ArticleThe Biochemical journal1993
The hepatic glucose-6-phosphatase system in Ehrlich-ascites-tumour-bearing mice.
Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- The human embryonic-fetal kidney endoplasmic reticulum phosphate-pyrophosphate transport protein.Virchows Archiv : an international journal of pathology · 1996Article
- An altered T2 beta translocase of the glucose-6-phosphatase system in the membrane of the endoplasmic reticulum from livers of Ehrlich-ascites-tumour-bearing mice.The Biochemical journal · 1995Article
- Histone II-A stimulates glucose-6-phosphatase and reveals mannose-6-phosphatase activities without permeabilization of liver microsomes.The Biochemical journal · 1995Article
- Multiple transport protein defects in a patient with glycogen storage disease type 1: GSD 1b/1c beta.Journal of inherited metabolic disease · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To examine the effects of the presence of Ehrlich ascites tumours on both the catalytic unit and the substrate/product translocase components of the glucose-6-phosphatase system in vivo, we isolated microsomes from the livers of control and tumour-bearing mice. Samples were analysed immunochemically for the quantity of catalytic unit, stabilizing protein and translocases T2 and T3 proteins. In comparison experiments, a variety of kinetic studies were performed. The most striking findings in tumour-bearing mice were: a 2.5-fold increase in the quantity of translocase T2 protein; increases in the Km and Vmax. for glucose 6-phosphate phosphohydrolase; and a decrease in the Km value for carbamoyl phosphate (carbamoyl-P) of carbamoyl-P:glucose phosphotransferase, all with intact microsomes. The percentage latency at Vmax. decreased for PPi phosphohydrolase and for glucose 6-phosphate phosphohydrolase, but was unaffected for carbamoyl-P:glucose phosphotransferase. These observations support a tumour-related increase in translocase T2 capacity in vivo, as it transports Pi from the microsomal lumen to the medium and carbamoyl-P or PPi from the medium to the microsomal lumen.
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