarboxylase induction in transformation by H-Ras and RhoA.
Shantz LM, Pegg AE. Shantz LM, et al. Cancer Res. 1998 Jul 1;58(13):2748-53. Cancer Res. 1998. PMID: 9661886 - Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential.
Shantz LM, Levin VA. Shantz LM, et al. Amino Acids. 2007 Aug;33(2):213-23. doi: 10.1007/s00726-007-0531-2. Epub 2007 Apr 19. Amino Acids. 2007. PMID: 17443268 Review.
Cited by
- The cellular response to induction of the p21 c-Ha-ras oncoprotein includes stimulation of jun gene expression.
Sistonen L, Hölttä E, Mäkelä TP, Keski-Oja J, Alitalo K. Sistonen L, et al. EMBO J. 1989 Mar;8(3):815-22. doi: 10.1002/j.1460-2075.1989.tb03442.x. EMBO J. 1989. PMID: 2498084 Free PMC article. - The translation in vitro of rat ornithine decarboxylase mRNA is blocked by its 5' untranslated region in a polyamine-independent way.
Van Steeg H, Van Oostrom CT, Hodemaekers HM, Peters L, Thomas AA. Van Steeg H, et al. Biochem J. 1991 Mar 1;274 ( Pt 2)(Pt 2):521-6. doi: 10.1042/bj2740521. Biochem J. 1991. PMID: 2006916 Free PMC article. - Polyamines are essential for cell transformation by pp60v-src: delineation of molecular events relevant for the transformed phenotype.
Hölttä E, Auvinen M, Andersson LC. Hölttä E, et al. J Cell Biol. 1993 Aug;122(4):903-14. doi: 10.1083/jcb.122.4.903. J Cell Biol. 1993. PMID: 7688751 Free PMC article. - Amino acids regulate expression of antizyme-1 to modulate ornithine decarboxylase activity.
Ray RM, Viar MJ, Johnson LR. Ray RM, et al. J Biol Chem. 2012 Feb 3;287(6):3674-90. doi: 10.1074/jbc.M111.232561. Epub 2011 Dec 7. J Biol Chem. 2012. PMID: 22157018 Free PMC article. - p44/42 mitogen-activated protein kinase is involved in the expression of ornithine decarboxylase in leukaemia L1210 cells.
Flamigni F, Facchini A, Capanni C, Stefanelli C, Tantini B, Caldarera CM. Flamigni F, et al. Biochem J. 1999 Jul 15;341 ( Pt 2)(Pt 2):363-9. Biochem J. 1999. PMID: 10393094 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials