Document Detail


Histone acetyltransferase activity in rat hepatomas.
MedLine Citation:
PMID:  2808481     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In view of various reports describing differences in histone acetylation between normal rat liver and hepatomas, the behaviour of histone acetyltransferase (EC 2.3.1.48) activity was elucidated in normal rat liver and in a spectrum of well-characterized rat hepatomas of slow, intermediate and rapid growth rates. In all tumours the acetyltransferase specific activity, expressed as nmol h-1 mg total protein-1, was higher than in the corresponding normal livers and the rise correlated positively with the proliferation rates of the tumors. No difference is observed if acetyltransferase activity is expressed per milligram of histone. This is explained by elevated ratios of histones and of DNA to total protein in the hepatomas compared to the ratios in normal liver. Electrophoretic analysis of [3H]acetate-labeled histones revealed similar patterns in hepatoma and normal liver. The extent of histone H4 acetylation, as indicated by the frequency distribution of non-, mono-, di-, tri-, and tetraacetylated H4-species, was found to be identical in hepatomas and normal liver. The histone protein and acetate labeling patterns were near normal in the slowly growing hepatomas.
Authors:
H H Grunicke; Y Yamada; Y Natsumeda; W Helliger; B Puschendorf; G Weber
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cancer research and clinical oncology     Volume:  115     ISSN:  0171-5216     ISO Abbreviation:  J. Cancer Res. Clin. Oncol.     Publication Date:  1989  
Date Detail:
Created Date:  1989-11-27     Completed Date:  1989-11-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7902060     Medline TA:  J Cancer Res Clin Oncol     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  435-8     Citation Subset:  IM    
Affiliation:
Institute for Medical Chemistry and Biochemistry, University of Innsbruck, Austria.
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MeSH Terms
Descriptor/Qualifier:
Acetylation
Acetyltransferases / analysis*
Animals
Histone Acetyltransferases
Histones / analysis,  metabolism
Liver / enzymology
Liver Neoplasms, Experimental / enzymology*
Rats
Rats, Inbred ACI
Rats, Inbred BUF
Saccharomyces cerevisiae Proteins*
Grant Support
ID/Acronym/Agency:
CA-13526/CA/NCI NIH HHS; CA-42510/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Histones; 0/Saccharomyces cerevisiae Proteins; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.48/Histone Acetyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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