Environmental Health Perspectives 105, Supplement 5, September 1997: Article by Trabelsi et al

Environmental Health Perspectives 105, Supplement 5, September 1997

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Alterations in Protein Glycosylation in PMA-differentiated U-937 Cells Exposed to Mineral Particles

Nourredine Trabelsi, ¹ Anne Greffard, ¹ Jean-Claude Pairon, ¹ Jean Bignon, ¹ Giovanna Zanetti, ² Bice Fubini, ² and Yannick Pilatte ¹

¹ INSERM, U139, IM3, Faculté de Médecine 8, Créteil, France
² Dipartimento Di Chimica Inorganica, Chimica Fisica e Chimica Dei Materiali, Universita di Torino, Torino, Italy

Abstract
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. -- Environ Health Perspect 105(Suppl 5):1153-1158 (1997)

Key words : U-937, DQ ₁₂ , MnO ₂ , TiO ₂ , PMA, sialyl Lewis ^x , glycosylation, sialic acid, lectin

This paper is based on a presentation at The Sixth International Meeting on the Toxicology of Natural and Man-Made Fibrous and Non-Fibrous Particles held 15-18 September 1996 in Lake Placid, New York. Manuscript was received at EHP 26 March 1997; accepted 22 April 1997.

Authors wish to thank M.-C. Jaurand for helpful discussions and C. Vaslin for her excellent secretarial assistance.

This work was supported by institutional funding from Institut National de la Santé et de la Recherche Médicale and European Union grant EV5V CT94 O399.

Address correspondence to Dr. Y. Pilatte, Institut National de la Santé et de la Recherche Médicale U139, Faculté de Médecine 8, rue Général Sarrail 94010, Créteil, Cedex, France. Telephone: 33 01 49 81 37 13. Fax: 33 01 49 81 35 33. E-mail: pilatte@im3.inserm.fr

Abbreviations used: AM, alveolar macrophage(s); ConA, concanavalin A; DQ ₁₂ , crystalline silica; ECL, enhanced chemical luminescence; Fuc, fucose; Gal, galactose; GalNac, N-acetylgalactosamine; GlucNac, N-acetylglucosamine; GS I-B4, Griffonia simplicifolia agglutinin; MAA, Maackia amurensis agglutinin; MnO ₂ , manganese dioxide; PBS, phosphate-buffered saline; PMA, phorbol myristate acetate; PNA, peanut agglutinin; PVP, polyvinylpyrolidone; RCA, Ricinus communis agglutinin I; SNA, Sambucus nigra agglutinin; TiO ₂ , titanium dioxide; UEA I, Ulex europeaus agglutinin I.

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Last Update: October 28, 1997