| Description |
1 online resource (xx, 184 pages) : illustrations (some color) |
| Series |
Advances in experimental medicine and biology ; v. 729 |
|
Advances in experimental medicine and biology ; v. 729. 0065-2598
|
| Contents |
Lipid rafts, caveolae, and GPI linked proteins / Valerie L. Reeves, Candice M. Thomas, and Eric J. Smart -- Caveolae and the regulation of endocytosis / Anna L. Kiss -- Caveolin : role in cell signaling / Cecile Boscher and Ivan Robert Nabi -- Regulation of ENOS in caveolae / Chieko Mineo and Philip W. Shaul -- Recent developments in the interactions between caveolin and pathogens / Fabiana S. Machado [and others] -- Caveolin and breast cancer : a new clinical perspective / Isabelle Mercier and Michael P. Lisanti -- Caveolin and prostate cancer progression / Michael R. Freeman, Wei Yang, and Dolores Di Vizio -- Caveolins and caveolae, roles in insulin signalling, and diabetes / Peter Strolfors -- Atherosclerosis, caveolae, and caveolin / Stephanos Pavlides [and others] -- Caveolins and heart diseases / Mathivadhani Panneerselvam, Hemal H. Patel, and David M. Roth -- Caveolins and lung function / Nikolaos A. Maniatis [and others] |
| Summary |
Caveolae are 50-100 nm flask-shaped invaginations of the plasma membrane that are primarily composed of cholesterol and sphingolipids. Using modern electron microscopy techniques, caveolae can be observed as omega-shaped invaginations of the plasma membrane, fully-invaginated caveolae, grape-like clusters of interconnected caveolae (caveosome), or as transcellular channels as a consequence of the fusion of individual caveolae. The caveolin gene family consists of three distinct members, namely Cav-1, Cav-2 and Cav-3. Cav-1 and Cav-2 proteins are usually co-expressed and particularly abundant in epithelial, endothelial, and smooth muscle cells as well as adipocytes and fibroblasts. On the other hand, the Cav-3 protein appears to be muscle-specific and is therefore only expressed in smooth, skeletal and cardiac muscles. Caveolin proteins form high molecular weight homo- and/or hetero-oligomers and assume an unusual topology with both their N- and C-terminal domains facing the cytoplasm |
| Analysis |
biomedische wetenschappen |
|
biomedicine |
|
Medicine (General) |
|
Geneeskunde (algemeen) |
| Bibliography |
Includes bibliographical references and index |
| Notes |
Print version record |
| Subject |
Membrane proteins.
|
|
Cellular signal transduction.
|
|
Caveolins -- physiology
|
|
Caveolae -- pathology
|
|
Caveolae -- physiology
|
|
Signal Transduction
|
|
Membrane Proteins
|
|
SCIENCE -- Life Sciences -- Cell Biology.
|
|
Cellular signal transduction
|
|
Membrane proteins
|
| Form |
Electronic book
|
| Author |
Jasmin, Jean-François, 1976-
|
|
Frank, Philippe G
|
|
Lisanti, Michael P
|
| ISBN |
9781461412229 |
|
1461412226 |
|
