Cell surface glycosylation diversity of embryonic thymic tissues

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dc.contributor.authorBalcan E.
dc.contributor.authorTuǧlu I.
dc.contributor.authorŞahin M.
dc.contributor.authorToparlak P.
dc.date.accessioned2024-07-22T08:22:35Z
dc.date.available2024-07-22T08:22:35Z
dc.date.issued2008
dc.description.abstractIn the thymus, glycosylation status of many cell surface molecules changes during the thymocyte maturation and selection processes. In this study, we evaluated the glycosylation changes and possible relationships with programmed cell death in the thymic tissues from mouse embryos at the days 14 (E14), 15 (E15), 16 (E16), 17 (E17) and 18 (E18) of embryonic development. In order to determine glycosylation changes we used three different plant lectins: peanut agglutinin (PNA), Maackia amurensis leucoagglutinin (MAL or MAAI) and Sambucus nigra agglutinin (SNA), which recognize core disaccharide galactose (1-3) N-acetylgalactosamine [Galβ(1→3)GalNAc], sialic acid linked (2→3) to galactose [SAα(2→3)Gal] and sialic acid linked to galactose [SAα(2→6)Gal] structures, respectively. Our lectin histochemistry and lectin blotting studies indicated that glycosylation pattern was modified in thymocytes at the embryonic developmental stages analyzed. The immature cortical thymocytes were labeled by PNA, whereas medullary thymocytes were positive for MAL and SNA binding. Many medullary thymocytes exhibited α(2→6)-linked sialic acid on their surface and this increased throughout the gestational stages. In the lectin blotting studies, different protein bands of various molecular weights were identified in thymocytes. Two of them were putatively identified as CD43 and CD45 glycoproteins. In addition, TUNEL (deoxynucleotdyltransferase-mediated dUDP nick end labeling) indicated that only PNA-positive cortical thymocytes were deleted in all embryonic stages. These results indicate that the glycosylation pattern was modified in thymocytes at all embryonic developmental stages, and these modifications can affect the T cell deletion, probably via the galectin-1 molecule in the embryonic thymus. © 2007 Elsevier GmbH. All rights reserved.
dc.identifier.DOI-ID10.1016/j.acthis.2007.07.003
dc.identifier.issn00651281
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/19154
dc.language.isoEnglish
dc.publisherElsevier GmbH
dc.subjectArachis hypogaea
dc.subjectMaackia amurensis
dc.subjectMus
dc.subjectSambucus nigra
dc.subjectCD45 antigen
dc.subjectdisaccharide
dc.subjectgalactose
dc.subjectgalectin 1
dc.subjectglycoprotein
dc.subjectleukoagglutinin
dc.subjectleukosialin
dc.subjectn acetylgalactosamine
dc.subjectpeanut agglutinin
dc.subjectplant lectin
dc.subjectsialic acid
dc.subjectanimal cell
dc.subjectanimal embryo
dc.subjectanimal tissue
dc.subjectapoptosis
dc.subjectarticle
dc.subjectcarbohydrate analysis
dc.subjectcell surface
dc.subjectdevelopmental stage
dc.subjectembryo
dc.subjectembryo development
dc.subjectembryonal tissue
dc.subjectfemale
dc.subjecthigher plant
dc.subjecthistochemistry
dc.subjecthuman
dc.subjectimmunoblotting
dc.subjectMaackia amurensis
dc.subjectmale
dc.subjectmolecular weight
dc.subjectmouse
dc.subjectnewborn
dc.subjectnick end labeling
dc.subjectnonhuman
dc.subjectprotein analysis
dc.subjectprotein glycosylation
dc.subjectprotein modification
dc.subjectSambucus nigra
dc.subjectT cell depletion
dc.subjectthymus
dc.titleCell surface glycosylation diversity of embryonic thymic tissues
dc.typeArticle

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