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BPNT1 — PLD5
Text-mined interactions from Literome
Huang et al., Mol Cell Biochem 1999
(Carcinoma, Hepatocellular) :
It was found that
phospholipase D was marginally
activated by
phosphatidyl-4-phosphate (PIP) and phosphatidylethanolamine ( PE ) ... The
activation of
phospholipase D by
PIP2 was dose dependent up to 50 microM of PIP2
Kurz et al., J Mol Cell Cardiol 2004
:
The addition of PIP2 restored the sensitivity of solubilized PLD to neomycin inhibition, indicating that neomycin
inhibits PLD activity by binding to endogenous
PIP2 ... Our results demonstrate a critical
role for
PIP2 in human cardiac
PLD activity and suggest that PIP2 synthesis ( by phosphatidylinositol 4-phosphate 5-kinase ) and hydrolysis ( by PIP2-specific PLC ) could be important determinants in regulating PLD signal transduction in the human heart
Ohguchi et al., J Biol Chem 1996
:
The PKC mediated
PLD activation was completely inhibited by neomycin, a high affinity ligand for PIP2, and this suppression was
recovered by the addition of exogenous
PIP2
Mayr et al., FEBS Lett 1996
:
In contrast, the Ca ( 2+ ) -dependent
PLD described here is not
affected by
PIP2 and does not catalyze transphosphatidylation
Liscovitch et al., J Lipid Mediat Cell Signal 1996
:
Neomycin, a high affinity ligand of
PIP2 ,
inhibits membrane
PLD activity, presumably by binding to endogenous PIP2