Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion

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 adh...

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Autor principal:	Osamu Suzuki
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Galectins B cell receptor CD45 B cell lymphoma Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
Acceso en línea:	https://doaj.org/article/b5bd191c4801490fb73c61fd60c2c0ad
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spelling	oai:doaj.org-article:b5bd191c4801490fb73c61fd60c2c0ad2021-11-14T04:36:16ZRegulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion2667-394010.1016/j.adcanc.2021.100016https://doaj.org/article/b5bd191c4801490fb73c61fd60c2c0ad2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2667394021000162https://doaj.org/toc/2667-3940To 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.Osamu SuzukiElsevierarticleGalectinsB cell receptorCD45B cell lymphomaNeoplasms. Tumors. Oncology. Including cancer and carcinogensRC254-282ENAdvances in Cancer Biology - Metastasis, Vol 3, Iss , Pp 100016- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Galectins B cell receptor CD45 B cell lymphoma Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
spellingShingle	Galectins B cell receptor CD45 B cell lymphoma Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282 Osamu Suzuki Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
description	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.
format	article
author	Osamu Suzuki
author_facet	Osamu Suzuki
author_sort	Osamu Suzuki
title	Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
title_short	Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
title_full	Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
title_fullStr	Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
title_full_unstemmed	Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion
title_sort	regulation of cell adhesion to galectins by glycosylation: a new concept in lymphoma cell adhesion
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/b5bd191c4801490fb73c61fd60c2c0ad
work_keys_str_mv	AT osamusuzuki regulationofcelladhesiontogalectinsbyglycosylationanewconceptinlymphomacelladhesion
_version_	1718429918307549184

Regulation of cell adhesion to galectins by glycosylation: A new concept in lymphoma cell adhesion

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