Properties of phospholipase C-β-mediated signaling in H9c2 cardiac myoblasts Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0c483q293

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  • The mechanisms by which the activities of phospholipase C-β (PLC-β) enzymes arenegatively regulated have not been well defined. We used cardiac-derived ratmyoblast H9c2 cells to investigate possible modes of regulation of PLC-β3 enzymes
  • The mechanisms by which the activities of phospholipase C-β (PLC-β) enzymes arenegatively regulated have not been well defined. We used cardiac-derived ratmyoblast H9c2 cells to investigate possible modes of regulation of PLC-β3 enzymes,the only endogenous β isoform abundantly found in these cells. The PLC-β3population in these cells was detected almost exclusively associated with membranewith only trace amounts being cytosolic. H9c2 cells responded to vasopressinstimulation through the PLC-β pathway in a concentration-dependent manner. Directactivation of endogenous protein kinase C (PKC) by phorbol 12-myristate 13-acetate(PMA) significantly diminished vasopressin effects on PLC-β3-mediated PIhydrolysis. However, phosphorylation of PLC-β3 at the Ser1105 residue, the widelyrecognized primary phosphorylation site on PLC-β3, was not observed upon PKCactivation. Other possible mechanisms by which the agonist-stimulated PLC-β3activity is modulated were also tested. Short-term or prolonged stimulation of thesecells with either vasopressin or stimulation of PKC by PMA did not promotetranslocation or down-regulation of the PLC-β3 population within the time frametested. Our observations imply that in H9c2 cells, activated PLC-β3 enzymes may benegatively regulated utilizing some other molecular mechanism not tested in thisstudy.
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