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2008 | 13 | 4 |

Tytuł artykułu

The identification and characterization of a new GTP-binding protein [Gbp45] involved in cell proliferation and death related to mitochondrial function

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
We describe the identification and characterization of a GTP-binding protein with a molecular weight of 45 kD (Gbp45). Gbp45 cDNA was found to overlap with a hypothetical human protein, PTD004, the sequence of which was previously deposited in the databases. The gene for PTD004 was recently found to be one of the ATPases, hOLA1 (human Obg-like ATPase 1). The Gbp45 gene encodes a protein of 396 amino acid residues. Immunocytochemical analysis and examination with GFP-tagged protein revealed that Gbp45 is primarily located in the cytosolic compartment. Immunoblot analysis showed that the Gbp45 protein is strongly expressed in the neuronal tissues and pancreas. T43N and T56N mutations resulted in a loss of Gbp45’s ability to bind to GTP and a loss of GTPase activity. In cultured cells, the transfection of wild-type Gbp45 accelerated cell proliferation, though T43N and T56N mutations induced cell death. Down-regulating Gbp45 expression decreased the cell proliferation rate and increased the rate of cell death induced by the inhibition of mitochondrial electron transport. These findings indicate that Gbp45 plays important roles in cell proliferation and death related to mitochondrial function.

Wydawca

-

Rocznik

Tom

13

Numer

4

Opis fizyczny

p.570-584,fig.,ref.

Twórcy

autor
  • Osaka City University Medical School, Osaka 545-8585, Japan
autor

Bibliografia

  • 1.Takai, Y., Sasaki, T. and Matozaki, T. Small GTP-binding proteins. Physiol. Rev. 81 (2001) 153-208.
  • 2. Jaffe, A.B. and Hall, A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21 (2005) 247-269.
  • 3. Mathupala, S.P., Rempel, A. and Pedersen, P.L. Aberrant glycolytic metabolism of cancer cells: a remarkable coordination of genetic, transcriptional, post-translational, and mutational events that lead to a critical role for type II hexokinase. J. Bioenerg. Biomembr. 29 (1997) 339-343.
  • 4. Pedersen, P.L. Tumor mitochondria and the bioenergetics of cancer cells. Prog. Exp. Tumor Res. 22 (1978) 190-274.
  • 5. Weinhouse, S. Oxidative metabolism of neoplastic tissues. Adv. Cancer Res. 3 (1955) 269-325.
  • 6. Papa, S., Scacco, S., Schliebs, M., Trappe, J. and Seibel, P. Mitochondrial diseases and aging. Mol. Aspects Med. 17 (1996) 513-563.
  • 7. Sui, G., Soohoo, C., Affar el, B., Gay, F., Shi, Y., Forrester, W.C. and Shi, Y. A DNA vector-based RNAi technology to suppress gene expression in mammalian cells. Proc. Natl. Acad. Sci. USA 99 (2002) 5515-5520.
  • 8. Kikuchi, A., Yamashita, T., Kawata, M., Yamamoto, K., Ikeda, K., Tanimoto, T. and Takai, Y. Purification and characterization of a novel GTP-binding protein with a molecular weight of 24,000 from bovine brain membranes. J. Biol. Chem. 263 (1988) 2897-2904.
  • 9. Koller-Eichhorn, R., Marquardt, T., Gail, R., Wittinghofer, A., Kostrewa, D., Kutay, U. and Kambach, C. Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding proteins. J. Biol. Chem. 282 (2007) 19928-19937.
  • 10. Sikora-Borgula, A., Slominska, M., Trzonkowski, P., Zielke, R., Mysliwski, A., Wegrzyn, G. and Czyz, A. A role for the common GTP-binding protein in coupling of chromosome replication to cell growth and cell division. Biochem. Biophys. Res. Commun. 292 (2002) 333-338.
  • 11. Chance, B., Sies, H. and Boveris, A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605.
  • 12. Papa, S. and Skulachev, V.P. Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174 (1997) 305-319.

Typ dokumentu

Bibliografia

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bwmeta1.element.agro-article-294681aa-b234-4b08-8e36-19f4877d0499
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