Fluoroaluminates mimic guanosine 5′-[γ-thio]triphosphate in activating the polyphosphoinositide phosphodiesterase of hepatocyte membranes. Role for the guanine nucleotide regulatory protein Gp in signal transduction

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Abstract
Fluoride and guanosine 5''-[.gamma.-thio]triphosphate (GTP.gamma.S) both activate the hepatocyte membrane poly-phosphoinositide phosphodiesterase (PPI-pde) in a concentration-dependent manner. AlCl2 enhances the fluoride effect, supporting the concept that [AlF4]- is the active species. Analysis of the products of inositol lipid hydrolysis demonstrate that phosphatidylinositol bisphosphate is the major lipid to be hydrolysed. Guanosine 5''-[.beta.-thio]diphosphate (GDP.beta.S) is an inhibitor of activation of PPI-pde both fluoride and GTP.gamma.S. These observations suggest that the guanine nucleotide regulatory protein (termed Gp) bears a structural resemblance to the well-characterized G-proteins of the adenylate cyclase system and the cyclic GMP phosphodiesterase system in phototransduction.

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