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Volume 271, Number 47, Issue of November 22, 1996 pp. 30052-30060
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of a G-protein Activator in the Neuroblastoma-Glioma Cell Hybrid NG108-15

(Received for publication, May 25, 1996, and in revised form, September 11, 1996)

From the Department of Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425

Purified bovine brain G-protein was used in a solution phase assay to identify membrane-associated proteins that influenced the activation of heterotrimeric G-proteins. Detergent-solubilized membrane extracts from the neuroblastoma-glioma cell hybrid NG108-15, but not the parent C6B4 glioma cell line, increased [³⁵S]GTPS binding to purified G-protein by ~460%. The G-protein activator was heat-sensitive, and the magnitude of its action was related to the amount of extract protein. The biophysical and biochemical properties of the G-protein activator were determined using DEAE ion exchange chromatography, gel filtration, and a lectin affinity matrix. In the presence of added GDP (1 µM), the enriched G-protein activator increased the initial rate of [³⁵S]GTPS binding to brain G-protein by up to 4-fold. In the absence of added GDP, the G-protein activator elicited an initial burst in [³⁵S]GTPS binding to brain G-protein within the first 30 s, after which the rate of nucleotide binding to G-protein was similar in the absence or presence of the G-protein activator. The stimulation of nucleotide binding to brain G-protein by the activator was also observed after resolution of G from G. The G-protein activator was distinct from other proteins (neuromodulin, tubulin, and -amyloid precursor protein) that influence nucleotide binding to G-protein, indicating the existence of a novel signal accelerator.

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