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J. Biol. Chem., Vol. 266, Issue 10, 6240-6245, Apr, 1991
J Gomez-Cambronero, E Wang, G Johnson, CK Huang and RI Sha'afi
The addition of platelet-activating factor (PAF) to human neutrophils
increases the levels of the tyrosine phosphorylation in several proteins.
These proteins have molecular weights of 41 (pp41), 54 (pp54), 66 (pp66),
104 (pp104), and 116 (pp116) kDa. The effect of PAF was dose-dependent and
could be seen at concentrations as low as 1 nM. The nonmetabolizable
bioactive PAF analog, C-PAF, caused an increase in the level of
phosphorylation of the same proteins in a time- and dose- dependent manner.
On the contrary, lyso-PAF, enantio-PAF, and L-
beta,gamma-dihexadecyl-alpha-lecithin failed to stimulate the
phosphorylation of any of the aforementioned proteins. The response to PAF
was prevented by the PAF antagonist BN-52021. The PAF-induced increases in
tyrosine phosphorylation in pp66, pp116, and pp104 were selectively
inhibited by pertussis toxin. In contrast, the level of pp41
phosphorylation remained unchanged after the pertussis toxin treatment. The
calcium chelator EGTA significantly inhibited the PAF- produced
phosphorylation of the pp41 protein. The intracellular calcium chelator
1,2-bis-(O-aminophenoxil)ethane-N,N,N',N'-tetraacetic acid (BAPTA)
potentiated the PAF-enhanced levels of tyrosine phosphorylation on the pp41
protein. On the other hand, the PAF-induced phosphorylations of pp66,
pp104, and pp116 were inhibited in BAPTA- treated cells. The calcium
ionophore A23187 selectively potentiated the phosphorylation of the pp41
protein and reduced the phosphorylation in the pp54 protein. This
phosphorylation was dependent on the extracellular calcium and was
inhibited in toxin-treated cells. The results suggest that PAF is able to
affect either directly or indirectly tyrosine kinase and/or phosphotyrosine
phosphatase activities. The phosphorylation of the high and low molecular
weight proteins are mediated by two different sets of kinases and/or
phosphatases.
Platelet-activating factor induces tyrosine phosphorylation in human neutrophils
Department of Pediatrics, University of Connecticut Health Center, Farmington 06032.
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