Bradykinin-stimulated changes in inositol phosphate mass in renal papillary collecting tubule cells.
The effect of bradykinin on changes in the chemical levels of myo-inositol polyphosphates in renal papillary collecting tubules was investigated. Myo-inositol phosphate mass was determined by means of an enzymatic, fluorometric assay. Bradykinin induced increases in myo-inositol mono-, bis-, and trisphosphate which were both time and concentration dependent. Furthermore, the magnitude of the chemical levels of myo-inositol monophosphate formed were unlikely to be accounted for solely by the formation and degradation of myo-inositol trisphosphate. These observations are consistent with the concomitant hydrolysis of phosphatidylinositol and phosphatidylinositol bisphosphate. This study also confirms, in freshly isolated renal tubules, observations regarding bradykinin-induced phosphatidylinositol bisphosphate hydrolysis made previously in radiolabeled cultures.
D000818:Animals; D001920:Bradykinin / Q000494:pharmacology*; D066298:In Vitro Techniques; D015544:Inositol 1,4,5-Trisphosphate; D007295:Inositol Phosphates / Q000378:metabolism*; D007684:Kidney Tubules / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D011817:Rabbits; D013403:Sugar Phosphates / Q000378:metabolism*
D007295:Inositol Phosphates; D013403:Sugar Phosphates; D015544:Inositol 1,4,5-Trisphosphate; D001920:Bradykinin