Open AccessNew pathways of phagocyte activation: the coupling of receptor‐linked phospholipase D and the role of tyrosine kinase in primed neutrophils
Author(s) -
Garland Lawrence G.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05907.x
Subject(s) - second messenger system , phosphatidic acid , phospholipase d , diacylglycerol kinase , microbiology and biotechnology , phosphoinositide phospholipase c , protein kinase c , phospholipase c , biology , pld2 , signal transduction , tyrosine kinase , tyrosine phosphorylation , receptor tyrosine kinase , biochemistry , phospholipid , membrane
Protein kinase C (PKC) appears to have a central role in the O 2 − response of neutrophils following stimulation of membrane receptors. The second messenger, diacylglycerol (DG), that activates PKC is derived from membrane phospholipids via activation of phosphatidylinositol 4,5‐bisphosphate (PIP 2 )‐phospholipase C (PLC) and phospholipase D (PLD), with the latter pathway being more prominent in primed cells. In resting cells receptor coupling of PLD is through a G‐protein. Priming brings a cytoplasmic tyrosine kinase into the transducer sequence which, through protein phosphorylation, increases the efficiency of coupling between membrane receptors and PLD. Phosphatidic acid (PA), the initial product of the PLD pathway, also appears to act as a second messenger by directly activating the NADPH oxidase responsible for generating O 2 − . Interconversion of PA and DG by phosphatidate phosphohydrolase and DG kinase determines which of these second messengers has the dominant role.