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Caveolin‐1 expression in Schwann cells

Glia, 1999
Caveolae are non-clathrin-coated invaginations of the plasma membrane, which are present in most cell types. An integral component of caveolae is the caveolin family of related proteins, which not only forms the structural framework of caveolae, but also likely subserves its functional roles, including regulation of signal transduction and cellular ...
Mikol, Daniel D.   +3 more
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Isoforms of caveolin-1 and caveolar structure

Journal of Cell Science, 2000
ABSTRACT The relationship between caveolin-1 isoforms (α and β) and caveolar ultrastructure was studied. By immunofluorescence microscopy of human fibroblasts, caveolae were observed as dots positive for caveolin-1, but many dots labeled by an antibody recognizing both isoforms (anti-αβ) were not labeled by another antibody specific for ...
Tomoko Une   +3 more
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Caveolin-1 in Brain Tumors

2011
Increasing evidences in the last years suggested a possible involvement of caveolin-1 (cav-1) in the biology of brain tumors. In vitro studies on glioma cell lines as well as immuno-phenotyping of primary human gliomas reported that cav-1 expression in brain tumors varies according to the histotype and grade, and could bear prognostic significance in ...
SENETTA, REBECCA, CASSONI, Paola
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Caveats of caveolin-1 in cancer progression

Cancer Letters, 2008
Caveolin-1, an essential scaffold protein of caveolae and cellular transport processes, lately gained recognition as a stage- and tissue-specific tumor modulator in vivo. Patient studies and rodent models corroborated its janus-faced role as a tumor suppressor in non-neoplastic tissue, its down-regulation (loss of function) upon transformation and its ...
Roland M. Schmid   +4 more
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Caveolae and caveolin-1 in reptilian liver

Micron, 2011
Caveolae are plasma-membrane invaginations that, by interacting with membrane-associated molecules such as endothelial nitric oxide synthase and tyrosine kinases, precisely regulate cell-signalling pathways responsible for cell structure and cell function. Indeed, there is widespread evidence that caveolae associate, structurally and functionally, with
Joanna M. Biazik   +2 more
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Tyrosine Phosphorylation of Caveolin-1 in the Endothelium

Experimental Cell Research, 1999
Caveolin-1, a scaffolding protein of caveolae, is known to be tyrosine-phosphorylated by Src kinases. Recently we generated a specific antibody to caveolin-1 phosphorylated at tyrosine-14 (PY14) (R. Nomura and T. Fujimoto, 1999, Mol. Biol. Cell 10, 975-986).
Takeo Aoki   +2 more
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Oxidative Stress, Caveolae and Caveolin-1

2004
Oxidative stress underlies a range of pathophysiological conditions. Reactive oxygen species are also generated intracellularly to serve as second messengers and some are linked to caveolae/raft signalling systems. The effect of oxidative stress on caveolin-1 expression, post-translational modifications, membrane trafficking and function are described.
Parat, Marie-Odile, Fox, Paul L
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The role of caveolin‐1 in cardiovascular regulation

Acta Physiologica, 2009
AbstractCaveolae are omega‐shaped membrane invaginations present in essentially all cell types in the cardiovascular system, and numerous functions have been ascribed to these structures. Caveolae formation depends on caveolins, cholesterol and polymerase I and transcript release factor‐Cavin (PTRF‐Cavin).
Karl Swärd, Awahan Rahman
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Caveolin-1 and Breast Cancer

2011
Caveolin-1 (Cav-1), the main protein component of caveolae, is expressed in several differentiated cell types such as mammary epithelial cells. It is well-established that caveolae function as an organizing center that recruits and sequesters various signaling molecules.
Michael P. Lisanti, Gloria Bonuccelli
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The Role of Caveolin-1 in Retinal Inflammation

2019
Although the retina resides within the immune-protected ocular environment, inflammatory processes mounted in the eye can lead to retinal damage. Unchecked chronic ocular inflammation leads to retinal damage. Thus, retinal degenerative diseases that result in chronic inflammation accelerate retinal tissue destruction and vision loss.
Jami M. Gurley, Michael H. Elliott
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