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dc.creatorIlić, Vesna
dc.creatorMilošević-Jovčić, Nadežda
dc.creatorPetrović, Sonja
dc.creatorMarković, Dragana
dc.creatorStefanović, Gordana
dc.creatorRistić, Tatjana
dc.date.accessioned2021-04-20T12:14:53Z
dc.date.available2021-04-20T12:14:53Z
dc.date.issued2008
dc.identifier.issn0282-0080
dc.identifier.urihttp://rimi.imi.bg.ac.rs/handle/123456789/201
dc.description.abstractLittle is known about the glycosylation of the isotype switched B cell receptor (BCR) in multiple myeloma, and the way it might affect receptor function. In this work IgG BCRs isolated from the individual lysates of peripheral blood lymphocytes (PBL) of 32 patients with IgG multiple myeloma and healthy controls were investigated for the expression of sialic acid (SA), galactose (Gal) and N-acetylglucosamine (GlcNAc), the sugars known to specify the glycoforms of human serum IgG. The degree of glycosylation and signaling status of all 32 isolated myeloma IgG BCRs were correlated and compared with the glycosylation of the IgG paraproteins isolated from sera of the same patients. It was shown that BCR IgG in myeloma is more heavily sialylated when compared with normal controls, that the increased sialylation of IgG BCR is associated with higher levels of tyrosine phosphorylation (signaling activity) of the IgG BCR supramolecular complex and that BCR IgG and serum IgG paraprotein from the same patient differed in all cases in the levels of terminal sugar expression. The results suggest that the development of the malignant clone in MM from post-switch B cells expressing IgG BCR at their surfaces to plasma cells secreting IgG paraprotein may be followed by permanent glycosylation changes in the IgG molecules.en
dc.publisherSpringer, Dordrecht
dc.rightsrestrictedAccess
dc.sourceGlycoconjugate Journal
dc.subjectmultiple myelomaen
dc.subjectIgG BCRen
dc.subjectsignaling activityen
dc.subjectglycosylationen
dc.titleGlycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCRen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage392
dc.citation.issue4
dc.citation.other25(4): 383-392
dc.citation.rankM23
dc.citation.spage383
dc.citation.volume25
dc.identifier.doi10.1007/s10719-007-9101-9
dc.identifier.pmid18188696
dc.identifier.scopus2-s2.0-41149114122
dc.identifier.wos000254302800009
dc.type.versionpublishedVersion


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