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Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.

Carbohydrate moieties of cell glycoconjugates play a pivotal role in molecular recognition phenomena involved in the regulation of most biological systems and the changes observed in cell surface carbohydrates during cell activation or differentiation frequently modulate certain cell functions. Cons...

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Autores principales: Trabelsi, N, Greffard, A, Pairon, J C, Bignon, J, Zanetti, G, Fubini, B, Pilatte, Y
Formato: Texto
Lenguaje:English
Publicado: 1997
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470180/
https://www.ncbi.nlm.nih.gov/pubmed/9400716
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author Trabelsi, N
Greffard, A
Pairon, J C
Bignon, J
Zanetti, G
Fubini, B
Pilatte, Y
author_facet Trabelsi, N
Greffard, A
Pairon, J C
Bignon, J
Zanetti, G
Fubini, B
Pilatte, Y
author_sort Trabelsi, N
collection PubMed
description Carbohydrate moieties of cell glycoconjugates play a pivotal role in molecular recognition phenomena involved in the regulation of most biological systems and the changes observed in cell surface carbohydrates during cell activation or differentiation frequently modulate certain cell functions. Consequently, some aspects of macrophage response to particle exposure might conceivably result from alterations in glycosylation. Therefore, the effect of mineral particles on protein glycosylation was investigated in phorbol myristate acetate (PMA)-differentiated U-937. Jacalin, a lectin specific for O-glycosylated structures, showed a global increase in O-glycosylation in particle-treated cells. In contrast, no significant modifications were observed with concanavalin A, a lectin that recognizes certain N-glycosylated structures. The sialic acid-specific lectins Sambucus nigra agglutinin and Maackia amurensis agglutinin and the galactose-specific lectin Ricinus communis agglutinin revealed a complex pattern of alterations in glycoprotein glycosylation after crystalline silica or manganese dioxide treatments. Expression of sialyl Lewis(x), a glycosylated structure implicated in leukocyte trafficking, could not be detected in control or treated cells. This finding was consistent with the decrease in sialyl Lewis(x) expression observed during PMA-induced differentiation. In conclusion, various treatments used in this study induced quantitative as well as qualitative changes in protein glycosylation. Whether these changes are due to glycosidase release or to an alteration in glycosyltransferase expression remains to be determined. The potential functional implications of these changes are currently under investigation.
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spelling pubmed-14701802006-06-01 Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles. Trabelsi, N Greffard, A Pairon, J C Bignon, J Zanetti, G Fubini, B Pilatte, Y Environ Health Perspect Research Article Carbohydrate moieties of cell glycoconjugates play a pivotal role in molecular recognition phenomena involved in the regulation of most biological systems and the changes observed in cell surface carbohydrates during cell activation or differentiation frequently modulate certain cell functions. Consequently, some aspects of macrophage response to particle exposure might conceivably result from alterations in glycosylation. Therefore, the effect of mineral particles on protein glycosylation was investigated in phorbol myristate acetate (PMA)-differentiated U-937. Jacalin, a lectin specific for O-glycosylated structures, showed a global increase in O-glycosylation in particle-treated cells. In contrast, no significant modifications were observed with concanavalin A, a lectin that recognizes certain N-glycosylated structures. The sialic acid-specific lectins Sambucus nigra agglutinin and Maackia amurensis agglutinin and the galactose-specific lectin Ricinus communis agglutinin revealed a complex pattern of alterations in glycoprotein glycosylation after crystalline silica or manganese dioxide treatments. Expression of sialyl Lewis(x), a glycosylated structure implicated in leukocyte trafficking, could not be detected in control or treated cells. This finding was consistent with the decrease in sialyl Lewis(x) expression observed during PMA-induced differentiation. In conclusion, various treatments used in this study induced quantitative as well as qualitative changes in protein glycosylation. Whether these changes are due to glycosidase release or to an alteration in glycosyltransferase expression remains to be determined. The potential functional implications of these changes are currently under investigation. 1997-09 /pmc/articles/PMC1470180/ /pubmed/9400716 Text en
spellingShingle Research Article
Trabelsi, N
Greffard, A
Pairon, J C
Bignon, J
Zanetti, G
Fubini, B
Pilatte, Y
Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title_full Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title_fullStr Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title_full_unstemmed Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title_short Alterations in protein glycosylation in PMA-differentiated U-937 cells exposed to mineral particles.
title_sort alterations in protein glycosylation in pma-differentiated u-937 cells exposed to mineral particles.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470180/
https://www.ncbi.nlm.nih.gov/pubmed/9400716
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