Phospholipase D Regulation in Relationship with Several Protein Kinases Activation in Human Neutrophil

1995 ◽  
pp. 49-55
Author(s):  
Valérie Planat ◽  
Jean-Marc Lanau ◽  
Michel Record ◽  
Hugues Chap
Keyword(s):  
Protein Kinases ◽  
Phospholipase D ◽  
Human Neutrophil

scholarly journals Novel polyisoprenyl phosphates block phospholipase D and human neutrophil activation in vitro and murine peritoneal inflammation in vivo

2005 ◽  
Vol 146 (3) ◽  
pp. 344-351 ◽  
Author(s):  
Bruce D Levy ◽  
Lorraine Hickey ◽  
Andrew J Morris ◽  
Mykol Larvie ◽  
Raquel Keledjian ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil ◽  
Neutrophil Activation ◽  
Peritoneal Inflammation

Activation of human neutrophil phospholipase D by three separable mechanisms

1990 ◽  
Vol 4 (2) ◽  
pp. 208-214 ◽  
Author(s):  
Sandra L. Reinhold ◽  
Stephen M. Prescott ◽  
Guy A. Zimmerman ◽  
Thomas M. McIntyre
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil

scholarly journals The temporal relationship between phospholipase activation, diradylglycerol formation and superoxide production in the human neutrophil

1990 ◽  
Vol 271 (1) ◽  
pp. 209-213 ◽  
Author(s):  
N T Thompson ◽  
J E Tateson ◽  
R W Randall ◽  
G D Spacey ◽  
R W Bonser ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil ◽  
Second Messengers ◽  
Superoxide Production ◽  
Human Neutrophils ◽  
Inositol 1,4,5 Trisphosphate ◽  
Phosphatidate Phosphohydrolase ◽  
Time Courses ◽  
Rapid Activation ◽  
Stimulation Of

Fluctuations in the amounts of choline, inositol 1,4,5-trisphosphate (IP3) and diradylglycerol have been used to monitor phospholipase activation in the human neutrophil. Stimulation of human neutrophils by formylmethionyl-leucylphenylalanine (fMet-Leu-Phe) resulted in a rapid activation of both phosphatidylinositol 4,5-bisphosphate breakdown by phospholipase C and phosphatidylcholine breakdown by phospholipase D. Diradylglycerol accumulation occurred more slowly than that of either choline or IP3 and was inhibited by 30 mM-butanol, suggesting that the bulk was derived from the phospholipase D pathway via phosphatidate phosphohydrolase. Consistent with this is the observation that choline and diradylglycerol are produced in similar amounts. 1,2-Diacylglycerol (DAG) and 1-O-alkyl-2-acyl-sn-glycerol species accumulated with different time courses, indicating that one or more steps in the phospholipase D pathway was selective for the diacyl species. Superoxide production by fMet-Leu-Phe-stimulated neutrophils paralleled DAG accumulation over the first 5 min, but thereafter this production stopped, despite the fact that DAG remained elevated. We conclude that DAG derived from the phospholipase D pathway is only one of the second messengers important in controlling this functional response.

scholarly journals RhoA and a Cytosolic 50-kDa Factor Reconstitute GTPγS-dependent Phospholipase D Activity in Human Neutrophil Subcellular Fractions

1995 ◽  
Vol 270 (45) ◽  
pp. 27093-27098 ◽  
Author(s):  
Jong-Young Kwak ◽  
Isabel Lopez ◽  
David J. Uhlinger ◽  
Sung Ho Ryu ◽  
J. David Lambeth
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil ◽  
Subcellular Fractions

scholarly journals Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil

1992 ◽  
Vol 281 (3) ◽  
pp. 597-600 ◽  
Author(s):  
I J Uings ◽  
N T Thompson ◽  
R W Randall ◽  
G D Spacey ◽  
R W Bonser ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Phospholipase C ◽  
Tyrosine Phosphorylation ◽  
Phospholipase D ◽  
Human Neutrophil ◽  
Human Neutrophils ◽  
Receptor Coupling ◽  
Kinase C

The tyrosine kinase inhibitors ST271, ST638 and erbstatin inhibited phospholipase D (PLD) activity in human neutrophils stimulated by fMet-Leu-Phe, platelet-activating factor and leukotriene B4. These compounds did not inhibit phorbol ester-stimulated PLD, indicating that they do not inhibit PLD per se, but probably act at a site between the receptor and the phospholipase. In contrast, the protein kinase C inhibitor Ro-31-8220 inhibited phorbol 12,13-dibutyrate- but not fMet-Leu-Phe-stimulated PLD activity, arguing against the involvement of protein kinase C in the receptor-mediated activation of PLD. ST271 did not inhibit Ins(1,4,5)P3 generation, but did inhibit protein tyrosine phosphorylation stimulated by fMet-Leu-Phe. The phosphotyrosine phosphatase inhibitor pervanadate increased tyrosine phosphorylation and stimulated PLD. These results suggest that tyrosine kinase activity is involved in receptor coupling to PLD but not to PtdIns(4,5)P2-specific phospholipase C in the human neutrophil.

Regulation of Phospholipase D and Secretion in Mast Cells by Protein Kinase A and Other Protein Kinases

2002 ◽  
Vol 968 (1) ◽  
pp. 198-212 ◽  
Author(s):  
WAHN SOO CHOI ◽  
AHMED CHAHDI ◽  
YOUNG MI KIM ◽  
PAUL F. FRAUNDORFER ◽  
MICHAEL A. BEAVEN
Keyword(s):  
Mast Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Protein Kinases ◽  
Phospholipase D ◽  
Kinase A
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