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Caveolae and caveolae-like membrane domains in cellular signaling and disease: Identification of downstream targets for the tumor suppressor protein caveolin-1 Biol. Res.
BENDER,FLORENT; MONTOYA,MARGARITA; MONARDES,VIRGINIA; LEYTON,LISETTE; QUEST,ANDREW F.G..
Caveolae are small, flask-shaped invaginations of the plasma membrane present on a large number of mammalian cells. Recent results obtained with knock-out mice for the gene caveolin-1 demonstrate that expression of caveolin-1 protein is essential for caveolae formation in vivo. Caveolae are implicated in a wide variety of cellular events including transcytosis, cholesterol trafficking and as cellular centers important in coordinating signalling events. Caveolae share this role and the property of detergent insolubility with plasma membrane assemblies rich in glycosphingolipids and cholesterol, often called lipid rafts, but preferably referred to here as caveolae-like membrane domains. Due to such widespread presence and usage in cellular function, caveolae...
Tipo: Journal article Palavras-chave: Caveolae; Caveolae-like domains; Lipid rafts; Caveolin-1; Tumor suppressor; Colon carcinoma cells; Microarray analysis.
Ano: 2002 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200006
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Caveolin-1-mediated post-transcriptional regulation of inducible nitric oxide synthase in human colon carcinoma cells Biol. Res.
FELLEY-BOSCO,EMANUELA; BENDER,FLORENT; QUEST,ANDREW F.G..
Reactive oxygen species are now widely recognized as important players contributing both to cell homeostasis and the development of disease. In this respect nitric oxide (NO) is no exception. The discussion here will center on regulation of the inducible form of nitric oxide synthase (iNOS) for two reasons. First, only iNOS produces micromolar NO concentrations, amounts that are high by comparison with the picomolar to nanomolar concentrations resulting from Ca2+-controlled NO production by endothelial eNOS or neuronal nNOS. Second, iNOS is not constitutively expressed in cells and regulation of this isoenzyme, in contrast to endothelial eNOS or neuronal nNOS, is widely considered to occur at the transcriptional level only. In particular, we were...
Tipo: Journal article Palavras-chave: Inducible nitric oxide synthase; Proteosome_mediated proteolysis; Nitroxysomes; Cytokines; Caveolae; Caveolin-1.
Ano: 2002 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200007
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Signaling triggered by Thy-1 interaction with ß3 integrin on astrocytes is an essential step towards unraveling neuronal Thy-1 function Biol. Res.
AVALOS,ANA MARIA; LABRA,CECILIA V.; QUEST,ANDREW F.G.; LEYTON,LISSETTE.
Thy-1 is an abundant neuronal glycoprotein in mammals. Despite such prevalence, Thy-1 function remains largely obscure in the absence of a defined ligand. Recently described evidence that Thy-1 interacts with ß3 integrin on astrocytes will be discussed. Thy-1 binding to ß3 integrin triggers tyrosine phosphorylation of focal adhesion proteins in astrocytes, thereby promoting focal adhesion formation, cell attachment and spreading. Thy-1 has been reported to modulate neurite outgrowth by triggering a cellular response in neurons. However, our data indicate that Thy-1 can also initiate signaling events that promote adhesion of adjacent astrocytes to the underlying surface. Preliminary results suggest that morphological changes observed in the actin...
Tipo: Journal article Palavras-chave: Thy-1 ligand/integrins; GPI-anchored proteins; Strocytes; Focal adhesion.
Ano: 2002 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200015
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