Literature DB >> 6415054

Chinese hamster ovary cells resistant to alpha-difluoromethylornithine are overproducers of ornithine decarboxylase.

J H Choi, I E Scheffler.   

Abstract

The selection of Chinese hamster ovary cells resistant to ornithine analogues has been extended to very high levels of the suicide inhibitor alpha-difluoromethylornithine. Stepwise selections resulted in stepwise increases in the inducible levels of ornithine decarboxylase activity. The enzyme is shown by several criteria to be normal in every respect: regulation in the cell cycle, inhibition by antizyme, absolute specific activity as determined with the help of alpha-[3H]difluoromethylornithine. The enzyme has been highly purified from such overproducing cells. The subunit molecular weight of the mammalian enzyme has been confirmed to be approximately 54,000. The location of the enzyme in two-dimensional polyacrylamide gel electrophoresis was determined, and the protein could be detected on two-dimensional gels with extracts from our best overproducers.

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Year:  1983        PMID: 6415054

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  12 in total

1.  Polyamine-mediated turnover of ornithine decarboxylase in Chinese-hamster ovary cells.

Authors:  J R Glass; E W Gerner
Journal:  Biochem J       Date:  1986-06-01       Impact factor: 3.857

2.  Tumor attenuation by combined heparan sulfate and polyamine depletion.

Authors:  Mattias Belting; Lubor Borsig; Mark M Fuster; Jillian R Brown; Lo Persson; Lars-Ake Fransson; Jeffrey D Esko
Journal:  Proc Natl Acad Sci U S A       Date:  2001-12-18       Impact factor: 11.205

3.  Antizyme, a protein induced by polyamines, accelerates the degradation of ornithine decarboxylase in Chinese-hamster ovary-cell extracts.

Authors:  Y Murakami; K Tanaka; S Matsufuji; Y Miyazaki; S Hayashi
Journal:  Biochem J       Date:  1992-05-01       Impact factor: 3.857

4.  Variations in amplification and expression of the ornithine decarboxylase gene in human breast cancer cells.

Authors:  T Thomas; D T Kiang; O A Jänne; T J Thomas
Journal:  Breast Cancer Res Treat       Date:  1991-11       Impact factor: 4.872

Review 5.  Rapid and regulated degradation of ornithine decarboxylase.

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

6.  Isolation of cloned cDNA encoding mammalian ornithine decarboxylase.

Authors:  C Kahana; D Nathans
Journal:  Proc Natl Acad Sci U S A       Date:  1984-06       Impact factor: 11.205

7.  Overproduction of stable ornithine decarboxylase and antizyme in the difluoromethylornithine-resistant cell line DH23b.

Authors:  J L Mitchell; C Y Choe; G G Judd; D J Daghfal; R J Kurzeja; A Leyser
Journal:  Biochem J       Date:  1996-08-01       Impact factor: 3.857

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

Authors:  Y Murakami; S Matsufuji; Y Miyazaki; S Hayashi
Journal:  Biochem J       Date:  1994-11-15       Impact factor: 3.857

9.  Ornithine decarboxylase production in vitro by using mouse cDNA.

Authors:  J R Glass; M MacKrell; J J Duffy; E W Gerner
Journal:  Biochem J       Date:  1987-07-01       Impact factor: 3.857

10.  Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney.

Authors:  J E Seely; L Persson; G J Sertich; A E Pegg
Journal:  Biochem J       Date:  1985-03-01       Impact factor: 3.857

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