Biochemical and Biophysical Research Communications
Regular ArticleWheat Germ Agglutinin-Induced Intracellular Calcium Mobilization in Human Platelets: Suppression by Staurosporine and Resistance to Cyclic AMP Inhibition
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Structure-function and application of plant lectins in disease biology and immunity
2019, Food and Chemical ToxicologyCitation Excerpt :Gong et al. have shown that Con A binds to LFA-1, that leads to the internalization of Con A and activates NLRP3 inflammasome through endoplasmic reticulum stress and subsequently leads to the release of proinflammatory cytokines like IL-1β and IL-18 (Gong et al., 2017). Con A and WGA are also reported to induce intracellular Ca2+ mobilization in different cell types that is hypothesized to be a mechanism of NLRP3 inflammasome activation (Grinstein et al., 1987; Yatomi et al., 1993). Dioclea violacea (Dvl), a lectin isolated from the Fabaceae family is reported to have anti-inflammatory properties whereby it inhibits neutrophil migration upon inflammation when injected intravenously (Nascimento et al., 2018; Freitas et al., 2015).
Lectin-induced Aggregates of Blood Cells from Patients with Acute Coronary Syndromes
2008, Archives of Medical ResearchCitation Excerpt :VAA has not been so far used to study changes of blood cells from patients with ACS, whereas the application of WGA and some other plant lectins as aggregants was reported recently (11). VAA and WGA, however, are not only able to induce cell aggregation but can also serve as potent stimuli of various signaling responses in cells including intracellular Ca2+ mobilization (29,30), generation of reactive oxygen species (30), upregulation of tyrosine and other protein kinases (31,32) as well as cytoskeleton perturbations (33,34). Most important is that all these lectin-induced changes may result in activation/expression of additional adhesion proteins on the cell surface allowing for stabilization of intracellular contacts and cell aggregates (12-17).
Plant lectins as carriers for oral drugs: Is wheat germ agglutinin a suitable candidate?
2005, Toxicology and Applied PharmacologycAMP does not inhibit convulxin-induced tyrosyl-phosphorylation of human platelet proteins, including PLCγ2, but completely blocks the integrin α(IIb)β<inf>3</inf>- dependent dephosphorylation step: Comparisons with RGDS peptide, cytochalasin D, and phenylarsine oxide
1998, Archives of Biochemistry and BiophysicsTyrosine phosphorylation of the Fc receptor γ-chain in collagen- stimulated platelets
1996, Journal of Biological Chemistry