The zinc chelator 1 , 10 - phenanthroline enhances the stimulatory effects of protein kinase C activators and staurosporine , but not sphingosine and H 202 , on phospholipase D activity in NIH 3 T 3 fibroblasts
نویسنده
چکیده
or inhibit, respectively, the stimulatory effects of PMA on PLD-mediated phospholipid hydrolysis. Instead, treatment of ['4C]cholineand [14C]ethanolamine-labelled NIH 3T3 fibroblasts with the high-affinity zinc chelator 1,10-phenanthroline (0.21 mM) for 20-30 min was found to enhance the stimulatory effects of PMA on PLD-mediated hydrolysis of phosphatidylcholine and phosphatidylethanolamine. In [14C]palmitic acidlabelled fibroblasts, in the presence of ethanol, phenanthroline
منابع مشابه
Regulation of phospholipase D by sphingosine involves both protein kinase C-dependent and -independent mechanisms in NIH 3T3 fibroblasts.
Previously, the protein kinase C (PKC) inhibitor sphingosine was found to stimulate phospholipase D (PLD)-mediated hydrolysis of both phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) in NIH 3T3 fibroblasts [Kiss & Anderson (1990) J. Biol. Chem. 265, 7345-7350]. Here we examined the possible relationship between the opposite effects of sphingosine on PKC-mediated protein phosph...
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Recently, phospholipase D-mediated hydrolysis of phosphatidylethanolamine (PtdEtn) was shown to be stimulated by activators of protein kinase C (Kiss, Z., and Anderson, W. B. (1989) J. Biol. Chem. 264, 1483-1487), suggesting that PtdEtn metabolism may play a role in signal transduction. Here we have studied the possible regulation of PtdEtn hydrolysis by adenine and guanine nucleotides, as well...
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Recently, phospholipase D-mediated hydrolysis of phosphatidylethanolamine (PtdEtn) was shown to be stimulated by activators of protein kinase C (Kiss, Z., and Anderson, W. B. (1989) J. Biol. Chem. 264,14831487), suggesting that PtdEtn metabolism may play a role in signal transduction. Here we have studied the possible regulation of PtdEtn hydrolysis by adenine and guanine nucleotides, as well a...
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