Dataset Information


Forced expression of antizyme abolishes ornithine decarboxylase activity, suppresses cellular levels of polyamines and inhibits cell growth.

ABSTRACT: Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. It is a short-lived protein and negatively regulated by its products, polyamines. Its degradation is accelerated by the binding of antizyme, an ODC-inhibitory protein induced by polyamines. To evaluate the physiological importance of antizyme we examined the effect of forced expression of antizyme on cellular ODC and polyamine levels and cell growth. Antizyme almost completely abolished the induction of ODC by growth stimuli. This may have been caused by antizyme-induced rapid degradation of newly synthesized ODC, since the half-life of ODC complexes with antizyme was less than 5 min. Forced expression of antizyme caused reductions of cellular putrescine and spermidine levels, and inhibited cell growth, which was partially restored by the addition of putrescine. These observations suggested a critically important role of antizyme in polyamine metabolism.

SUBMITTER: Murakami Y 

PROVIDER: S-EPMC1137469 | BioStudies | 1994-01-01

SECONDARY ACCESSION(S): 10.1042/bj3040183

REPOSITORIES: biostudies

Similar Datasets

2005-01-01 | S-EPMC1134669 | BioStudies
2000-01-01 | S-EPMC1220902 | BioStudies
1000-01-01 | S-EPMC535087 | BioStudies
2015-01-01 | S-EPMC5349141 | BioStudies
2000-01-01 | S-EPMC1221293 | BioStudies
1992-01-01 | S-EPMC1130936 | BioStudies
2000-01-01 | S-EPMC1220960 | BioStudies
2002-01-01 | S-EPMC1222781 | BioStudies
1998-01-01 | S-EPMC1219064 | BioStudies
2001-01-01 | S-EPMC1222066 | BioStudies