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This version published online on December 11, 2003
Endocrinology, doi:10.1210/en.2003-1432
A more recent version of this article appeared on March 1, 2004
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Submitted on October 23, 2003
Accepted on December 3, 2003

Sphingolipid-cholesterol domains (lipid rafts) in normal human and dog thyroid follicular cells are not involved in thyrotropin receptor signaling

M. J. Costa1, Y. Song1, P. Macours1, C. Massart1, M. C. Many1, S. Costagliola1, J. E. Dumont1, J. Van Sande1*, and V. Vanvooren1

1 Institute of Interdisciplinary Research (IRIBHM), Free University of Brussels, School of Medicine, Brussels, Belgium. Faculty of Medicine, University of Porto, Porto, Portugal. Histology Unit, Catholic University of Leuven, Medical School, Brussels, Belgium.

* To whom correspondence should be addressed. E-mail: jvsande{at}ulb.ac.be.

Partition of signaling molecules in sphingolipids-cholesterol enriched membrane domains - among which the caveolae - may contribute to signal transduction efficiency. In normal thyroid, nothing is known about a putative TSH (TSH)/cyclic AMP (cAMP) cascade compartmentation in caveolae or other sphingolipid-cholesterol enriched membrane domains. In this study, we show for the first time that caveolae are present in the apical membrane of dog and human thyrocytes: caveolin-1 mRNA presence is demonstrated by Northen blotting in primary cultures and that of the caveolin-1 protein by immunohistochemistry performed on human thyroid tissue. The TSH receptor located in the basal membrane can therefore not be located in caveolae. We demonstrate, for the first time by biochemical methods the existence of sphingolipid-cholesterol enriched domains in human and dog thyroid follicular cells, that contain caveolin, flotillin-2 and the insulin receptor. We assessed a possible sphingolipid-cholesterol enriched domains compartmentation of the TSH receptor and the {alpha}-subunit of the heterotrimeric Gs and Gq proteins using two approaches: Western blotting on detergent-resistant membranes isolated from thyrocytes in primary cultures and the influence of 10 mM methyl {beta}-cyclodextrin (M{beta}CD), a cholesterol chelator, on the basal and stimulated cAMP accumulation in intact thyrocytes. The results from both types of experiments strongly suggest that the TSH/cAMP cascade in thyroid cells is not associated with sphingolipid-cholesterol enriched membrane domains.
Key words: TSH receptor • lipid rafts • thyrocytes • caveolae • caveolin




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