Arachidonic acid activation of guinea pig lung guanylate cyclase by two independent mechanisms

D Y Gruetter, L J Ignarro


The purpose of this study was to elucidate the mechanisms by which arachidonic acid activates guanylate cyclase from guinea pig lung. Guanylate cyclase activities in both homogenate and soluble fractions of lung were examined. Guanylate cyclase activity was determined by measuring formtion of [32-P] cyclic GMP from alpha-[32-P] GTP in the presence of Mn2+, a phosphodiesterase inhibitor and a suitable GTP regenerating system. Arachidonic acid, and to a slight extent dihomo-gamma-linolenic acid, activated guanylate cyclase in homogenate but not soluble fractions. Similarly, phospholipase A2 activated homogenate but not soluble guanylate cyclase. Methyl arachidonate, linolenic, linoleic and oleic acids did not activate guanylate cyclase in either fraction. High concentrations of indomethacin, meclofenamate and aspirin inhibited activation of homogenate guanylate cyclase by arachidonic acid and phospholipase A2, without altering basal enzyme activity. These data suggested that a product of cyclooxygenase activity, present in the microsomal fraction, may have accounted for the capacity of arachidonic acid to activate homogenate guanylate cyclase. This view was supported by the findings that addition of the microsomal fraction to be ...Continue Reading


Nov 8, 1976·Biochemical and Biophysical Research Communications·T AsakawaR Ho
Sep 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·H Hidaka, T Asano
Oct 10, 1977·Biochemical and Biophysical Research Communications·T Asano, H Hidaka
Apr 30, 1971·Annals of the New York Academy of Sciences·W LandsW Smith

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