Fiche publication
Date publication
novembre 2000
Journal
Lipids
Auteurs
Membres identifiés du Cancéropôle Est :
Pr MARTINY Laurent
,
Dr SCHNEIDER Christophe
,
Dr EL BTAOURI Hassan
Tous les auteurs :
Schneider C, Delorme N, Buisson-Legendre N, Bellon G, Emonard H, Btaouri HE, Hornebeck W, Haye B, Martiny L
Lien Pubmed
Résumé
Neutral sphingomyelinase (Smase) is a cell membrane-associated phospholipase that hydrolyzes sphingomyelin to phosphocholine and ceramide, a lipid second messenger involved in cell differentiation and/or apoptosis. We first evidenced that porcine cultured thyroid cells could express neutral Smase activity even if thyrotropin (TStH), an essential hormone in thyroid cell differentiation, was found to induce a 1.7-fold decrease in Smase activity. Triggering the ceramide pathway by exogenous addition of neutral bacterial Smase (0.1 U/mL for 48 h), which transiently increased ceramide level by fourfold, drastically modified thyroid cell morphology. The follicle-like structures generated by TSH were disrupted, and the Smase-induced cell spreading was accompanied by a parallel loss of cell ability to iodinate proteins as well as a decrease of the adenylate cyclase system response. These inhibitory effects have been reproduced using short-chain exogenous ceramide analogs (C2-ceramides). Overall these data showed that ceramides emerged as potential mediators of dedifferentiation in thyroid cells.
Mots clés
Animals, Cell Differentiation, drug effects, Cells, Cultured, Ceramides, metabolism, Signal Transduction, Sphingomyelin Phosphodiesterase, metabolism, Swine, Thyroid Gland, cytology, Thyrotropin, pharmacology
Référence
Lipids. 2000 Nov;35(11):1259-68
