Abstract:
:Regulation of phospholipase D (PLD) activation by protein kinase C (PKC) was studied in membranes isolated from human promyelocytic leukemia HL60 cells. The activation of membrane-bound PLD by PKC partially purified from rat brain was most effectively induced with phorbol 12-myristate 13-acetate (PMA) and Ca2+ (1 microM) which caused translocation of PKC to membranes. Ro31-8425, a potent inhibitor of PKC, suppressed the catalytic activity of PKC in a concentration-dependent manner, with complete inhibition at 5 microM. However, the PKC-mediated PLD activation was not affected by Ro31-8425. It was thus suggested that membrane-bound PLD of HL60 cells was activated by PKC translocation but probably via a phosphorylation-independent mechanism. Furthermore, addition by guanosine 5'-3-O-(thio)trisphosphate (GTP gamma S) potentiated the PKC-mediated PLD activation and this potentiating effect was abolished by Rho GTPase dissociation inhibitor (RhoGDI). The suppressed PLD activation by RhoGDI was completely restored by addition of recombinant RhoA. These results indicate that the PKC-mediated PLD activation can be synergistically potentiated by RhoA in HL60 membranes.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ohguchi K,Banno Y,Nakashima S,Nozawa Ydoi
10.1006/bbrc.1995.1811subject
Has Abstractpub_date
1995-06-06 00:00:00pages
306-11issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(85)71811-6journal_volume
211pub_type
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