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J. Biol. Chem., Vol. 275, Issue 52, 41074-41081, December 29, 2000
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From the Thyroid hormone synthesis by thyrocytes depends
upon apical secretion of thyroglobulin (Tg), the glycoprotein
prohormone. In stably transfected MDCK cells, recombinant Tg is also
secreted apically. All secreted Tg has undergone Golgi carbohydrate
modification, whereas most intracellular Tg (which is slow to exit the
endoplasmic reticulum) is sensitive to digestion with
endoglycosidase H. However, in MDCK cells and PC Cl3 thyrocytes, a
subpopulation of newly synthesized recombinant and endogenous Tg,
respectively, is recovered in a Triton X-100 insoluble,
glycosphingolipid/cholesterol-enriched (GEM/raft) fraction, and this
small subpopulation is overwhelmingly endoglycosidase H resistant. Upon
apical secretion, Tg solubility is restored. Apical secretion of Tg is
inhibited by cellular cholesterol depletion. In FRT cells, recombinant
Tg becomes Triton X-100 insoluble within 60 min after synthesis and a
portion is actually endoglycosidase H-sensitive, suggesting early Tg
entry into GEMs/rafts. Interestingly in FRT cells, Tg remains
associated with the apical plasma membrane upon exocytosis, and all
surface Tg is GEM/raft-associated. Thus, Tg is the first secretory
protein demonstrated to enter Triton X-100 insoluble membranes en route
to the apical surface of epithelial cells. The data imply that Tg
utilizes a cargo-selective mechanism for apical sorting.
Thyroglobulin Is Selected as Luminal Protein Cargo for Apical
Transport via Detergent-resistant Membranes in Epithelial Cells*
§,,
Centro de Biologia Molecular "Severo
Ochoa," Universidad Autonoma de Madrid, Madrid 280-49, Spain
and the ¶ Department of Developmental and Molecular Biology,
and Division of Endocrinology, Albert Einstein College of
Medicine, Bronx, New York 10461
*
This work was supported by grants from the National
Institutes of Health (DK40344 to P. A.), the Direccion General de
Ensenanza Superior (PM99-0092 to M. A. A.), and the Comunidad de
Madrid (08.3/0020/1998) and by an institutional grant from the
Fundacion Ramon Areces to Centro de Biologia Molecular
"Severo Ochoa."The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Div. of
Endocrinology, Albert Einstein College of Medicine, 1300 Morris Park
Ave., Bronx NY 10461. Tel.: 718-430-8685; FAX: 718-430-8557; E-mail: arvan@aecom.yu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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