Abstract
Caveolae are plasmamembrane regions which take part in the regulation of intracellular trafficking and signaling of tyrosine kinase receptors. Insulin and IGF-I receptors and their intracellular substrates localize in caveolae. Also eNOS is targeted to caveolae and caveolin-1, the major caveolar protein, acts as a regulator of eNOS activity. Since Insulin and IGF-I phosphorylate and activate eNOS, we investigated the role of caveolin-1 in Insulin and IGF-I stimulated eNOS activity. Here we show that: (1) in human endothelial cells, Insulin and IGF-I stimulate eNOS phosphorylation in a different manner both qualitatively and quantitatively; (2) caveolin-1 down regulation abolishes Insulin and IGF-I stimulated eNOS phosphorylation. These results suggest that caveolae could represent an intracellular site that contributes to differentiate IR and IGF-IR activity, and demonstrate the role of caveolin-1 in the eNOS activation by Insulin and IGF-I.
| Original language | English |
|---|---|
| Pages (from-to) | 849-852 |
| Number of pages | 4 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 337 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 25 2005 |
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Keywords
- Caveolin-1
- eNOS
- HUVECs
- IGF-I receptor
- Insulin receptor
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Insulin and IGF-I phosphorylate eNOS in HUVECs by a caveolin-1 dependent mechanism. / Repetto, Silvia; Salani, Barbara; Maggi, Davide; Cordera, Renzo.
In: Biochemical and Biophysical Research Communications, Vol. 337, No. 3, 25.11.2005, p. 849-852.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Insulin and IGF-I phosphorylate eNOS in HUVECs by a caveolin-1 dependent mechanism
AU - Repetto, Silvia
AU - Salani, Barbara
AU - Maggi, Davide
AU - Cordera, Renzo
PY - 2005/11/25
Y1 - 2005/11/25
N2 - Caveolae are plasmamembrane regions which take part in the regulation of intracellular trafficking and signaling of tyrosine kinase receptors. Insulin and IGF-I receptors and their intracellular substrates localize in caveolae. Also eNOS is targeted to caveolae and caveolin-1, the major caveolar protein, acts as a regulator of eNOS activity. Since Insulin and IGF-I phosphorylate and activate eNOS, we investigated the role of caveolin-1 in Insulin and IGF-I stimulated eNOS activity. Here we show that: (1) in human endothelial cells, Insulin and IGF-I stimulate eNOS phosphorylation in a different manner both qualitatively and quantitatively; (2) caveolin-1 down regulation abolishes Insulin and IGF-I stimulated eNOS phosphorylation. These results suggest that caveolae could represent an intracellular site that contributes to differentiate IR and IGF-IR activity, and demonstrate the role of caveolin-1 in the eNOS activation by Insulin and IGF-I.
AB - Caveolae are plasmamembrane regions which take part in the regulation of intracellular trafficking and signaling of tyrosine kinase receptors. Insulin and IGF-I receptors and their intracellular substrates localize in caveolae. Also eNOS is targeted to caveolae and caveolin-1, the major caveolar protein, acts as a regulator of eNOS activity. Since Insulin and IGF-I phosphorylate and activate eNOS, we investigated the role of caveolin-1 in Insulin and IGF-I stimulated eNOS activity. Here we show that: (1) in human endothelial cells, Insulin and IGF-I stimulate eNOS phosphorylation in a different manner both qualitatively and quantitatively; (2) caveolin-1 down regulation abolishes Insulin and IGF-I stimulated eNOS phosphorylation. These results suggest that caveolae could represent an intracellular site that contributes to differentiate IR and IGF-IR activity, and demonstrate the role of caveolin-1 in the eNOS activation by Insulin and IGF-I.
KW - Caveolin-1
KW - eNOS
KW - HUVECs
KW - IGF-I receptor
KW - Insulin receptor
UR - http://www.scopus.com/inward/record.url?scp=26844557817&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=26844557817&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.09.125
DO - 10.1016/j.bbrc.2005.09.125
M3 - Article
C2 - 16225848
AN - SCOPUS:26844557817
VL - 337
SP - 849
EP - 852
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -