E. Rezaei et al., A NOVEL INHIBITORY-ACTION OF WHEAT-GERM-AGGLUTININ ON PHOSPHOLIPASE-CIN HEL AND MEG-O1 CELL-LINES, Biochimica et biophysica acta. Molecular cell research, 1356(1), 1997, pp. 101-110
Stimulation of HEL megakaryocytic cells by Fc gamma RIIA crosslinking
is associated with tyrosine phosphorylation of syk and phospholipase C
gamma 2(PLC gamma 2) and is accompanied by formation of inositol phos
phates and release of intracellular Ca2+ These responses are inhibited
by the kinase inhibitors, staurosporine and ST271. In contrast, the G
-protein receptor agonist, thrombin induces formation of inositol phos
phates and release of intracellular calcium without an increase in tyr
osine phosphorylation. The plant lectin wheat germ agglutinin (WGA) st
imulates tyrosine phosphorylation of syk and PLC gamma 2 but surprisin
gly does not stimulate formation of inositol phosphates and induce rel
ease of intracellular Ca2+. WGA also inhibited formation of inositol p
hosphates and release of intracellular Ca2+ by Fc gamma RIIA crosslink
ing and thrombin-stimulation. A similar inhibitory effect of WGA was o
bserved against elevation of Ca2+ by the same two stimuli in MEG-01 me
gakaryotic cells. The results demonstrate a novel pathway of inhibitio
n of PLC on crosslinking of cell surface proteins that is not present
in platelets.