Literature DB >> 1577163

Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation.

C Ceriani1, N S González, I D Algranati.   

Abstract

Ornithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half-life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia ODC levels were not reduced by polyamines.

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Year:  1992        PMID: 1577163     DOI: 10.1016/0014-5793(92)80253-d

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain.

Authors:  F Svensson; C Ceriani; E L Wallström; I Kockum; I D Algranati; O Heby; L Persson
Journal:  Proc Natl Acad Sci U S A       Date:  1997-01-21       Impact factor: 11.205

Review 2.  Rapid and regulated degradation of ornithine decarboxylase.

Authors:  S Hayashi; Y Murakami
Journal:  Biochem J       Date:  1995-02-15       Impact factor: 3.857

3.  Trypanosoma cruzi Coexpressing Ornithine Decarboxylase and Green Fluorescence Proteins as a Tool to Study the Role of Polyamines in Chagas Disease Pathology.

Authors:  Jeremías José Barclay; Luciano Gastón Morosi; María Cristina Vanrell; Edith Corina Trejo; Patricia Silvia Romano; Carolina Carrillo
Journal:  Enzyme Res       Date:  2011-06-01
  3 in total

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