NDLI: A mutant alpha subunit of G12 potentiates the eicosanoid pathway and is highly oncogenic in NIH 3T3 cells.

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A mutant alpha subunit of G12 potentiates the eicosanoid pathway and is highly oncogenic in NIH 3T3 cells.

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A mutant alpha subunit of G12 potentiates the eicosanoid pathway and is highly oncogenic in NIH 3T3 cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bradley, L. Gutkind, J. S. Xu, N. Ambdukar, I.
Description	Author Affiliation: Xu N ( Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.);
Abstract	The discovery of GTPase-inhibiting mutations in genes for alpha subunits of Gs or G(i2) in certain human endocrine tumors has raised the possibility that heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) might contribute to neoplastic disease. Expression of GTPase-deficient alpha s or alpha i2 polypeptides in rodent fibroblasts increases or decreases cAMP, respectively, and induces certain alterations in cell growth but only a few of the phenotypic changes associated with cellular transformation. In contrast, an analogous mutation in the alpha subunit of Gq, which activates phosphatidylinositol (PI)-specific phospholipase C, is fully oncogenic. However, activated alpha q is cytotoxic and several orders of magnitude less potent as an oncogene than certain G protein-coupled receptors. Thus, G proteins other than those inducing PI hydrolysis might possess high transforming efficiency. In the present study, we explored the G12 family of G proteins for their oncogenic potential. Our results show that whereas overexpression of wild-type alpha 12 in NIH 3T3 cells is itself weakly transforming, an activated alpha 12 behaves as a remarkably potent oncogene. Transformation by alpha 12 correlates with alterations in the eicosanoid pathway but not with PI-specific phospholipase C or other G protein-linked second messengers.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Transformation, Neoplastic Genetics Eicosanoids Metabolism GTP-Binding Proteins Multigene Family Oncogenes 3T3 Cells Amino Acid Sequence Animals Cell Division Cyclic AMP Enzyme Activation Classification Inositol Phosphates Mice Mice, Nude Molecular Sequence Data Mutation Neoplasms, Experimental Second Messenger Systems Transfection Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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