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03138nam a22004455i 4500 |
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978-1-4614-1222-9 |
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|a 9781461412229
|9 978-1-4614-1222-9
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|a 10.1007/978-1-4614-1222-9
|2 doi
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|a Caveolins and Caveolae
|h [electronic resource] :
|b Roles in Signaling and Disease Mechanisms /
|c edited by Jean-François Jasmin, Philippe G. Frank, Michael P. Lisanti.
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|a New York, NY :
|b Springer US,
|c 2012.
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| 300 |
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|a XX, 184p. 27 illus., 1 illus. in color.
|b online resource.
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|a text
|b txt
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|a computer
|b c
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|a online resource
|b cr
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|a text file
|b PDF
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|a Advances in Experimental Medicine and Biology,
|x 0065-2598 ;
|v 729
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|a Lipid Rafts, Caveolae and GPI‑Linked Proteins -- Caveolae and the Regulation of Endocytosis -- Caveolin‑1: Role in Cell Signaling -- Regulation of eNOS in Caveolae -- Recent Developments in the Interactions Between Caveolin and Pathogens -- Caveolin‑1 and Breast Cancer: A New Clinical Perspective -- Caveolin‑1 and Prostate Cancer Progression -- Caveolins and Caveolae, Roles in Insulin Signalling and Diabetes -- Atherosclerosis, Caveolae and Caveolin‑1 -- Caveolins and Heart Diseases -- Caveolins and Lung Function.
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|a 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.
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|a Medicine.
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| 650 |
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|a Biomedicine.
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| 650 |
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|a Biomedicine general.
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| 700 |
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|a Jasmin, Jean-François.
|e editor.
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| 700 |
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|a Frank, Philippe G.
|e editor.
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| 700 |
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|a Lisanti, Michael P.
|e editor.
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| 710 |
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|a SpringerLink (Online service)
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|t Springer eBooks
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| 776 |
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|i Printed edition:
|z 9781461412212
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| 830 |
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|a Advances in Experimental Medicine and Biology,
|x 0065-2598 ;
|v 729
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| 856 |
4 |
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|u http://dx.doi.org/10.1007/978-1-4614-1222-9
|z Full Text via HEAL-Link
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| 912 |
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|a ZDB-2-SBL
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| 950 |
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|a Biomedical and Life Sciences (Springer-11642)
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