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Publication : Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties.

First Author  Sánchez-Martínez C Year  2000
Journal  Biochem Biophys Res Commun Volume  271
Issue  3 Pages  635-40
PubMed ID  10814514 Mgi Jnum  J:64909
Mgi Id  MGI:1890113 Doi  10.1006/bbrc.2000.2681
Citation  Sanchez-Martinez C, et al. (2000) Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties. Biochem Biophys Res Commun 271(3):635-40
abstractText  The phosphofructokinase C isozyme (PFK-C) from ascites tumor cells has been cloned and characterized to investigate the particular properties of PFK activity in this type of cells. The isolated cDNA encodes a protein of 784 amino acids and 85.5 kDa, whose expression was constant along tumor growth and markedly decreased when cell proliferation stops. The enzyme was functionally expressed in a PFK-deficient strain of Saccharomyces cerevisiae and purified to homogeneity. Recombinant PFK-C exhibited the same subunit size as the tumor wild-type isozyme and its steady-state kinetic parameters were similar to those of the form present in normal cells. The regulatory properties of the C isozyme accounted for the lack of fructose-1,6-P(2) activation and the P-enolpyruvate inhibition of PFK activity observed in ascites tumor preparations containing the various isozyme types. Nevertheless, PFK-C binds fructose-1,6-P(2) to an allosteric site as suggested by protection against thermal denaturation. Our results indicate that glucose metabolism in tumor cells is not regulated by a mutant form of PFK-C but by a high level expression of the normal C isozyme. Copyright 2000 Academic Press.
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