{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T20:55:35Z","timestamp":1771102535307,"version":"3.50.1"},"reference-count":42,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2019,7,17]],"date-time":"2019-07-17T00:00:00Z","timestamp":1563321600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Pathology International"],"published-print":{"date-parts":[[2019,8]]},"abstract":"<jats:p>Research using mouse lymphoma cell lines has resulted in many reports of glycosylation being a key regulator for the distant metastasis of mouse lymphoma cells in animal models. In contrast, there are only a few reports of experiments examining human lymphoma cell metastasis. The glycosylation pattern in human lymphoma shows that loss of <jats:italic>Phaseolus vulgaris<\/jats:italic> leukoagglutinating lectin (L\u2010PHA) reactive oligosaccharides, and sialylation of L\u2010PHA reactive oligosaccharides, are closely associated with a worse prognosis for diffuse large B cell lymphoma (DLBCL) patients. Sialic acid is related to cell adhesion to the extracellular matrix and metastasis of HBL\u20108 Burkitt lymphoma cells in a severe combined immunodeficiency (SCID) mouse animal model. In HBL\u20108 clones, differential cell surface sialylation was due to different expression levels of UDP\u2010GlcNAc 2\u2010epimerase (GNE). Knockdown of beta\u2010galactoside alpha\u20102,6\u2010sialyltransferase (ST6Gal1) resulted in enhanced lymphoma cell adhesion to galectin\u20101 in anaplastic large cell lymphoma cell line, H\u2010ALCL. A fluorinated sialic acid analogue was shown to be useful for inhibiting sialyltransferase and may provide a new glycoengineering strategy for desialylation, as well as inhibiting invasion and metastasis and inducing cell death in lymphoma cell lines. This paper discusses glycosylation and sialylation in human lymphoma, and several glycoengineering therapeutic strategies for lymphoma.<\/jats:p>","DOI":"10.1111\/pin.12834","type":"journal-article","created":{"date-parts":[[2019,7,18]],"date-time":"2019-07-18T05:23:05Z","timestamp":1563427385000},"page":"441-449","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Glycosylation in lymphoma: Biology and glycotherapy"],"prefix":"10.1111","volume":"69","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9195-7745","authenticated-orcid":false,"given":"Osamu","family":"Suzuki","sequence":"first","affiliation":[{"name":"Department of Diagnostic Pathology, School of Medicine Fukushima Medical University  Fukushima 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