Advances in Cancer Biology - Metastasis (Dec 2021)
Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
Abstract
To investigate the biological roles of glycosylation in human lymphoma cell adhesion to galectins, I performed the cell adhesion assay using neuraminidase or glycosylation inhibitors on B cell lymphoma cell line. I show that desialylation by neuraminidase treatment results in enhancement of cell adhesion to Phaseolus vulgaris leukoagglutinating lectin (L-PHA), suggesting that neuraminidase treatment removes sialic acids from N-glycans, which we have shown react to L-PHA in a lymphoma cell line. Neuraminidase treatment resulted in enhancement of cell adhesion to galectin-3, an effect that was especially pronounced following pre-stimulation of B cell receptors (BCR) by anti-IgM antibody treatment. This suggests that sialic acid may be a candidate regulator of interactions between glycans on BCR and galectins. From treatment with tunicamycin (TM), a potent inhibitor of N-glycosylation, cell adhesion capacity decreased. Furthermore, it is suggested that IgM and CD45 have N-glycans for binding to galectins in western blot analysis. In a glycoengineering approach, I found that treatment with the sialic acid mimetic analogue 3Fax-peracetyl Neu5Ac, which is a potent inhibitor of sialyltransferases, markedly enhanced lymphoma cell adhesion to galectin-3. In conclusion, sialic acids and N-glycosylation appeared to influence lymphoma cell adhesion to galectins.
