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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
40
|
| pubmed:dateCreated |
1998-11-12
|
| pubmed:abstractText |
In most hepatoma cells, the high-Km GLUT2/glucokinase proteins are replaced by the ubiquitous low-Km GLUT1/hexokinase type I proteins. In the mhAT3F hepatoma cells, the stimulatory effect of glucose on gene expression and glycogen accumulation was not maximal at 5 mmol/liter glucose. This response to high glucose is observed in mhAT3F cells, where GLUT2 was expressed, but not glucokinase (assessed by Northern blotting and reverse transcription-polymerase chain reaction). A low-Km hexokinase activity (19.6 +/- 3.8 milliunits/mg of protein) was present, but a high-Km (40 mmol/liter) hexokinase activity (13.9 +/- 2.5 milliunits/mg) was also detected in mhAT3F cells. The high-Km hexokinase activity was dependent on both ATP (or PPi) and glucose in the assay and was recovered in a 10-50-kDa fraction after filtration. A 30-kDa protein was detected using an anti-glucokinase antibody and localized by confocal microscopy at the same sites as glucokinase in hepatocytes. In FAO cells, the high-Km hexokinase activity and 30-kDa protein were not found. We conclude that a high-Km hexokinase activity is present in mhAT3F cells. This might explain why the effects of glucose on gene expression were not maximal at a glucose concentration of 5 mmol/liter. A 30-kDa protein identified using an anti-glucokinase antibody may be responsible for this activity present in mhAT3F cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
26187-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9748301-Adenosine Triphosphate,
pubmed-meshheading:9748301-Animals,
pubmed-meshheading:9748301-Carcinoma, Hepatocellular,
pubmed-meshheading:9748301-Female,
pubmed-meshheading:9748301-Gene Expression Regulation,
pubmed-meshheading:9748301-Glucose,
pubmed-meshheading:9748301-Glucose Transporter Type 2,
pubmed-meshheading:9748301-Hexokinase,
pubmed-meshheading:9748301-Immunohistochemistry,
pubmed-meshheading:9748301-Kinetics,
pubmed-meshheading:9748301-Mice,
pubmed-meshheading:9748301-Microscopy, Fluorescence,
pubmed-meshheading:9748301-Monosaccharide Transport Proteins,
pubmed-meshheading:9748301-Nucleotides,
pubmed-meshheading:9748301-RNA, Messenger,
pubmed-meshheading:9748301-Rats,
pubmed-meshheading:9748301-Rats, Wistar,
pubmed-meshheading:9748301-Tumor Cells, Cultured
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
An unusual high-Km hexokinase is expressed in the mhAT3F hepatoma cell line.
|
| pubmed:affiliation |
Endocrinologie Métabolisme et Développement, CNRS UPR1524, 9, rue Jules Hetzel, 92190 Meudon Bellevue, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|