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. 2001 Mar 5;152(5):1079–1086. doi: 10.1083/jcb.152.5.1079

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© 2001 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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(a and b) Immunoelectron microscopy of HepG2 expressing caveolin-2β (clone A-8). Bar, 500 nm. (a) Ultrathin cryosection. Gold particles labeling caveolin-2 are observed in the rim of LD in small clusters (arrowheads); the content of LD appears vacant. (b) Freeze-fracture replica. Gold particles for caveolin-2 are observed in clusters (arrowheads) on the P face of LD, which show an onion-like morphology. The E face of LD (E) is devoid of labeling. (c) Western blotting of subcellular fractions obtained from HepG2 clone A-8. The graph shows the protein content of the fractions. The top two fractions (#1 and #2) contained little protein, but showed positive signals for caveolin-2 and adipophilin. GM130, 66-kD protein, and Na⁺/K⁺-ATPase (Golgi, ER, and plasma membrane markers, respectively) are found only in the bottom fractions.