| Overproduction of S-adenosylmethionine decarboxylase in ethylglyoxal-bis(guanylhydrazone)-resistant mouse FM3A cells. | |
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MedLine Citation:
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PMID: 8344293 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A variant cell line, termed SAM-1, which overproduced S-adenosylmethionine decarboxylase (AdoMetDC), was isolated by treatment of mouse FM3A cells with N-methyl-N'-nitro-N-nitrosoguanidine and subsequent incubation with ethylglyoxal bis(guanylhydrazone), an inhibitor of the enzyme. The cells were resistant to ethylglyoxal bis(guanylhydrazone), and showed AdoMetDC activity approximately five-times higher than control cells. The rate of AdoMetDC synthesis and the amount of AdoMetDC existing in SAM-1 cells were about five-times those in control cells. The amount of AdoMetDC mRNA existing in SAM-1 cells was five-times more than that in control cells. The amount of 5'-([(Z)-4-amino-2-butenyl]methylamino)-5'-deoxyadenosine, an irreversible inhibitor of AdoMetDC, necessary to inhibit cell growth was also five-times more in SAM-1 cells than in control cells. However, the following were the same in both SAM-1 and control cells; the amount of genomic DNA for AdoMetDC, the size and nucleotide sequence of 5' untranslated region of AdoMetDC mRNA, the deduced amino acid sequence (334 residues) from the nucleotide sequence of AdoMetDC cDNA and the degradation rate (t1/2 = about 4 h) of AdoMetDC. In addition, AdoMetDC mRNA in control cells was slightly more stable than that in SAM-1 cells. The results indicate that the overproduction of AdoMetDC in SAM-1 cells was caused by the increase of AdoMetDC mRNA. The variant cell line is convenient for studying the regulation of AdoMetDC and the physiological function of polyamines. |
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Authors:
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T Suzuki; Y Sadakata; K Kashiwagi; K Hoshino; Y Kakinuma; A Shirahata; K Igarashi |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 215 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1993 Jul |
Date Detail:
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Created Date: 1993-09-03 Completed Date: 1993-09-03 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 247-53 Citation Subset: IM |
Affiliation:
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Faculty of Pharmaceutical Sciences, Chiba University, Japan. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/D12780; L09682; L09683; X71336; X71337; X71338; X71339; X71340; X72303; X72968 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosylmethionine Decarboxylase
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antagonists & inhibitors,
biosynthesis*,
chemistry,
genetics Animals Base Sequence Blotting, Northern Blotting, Southern Cell Division / drug effects Cell Line DNA / chemistry, genetics Drug Resistance Half-Life Methylnitronitrosoguanidine / pharmacology Mice Mitoguazone / analogs & derivatives*, metabolism, pharmacology Molecular Sequence Data Polyamines / metabolism RNA, Messenger / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Polyamines; 0/RNA, Messenger; 1945-68-2/ethylglyoxal bis(guanylhydrazone); 459-86-9/Mitoguazone; 70-25-7/Methylnitronitrosoguanidine; 9007-49-2/DNA; EC 4.1.1.50/Adenosylmethionine Decarboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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