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Author

Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Inhibition of phospholipase D by a protein factor from bovine brain cytosol - Partial, purification and characterization of the inhibition mechanism

Cited 20 times inthomson ciCited 18 times inthomson ci
Title
Inhibition of phospholipase D by a protein factor from bovine brain cytosol - Partial, purification and characterization of the inhibition mechanism
Author
Kim, JHSuh, YJLee, TGKim, YBae, SSKim, MJLambeth, JDSuh, Pann-GhillRyu, SH
Keywords
ADP-RIBOSYLATION FACTOR; GTP-BINDING PROTEIN; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; GROWTH-FACTOR; D ACTIVATION; MEMBRANE; ARF; NEUTROPHILS; RHOA; GRANULOCYTES
Issue Date
199610
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.271, no.41, pp.25213 - 25219
Abstract
A specific protein inhibitor of partially purified bovine brain phospholipase D (PLD) was identified from bovine brain cytosol. The PLD inhibitor has been enriched through several chromatographic steps and characterized with respect to size and mechanism of inhibition. The inhibitor showed an apparent molecular mass of 30 kDa by Superose 12 gel exclusion chromatography and inhibited PLD activity with an IC50 of 7 nM. The inhibitor had neither proteolytic activity nor phospholipid-hydrolyzing activity. Because phosphatidylinositol 4,5-bisphosphate (PIP2), which is included in substrate vesicles, is an essential cofactor for PLD, we examined whether the inhibition might be mediated by sequestration of PIP2. PIP2 hydrolysis by phospholipase C (PLC)-β1 was not affected by the inhibitor and the inhibitor did not bind to substrate vesicles containing PIP2. In contrast, a PH domain derived from PLC-δ1, which could bind to PIP2, showed a nearly identical inhibition of both PLC-β1 and PLD activities. Thus, the PLD inhibition by the inhibitor is due to the specific interaction with not PIP2 but PLD. The suppression of PLD activity by the inhibitor was largely eliminated by the addition of ADP-ribosylation factor (ARF) and GTPγS. We propose that the inhibitor plays a negative role in regulation of PLD activity by PIP2 and ARF.
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DOI
http://dx.doi.org/10.1074/jbc.271.41.25213
ISSN
0021-9258
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