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Department of Molecular Pharmacology and the Albert Einstein Cancer Center, Albert Einstein College of Medicine, Bronx, New York
Although they were discovered more than 50 years ago, caveolae have remained enigmatic plasmalemmal organelles. With their characteristic "flasklike" shape and virtually ubiquitous tissue distribution, these interesting structures have been implicated in a wide range of cellular functions. Similar to clathrin-coated pits, caveolae function as macromolecular vesicular transporters, while their unique lipid composition classifies them as plasma membrane lipid rafts, structures enriched in a variety of signaling molecules. The caveolin proteins (caveolin-1, -2, and -3) serve as the structural components of caveolae, while also functioning as scaffolding proteins, capable of recruiting numerous signaling molecules to caveolae, as well as regulating their activity. That so many signaling molecules and signaling cascades are regulated by an interaction with the caveolins provides a paradigm by which numerous disease processes may be affected by ablation or mutation of these proteins. Indeed, studies in caveolin-deficient mice have implicated these structures in a host of human diseases, including diabetes, cancer, cardiovascular disease, atherosclerosis, pulmonary fibrosis, and a variety of degenerative muscular dystrophies. In this review, we provide an in depth summary regarding the mechanisms by which caveolae and caveolins participate in human disease processes.
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X.-Y. Wang, M.-G. Vannucchi, F. Nieuwmeyer, J. Ye, M.-S. Faussone-Pellegrini, and J. D. Huizinga Changes in Interstitial Cells of Cajal at the Deep Muscular Plexus Are Associated with Loss of Distention-Induced Burst-Type Muscle Activity in Mice Infected by Trichinella spiralis Am. J. Pathol., August 1, 2005; 167(2): 437 - 453. [Abstract] [Full Text] [PDF] |
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C. Gurkan, H. Lapp, C. Alory, A. I. Su, J. B. Hogenesch, and W. E. Balch Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome Mol. Biol. Cell, August 1, 2005; 16(8): 3847 - 3864. [Abstract] [Full Text] [PDF] |
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T. M. Williams, G. S. Hassan, J. Li, A. W. Cohen, F. Medina, P. G. Frank, R. G. Pestell, D. Di Vizio, M. Loda, and M. P. Lisanti Caveolin-1 Promotes Tumor Progression in an Autochthonous Mouse Model of Prostate Cancer: GENETIC ABLATION OF Cav-1 DELAYS ADVANCED PROSTATE TUMOR DEVELOPMENT IN TRAMP MICE J. Biol. Chem., July 1, 2005; 280(26): 25134 - 25145. [Abstract] [Full Text] [PDF] |
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D. Cunningham, D. Swartzlander, S. Liyanarachchi, R. V. Davuluri, and G. E. Herman Changes in gene expression associated with loss of function of the NSDHL sterol dehydrogenase in mouse embryonic fibroblasts J. Lipid Res., June 1, 2005; 46(6): 1150 - 1162. [Abstract] [Full Text] [PDF] |
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J. Wharton, T. Meshulamy, G. Vallega, and P. Pilch Dissociation of Insulin Receptor Expression and Signaling from Caveolin-1 Expression J. Biol. Chem., April 8, 2005; 280(14): 13483 - 13486. [Abstract] [Full Text] [PDF] |
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A. W. Cohen, W. Schubert, D. L. Brasaemle, P. E. Scherer, and M. P. Lisanti Caveolin-1 Expression Is Essential for Proper Nonshivering Thermogenesis in Brown Adipose Tissue Diabetes, March 1, 2005; 54(3): 679 - 686. [Abstract] [Full Text] [PDF] |
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