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A novel inhibitory action of wheat germ agglutinin on phospholipase C in HEL and MEG-01 cell lines

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
0167-4889
Publisher
Elsevier
Publication Date
Volume
1356
Issue
1
Identifiers
DOI: 10.1016/s0167-4889(96)00160-7
Keywords
  • Phospholipase C
  • Wheat Germ Agglutinin
  • Megakaryotic Cell
  • (Human)
Disciplines
  • Biology

Abstract

Abstract Stimulation of HEL megakaryocytic cells by Fc γRIIA crosslinking is associated with tyrosine phosphorylation of syk and phospholipase C γ2 (PLC γ2) and is accompanied by formation of inositol phosphates and release of intracellular Ca 2+. These responses are inhibited by the kinase inhibitors, staurosporine and ST271. In contrast, the G-protein receptor agonist, thrombin induces formation of inositol phosphates and release of intracellular calcium without an increase in tyrosine phosphorylation. The plant lectin wheat germ agglutinin (WGA) stimulates tyrosine phosphorylation of syk and PLC γ2 but surprisingly does not stimulate formation of inositol phosphates and induce release of intracellular Ca 2+. WGA also inhibited formation of inositol phosphates and release of intracellular Ca 2+ by Fc γRIIA crosslinking and thrombin-stimulation. A similar inhibitory effect of WGA was observed against elevation of Ca 2+ by the same two stimuli in MEG-01 megakaryotic cells. The results demonstrate a novel pathway of inhibition of PLC on crosslinking of cell surface proteins that is not present in platelets.

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