| Agmatine modulates polyamine content in hepatocytes by inducing spermidine/spermine acetyltransferase. | |
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MedLine Citation:
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PMID: 10092884 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Agmatine has been proposed as the physiological ligand for the imidazoline receptors. It is not known whether it is also involved in the homoeostasis of intracellular polyamine content. To show whether this is the case, we have studied the effect of agmatine on rat liver cells, under both periportal and perivenous conditions. It is shown that agmatine modulates intracellular polyamine content through its effect on the synthesis of the limiting enzyme of the interconversion pathway, spermidine/spermine acetyltransferase (SSAT). Increased SSAT activity is accompanied by depletion of spermidine and spermine, and accumulation of putrescine and N1-acetylspermidine. Immunoblotting with a specific polyclonal antiserum confirms the induction. At the same time S-adenosylmethionine decarboxylase activity is significantly increased, while ornithine decarboxylase (ODC) activity and the rate of spermidine uptake are reduced. This is not due to an effect on ODC antizyme, which is not significantly changed. All these modifications are observed in HTC cells also, where they are accompanied by a decrease in proliferation rate. SSAT is also induced by low oxygen tension which mimics perivenous conditions. The effect is synergic with that promoted by agmatine. |
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Authors:
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C Vargiu; C Cabella; S Belliardo; C Cravanzola; M A Grillo; S Colombatto |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 259 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1999 Feb |
Date Detail:
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Created Date: 1999-04-22 Completed Date: 1999-04-22 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: 933-8 Citation Subset: IM |
Affiliation:
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Dipartimento di Medicina e Oncologia Sperimentale, Universitá di Torino, Italy. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acetyltransferases
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metabolism* Adenosylmethionine Decarboxylase / metabolism Agmatine / pharmacology* Animals Cell Division / genetics Cells, Cultured Humans Liver / drug effects, enzymology* Male Ornithine Decarboxylase / metabolism Polyamines / metabolism* Rats Rats, Wistar Recombinant Proteins Spermidine / metabolism Time Factors |
| Chemical | |
Reg. No./Substance:
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0/Polyamines; 0/Recombinant Proteins; 124-20-9/Spermidine; 306-60-5/Agmatine; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.57/diamine N-acetyltransferase; EC 4.1.1.17/Ornithine Decarboxylase; EC 4.1.1.50/Adenosylmethionine Decarboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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