Pressure effects on the GTPase activity of brain membrane G proteins of deep-living marine fishes

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In marine fishes, heterotrimeric guanyl nucleotide binding proteins (G proteins), which couple cell surface membrane receptors to their effector elements, are sensitive to hydrostatic pressure. The intrinsic high affinity GTPase activity of the alpha subunits of G proteins in three signaling systems coupled to adenylyl cyclase, the A(1) adenosine receptor, the muscarinic cholinergic receptor and the beta-adrenergic receptor, was tested at pressures up to 340 atm. Brain membrane preparations from four members of the deep-sea teleost fish family Macrouridae were studied. Coryphaenoides armatus, C. filifer, C. rupestris and Macrourus berglax have depth distributions which together span 100-5810 m. Increased pressure inhibited basal GTPase activity only in M. berglax, which of the four species has the shallowest center of abundance. Increased hydrostatic pressure did not alter the response of GTPase activity to the beta-adrenergic receptor agonist isoproterenol. Increased pressure decreased the stimulation of GTPase activity by the A(1) adenosine receptor agonist cyclopentyladenosine (CPA) in C. armatus and M. berglax, and by the muscarinic cholinergic receptor agonist carbamyl choline in C. armatus, C. filifer and M. berglax. Decreased agonist-stimulation of the GTPase activity at elevated pressure may result from pressure-induced changes in conformational states or inhibition of agonist binding. The binding of the non-hydrolyzable GTP analog guanosine 5'-[gamma-thio]triphosphate (GTP[S]) in response to CPA was determined at 5 degrees C and atmospheric pressure. Six macrourid species and a morid were studied. The halftime (t(1/2)) values for GTP[S] binding, ranging from 20.8 to 40.9 min, are similar to values previously reported for two other cold-adapted fishes.

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Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology

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