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  1. Home
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Browsing by Subject "Galectins"

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    Characterization of ligands for galectins, natural galactoside-binding immunoglobulin G subfractions and sarcolectin and also of the expression of calcyclin in thyroid lesions
    (Murcia : F. Hernández, 2000) Nagy, N.; Decaestecker, C.; Dong, X.; Kaltner, H.; Schuring, M.P.; Rocman, P.; Danguy, A.; Gabius, H.J.; Kiss, R.; Salmon, I.
    The purpose of this study was to characterize ligands for galectins, natural galactoside-binding immunoglobulin G subfractions and sarcolectin and also the expression of calcyclin in various benign and malignant thyroid lesions. The extent of the binding of eight glycochemical probes was quantitatively assessed using computer-assisted microscopy on 76 thyroid lesions including 10 not-otherwise-specified multinodular goiters (S-MNG), 11 multinodular goiters with adenomatous hyperplasia (AH-MNG), 8 normomacrovesicular (NM-ADE) and 12 microvesicular (MIC-ADE) adenomas, and 9 papillary (P-CAR), 10 follicular variants of papillary (FvarP-CAR), 7 follicular (F-CAR) and 9 anaplastic (A-CAR) carcinomas. The 8 histochemical probes included 5 animal lectins (including galectins and sarcolectin), 1 polyclonal antibody (raised against calcyclin) and 2 immunoglobulin G subfractions from human serum with selectivity to a- and R-galactosyl residues. The results show that multinodular goiters with adenomatous hyperplasia exhibited histochemical characteristics intermediate to those of normal multinodular goiters and microvesicular adenomas. ~ormomacro~vesicular adenomas behaved very distinctly from microvesicular ones. ~ i c r o v e s i c u l aard enomas were more close1 y related to differentiated thyroid carcinomas than any other type of benign thyroid lesions of epithelia1 origin. Papillary and follicular carcinomas seemed to represent the two extremes of the same biological entity with the follicular variant of the papillary carcinoma serving as a biological link between these two extremes. Anaplastic carcinomas behaved in a significantly different manner Offprint requests to: Dr. Robert Kiss, Ph.D., Laboratoire d'Histopathologie, Faculte de Medecine, Un~versiteL ibre de Bruxelles, 808 route de Lennik, 1070 Brussels, Belgium. Fax: 322 555 62 85. e-mail: rkiss@med.ulb.ac.be when compared to the differentiated forms of thyroid carcinomas. The results suggest that the patterns of expression of the glycoconjugates investigated in the present study may constitute useful tools for characterizing lesions in the human thyroid.
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    Comparative analyses on expression of galectins1-4, 7-10 and 12 in first trimester placenta, decidua and isolated trophoblast cells in vitro
    (Universidad de Murcia. Departamento de Biología Celular e Histología, 2016) Unverdorben, Laura; Jeschke, Udo; Santoso, Laura; Hofmann, Simone; Kuhn, Christina; Arck, Petra; Hutter, Stefan
    Introduction: Galectins are members of the mammalian β-galactoside-binding proteins, which recognize Galβ1-4GlcNAc sequences of several cell surface oligosaccharides. Plenty of galectins are already described in human tissue, especially in placenta. Here, gal-1-4, 7-10 and gal-12 were investigated systematically in trophoblast and decidua cells of first trimester placentas. Material and methods: Within this study, 15 first trimester placentas after induced abortion (7th-14th week of gestation) were examined with immunohistology and immunofluorescence based on a scoring system. Moreover, isolated and cultivated trophoblast cells from the first trimester were analyzed and evaluated for expression of gal-1-4, gal-7-10 and gal-12 at mRNA and protein level with real-time RTPolymerase chain Reaction/PCR (Taq-Man). Double immunofluorescence with trophoblast specific markers identified galectin expressing cells at the feto-maternal interface. Results: We could detect immunohistochemical staining of galectins 1-4, 7-10 and 12 in first trimester placenta: all examined galectins were found in the cytotrophoblast (CTB) and syncytiotrophoblast (SCT). Gal-1, -2, -3, -4, -7, -8, -9, -10 and -12 were identified in extravillous trophoblast cells (EVT) in immunohistology and immunoflourescence. The expression of gal-1, -9, - 10, and gal-12 increased after 96h incubation in vitro without stimulation at mRNA level, while gal-2, -3, -4, -7 and -8 were decreased. Discussion and conclusion: This study describes a systematic analysis of the expression of gal-1-4, gal-7-10 and gal-12 in first trimester placentas and isolated trophoblast cells. Expression levels at mRNA level and the change within 96h cultivation in vitro indicate a possible influence on syncytium building of trophoblast cell on expression of galectins. Therefore, an interaction of galectins in vitro in syncytium building is possible.
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    Expression of galectin-l and -3 and of accessible binding sites during murine hair cycle
    (Murcia : F. Hernández, 2000) Wollina, U.; Lange, D.; Paus, R.; Burchert, M.; Gabius, H.J.
    Although protein-carbohydrate interactions are supposed to play key roles in cell adhesion, signalling and growth control. Their exact role in skin physiology has only recently been investigated. The endogenous lectins galectin-l and galectin-3 have been identified in skin including hair follicles. Here, we analyzed the expression and distribution of these galectins and their binding sites in C57BL/6 mice during hair cycle. The expression of galectin-l and galectin-3 binding sites was found to be predominantly hair cycledependent showing some overlapping to the expression of galectin-l and -3. The outer root sheath (ORS) expressed galectin-l binding sites during anagen IV to V1 and in early catagen, whereas galectin-l was expressed from early anagen to late catagen. The ORS expressed galectin-3 binding sites during catagen transition corresponding to a galectin-3 expression during anagen V and catagen. The innermost layer of the ORS expressed galectin-3 binding sites during anagen V1 until catagen VIII, but galectin-3 during anagen I11 to IV and catagen. The inner root sheath (IRS) expressed galectin-3 binding sites only in anagen IV but missed expression of any of the two galectins. The matrix cells expressed galectin-3 binding sites in catagen 11-111 as well as galectin-3 during anagen V to catagen IV. The present study provides the first evidence for a cyclerelated expression of both galectin-l and -3 and their binding sites during murine hair cycle.

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