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dc.creatorBENDER,FLORENT
dc.creatorMONTOYA,MARGARITA
dc.creatorMONARDES,VIRGINIA
dc.creatorLEYTON,LISETTE
dc.creatorQUEST,ANDREW F.G.
dc.date2002-01-01
dc.date.accessioned2019-05-02T21:21:05Z
dc.date.available2019-05-02T21:21:05Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200006
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/81409
dc.descriptionCaveolae 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 and related domains are implicated in human diseases, including cancer. In particular, the protein caveolin-1 is suggested to function as a tumor suppressor protein. Evidence demonstrating such a role for caveolin-1 in human colon carcinoma cells will be discussed together with data from microarray experiments seeking to identify caveolin-1 target genes responsible for such behavior.
dc.formattext/html
dc.languageen
dc.publisherSociedad de Biología de Chile
dc.relation10.4067/S0716-97602002000200006
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceBiological Research v.35 n.2 2002
dc.subjectcaveolae
dc.subjectcaveolae-like domains
dc.subjectlipid rafts
dc.subjectcaveolin-1
dc.subjecttumor suppressor
dc.subjectcolon carcinoma cells
dc.subjectmicroarray analysis
dc.titleCaveolae and caveolae-like membrane domains in cellular signaling and disease: Identification of downstream targets for the tumor suppressor protein caveolin-1


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