TY - JOUR
T1 - Involvement of caveolae and caveolae-like domains in signalling, cell survival and angiogenesis
AU - Massimino, Maria Lina
AU - Griffoni, Cristiana
AU - Spisni, Enzo
AU - Toni, Mattia
AU - Tomasi, Vittorio
PY - 2002
Y1 - 2002
N2 - Caveolae, the flask-shaped membrane invaginations abundant in endothelial cells, have acquired a prominent role in signal transduction. Evidence, that events occurring in caveolae participate in cell survival and angiogenesis, has been recently substantiated by the identification of two novel caveolar constituents: prostacyclin synthase (PGIS) and the cellular form of prion protein (PrPc). We have shown that PGIS, previously described as an endoplasmic reticulum component, is bound to caveolin-1 (cav-1) and localized in caveolae in human endothelial cells. By generating prostacyclin, PGIS is involved in angiogenesis. Previous observations regarding the localization of PrPc in caveolae-like membrane domains (CLDs) have been recently confirmed and extended. It has been demonstrated that PrPc is bound to cav-1 and, by recruiting Fyn kinase, can participate in signal transduction events connected to cell survival and differentiation. The new entries of PGIS and PrPc in caveolar components place caveolae and CLDs at the centre of a network, where cells decide whether to proliferate or differentiate and whether to survive or to suicide by apoptosis.
AB - Caveolae, the flask-shaped membrane invaginations abundant in endothelial cells, have acquired a prominent role in signal transduction. Evidence, that events occurring in caveolae participate in cell survival and angiogenesis, has been recently substantiated by the identification of two novel caveolar constituents: prostacyclin synthase (PGIS) and the cellular form of prion protein (PrPc). We have shown that PGIS, previously described as an endoplasmic reticulum component, is bound to caveolin-1 (cav-1) and localized in caveolae in human endothelial cells. By generating prostacyclin, PGIS is involved in angiogenesis. Previous observations regarding the localization of PrPc in caveolae-like membrane domains (CLDs) have been recently confirmed and extended. It has been demonstrated that PrPc is bound to cav-1 and, by recruiting Fyn kinase, can participate in signal transduction events connected to cell survival and differentiation. The new entries of PGIS and PrPc in caveolar components place caveolae and CLDs at the centre of a network, where cells decide whether to proliferate or differentiate and whether to survive or to suicide by apoptosis.
KW - Angiogenesis
KW - Caveolin
KW - Prion protein
KW - Prostacyclin synthase
KW - Signal transduction
UR - http://www.scopus.com/inward/record.url?scp=0036142738&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036142738&partnerID=8YFLogxK
U2 - 10.1016/S0898-6568(01)00232-7
DO - 10.1016/S0898-6568(01)00232-7
M3 - Article
C2 - 11781132
AN - SCOPUS:0036142738
VL - 14
SP - 93
EP - 98
JO - Cellular Signalling
JF - Cellular Signalling
SN - 0898-6568
IS - 2
ER -