Document Detail


Agmatine modulates polyamine content in hepatocytes by inducing spermidine/spermine acetyltransferase.
MedLine Citation:
PMID:  10092884     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
C Vargiu; C Cabella; S Belliardo; C Cravanzola; M A Grillo; S Colombatto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  259     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1999 Feb 
Date Detail:
Created Date:  1999-04-22     Completed Date:  1999-04-22     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  933-8     Citation Subset:  IM    
Affiliation:
Dipartimento di Medicina e Oncologia Sperimentale, Universitá di Torino, Italy.
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MeSH Terms
Descriptor/Qualifier:
Acetyltransferases / 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:
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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