Characterization of a new liver- and kidney-specific pfkfb3 isozyme that is downregulated by cell proliferation and dedifferentiation
- Unitat Bioquimica i Biologia Molecular, Departament de Ciencies Fisiologiques, Campus de Ciencies de la Salut, IDIBELL - Universitat de Barcelona (Spain)
- Laboratory of Epithelial Homeostasis and Cancer, Department of Differentiation and Cancer, Center for Genomic Regulation (Spain)
- Unitat de Biofisica, Departament de Ciencies Fisiologiques, Campus de Ciencies de la Salut, IDIBELL - Universitat de Barcelona (Spain)
The bifunctional enzyme 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK-2) catalyzes the synthesis and degradation of fructose 2,6-bisphosphate (Fru-2,6-P{sub 2}), a signalling molecule that controls the balance between glycolysis and gluconeogenesis in several cell types. Four genes, designated Pfkfb1-4, code several PFK-2 isozymes that differ in their kinetic properties, molecular masses, and regulation by protein kinases. In rat tissues, Pfkfb3 gene accounts for eight splice variants and two of them, ubiquitous and inducible PFK-2 isozymes, have been extensively studied and related to cell proliferation and tumour metabolism. Here, we characterize a new kidney- and liver-specific Pfkfb3 isozyme, a product of the RB2K3 splice variant, and demonstrate that its expression, in primary cultured hepatocytes, depends on hepatic cell proliferation and dedifferentiation. In parallel, our results provide further evidence that ubiquitous PFK-2 is a crucial isozyme in supporting growing and proliferant cell metabolism.
- OSTI ID:
- 21043664
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 367, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2008.01.005; PII: S0006-291X(08)00027-2; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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