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Endocrinology Vol. 139, No. 4 2077-2084
Copyright © 1998 by The Endocrine Society

ARTICLES

Expression of the MAL Gene in the Thyroid: the MAL Proteolipid, a Component of Glycolipid-Enriched Membranes, Is Apically Distributed in Thyroid Follicles1

Fernando Martín-Belmonte, Leonor Kremer, Juan P. Albar, Mónica Marazuela and Miguel A. Alonso

Centro de Biología Molecular "Severo Ochoa" (F.M.-B., M.A.A.), Universidad Autónoma de Madrid and Consejo Superior de Investigaciones Científicas, Cantoblanco, 28049-Madrid, Spain; Departarment of Immunology and Oncology (L.K., J.P.A.), Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Cantoblanco, 28049-Madrid, Spain; and Department of Endocrinology (M.M.), Hospital de la Princesa, 28006-Madrid, Spain

Address all correspondence and requests for reprints to: Miguel A. Alonso, Centro de Biología Molecular "Severo Ochoa", Universidad Autónoma de Madrid, Cantoblanco, 28049-Madrid, Spain. E-mail: maalonso{at}trasto.cbm.uam.es

The MAL proteolipid, an integral membrane protein expressed in T lymphocytes, polarized epithelial MDCK cells, and myelin-forming cells, has been identified as a component of internal glycolipid-enriched membrane (GEM) microdomains. On the basis of its ability to induce vesicle formation by ectopic expression, MAL has been recently proposed as a component of the machinery for GEM vesiculation. Taking into account the proposed role of GEMs in polarized transport, we have investigated the expression of the MAL gene in thyroid cells. Interestingly, MAL messenger RNA species were detected in the human thyroid, whereas they were undetectable in other endocrine glands tested. Moreover, epithelial FRT cells, a polarized rat cell line of thyroid origin, also expressed MAL transcripts. Immunohistochemical analysis of thyroid follicles, with a newly developed anti-MAL monoclonal antibody, indicates that MAL distribution is restricted to the apical zone of thyroid epithelial cells. Biochemical analyses, using FRT cells, indicate exclusive residence of MAL in GEM microdomains, and these analyses allowed the identification of MAL as a major protein component of the GEM fraction in this cell line. Our results are consistent with a role for MAL as a component of GEM microdomains in thyroid epithelial cells.




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