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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1989-6-1
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pubmed:abstractText |
Quantitation of D-beta-hydroxybutyrate dehydrogenase (BDH) in normal rat hepatocytes was compared with that in two rat hepatoma cell lines, H4-II-EC3 and RLT-3C. BDH activity in normal rat hepatocyte mitochondria was 321 nmol/min/mg, which was greatly reduced to 10.7 nmol/min/mg and 1.7 nmol/min/mg in H4-II-EC3 and RLT-3C cell mitochondria, respectively. The cell growth rate and L-[35S]methionine incorporation rate showed that RLT-3C cells had the highest growth rate (32.4-h doubling time) and the fastest protein biosynthesis rate (2.65 x 10(5) cpm/min/10(6) cells). The H4-II-EC3 cell line grew more slowly (48.5-h doubling time) and had lower protein biosynthesis rate (1.46 x 10(5) cpm/min/10(6) cells). The protein synthesis rate in hepatocytes was 1.25 x 10(5) cpm/min/10(6) cells. These results suggest that there is a reciprocal correlation between BDH activity and cell growth and protein synthesis rates. Immunochemical quantitation of BDH showed the amount of BDH in H4-II-EC3 and RLT-3C cells was about 4.8 and 0.5% of that in normal rat hepatocytes, respectively. Quantitation of BDH by biosynthesis indicated that BDH content in H4-II-EC3 cells and RLT-3C cells was 9.3 and 4.0% of that of normal hepatocytes, respectively. Precursor BDH synthesized by in vitro translation primed with RNA of H4-II-EC3 cells or RLT-3C cells was 3.0 and 1.1% of that translated from normal rat hepatocyte RNA. These results suggest that the decrease in BDH content in hepatoma cells results from a decrease in functional BDH-mRNA. The coupling of a decrease in BDH activity with an increase in activity of succinyl-CoA: acetoacetyl-CoA transferase in hepatoma cells may play a role in generating additional energy required for the rapid growth of tumor cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0008-5472
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2433-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2706630-Animals,
pubmed-meshheading:2706630-Cell Division,
pubmed-meshheading:2706630-Coenzyme A-Transferases,
pubmed-meshheading:2706630-Hydroxybutyrate Dehydrogenase,
pubmed-meshheading:2706630-Liver Neoplasms, Experimental,
pubmed-meshheading:2706630-Mitochondria, Liver,
pubmed-meshheading:2706630-Neoplasm Proteins,
pubmed-meshheading:2706630-Protein Biosynthesis,
pubmed-meshheading:2706630-RNA, Messenger,
pubmed-meshheading:2706630-Rats,
pubmed-meshheading:2706630-Rats, Inbred Strains,
pubmed-meshheading:2706630-Tumor Cells, Cultured
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pubmed:year |
1989
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pubmed:articleTitle |
Regulation of D-beta-hydroxybutyrate dehydrogenase in rat hepatoma cell lines.
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pubmed:affiliation |
Department of Biology, University of Alabama, Tuscaloosa 35487-0344.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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