Abstract
Sodium vanadate activates "in vitro" insulin receptor autophosphorylation and protein tyrosine kinase in a dose-dependent manner. Insulin receptor protein tyrosine kinase is directly activated also by the anti-insulin receptor beta subunit monoclonal antibody 18-44. We previously demonstrated that the anti-insulin receptor monoclonal antibody MA-10 decreases insulin-stimulated receptor protein tyrosine kinase activity "in vitro", without inhibiting insulin receptor binding. In this report we show that insulin receptor protein tyrosine kinase, activated by sodium vanadate or by monoclonal antibody 18-44, is inhibited by MA-10 antibody. These data suggest that insulin receptor protein tyrosine kinase activity can be either activated and inhibited through mechanisms different from insulin binding.
| Original language | English |
|---|---|
| Pages (from-to) | 1474-1480 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 152 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - May 16 1988 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies. / Gherzi, Roberto; Caratti, Cinzia; Andraghetti, Gabriella; Bertolini, Stefano; Montemurro, Antonio; Sesti, Giorgio; Cordera, Renzo.
In: Biochemical and Biophysical Research Communications, Vol. 152, No. 3, 16.05.1988, p. 1474-1480.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies
AU - Gherzi, Roberto
AU - Caratti, Cinzia
AU - Andraghetti, Gabriella
AU - Bertolini, Stefano
AU - Montemurro, Antonio
AU - Sesti, Giorgio
AU - Cordera, Renzo
PY - 1988/5/16
Y1 - 1988/5/16
N2 - Sodium vanadate activates "in vitro" insulin receptor autophosphorylation and protein tyrosine kinase in a dose-dependent manner. Insulin receptor protein tyrosine kinase is directly activated also by the anti-insulin receptor beta subunit monoclonal antibody 18-44. We previously demonstrated that the anti-insulin receptor monoclonal antibody MA-10 decreases insulin-stimulated receptor protein tyrosine kinase activity "in vitro", without inhibiting insulin receptor binding. In this report we show that insulin receptor protein tyrosine kinase, activated by sodium vanadate or by monoclonal antibody 18-44, is inhibited by MA-10 antibody. These data suggest that insulin receptor protein tyrosine kinase activity can be either activated and inhibited through mechanisms different from insulin binding.
AB - Sodium vanadate activates "in vitro" insulin receptor autophosphorylation and protein tyrosine kinase in a dose-dependent manner. Insulin receptor protein tyrosine kinase is directly activated also by the anti-insulin receptor beta subunit monoclonal antibody 18-44. We previously demonstrated that the anti-insulin receptor monoclonal antibody MA-10 decreases insulin-stimulated receptor protein tyrosine kinase activity "in vitro", without inhibiting insulin receptor binding. In this report we show that insulin receptor protein tyrosine kinase, activated by sodium vanadate or by monoclonal antibody 18-44, is inhibited by MA-10 antibody. These data suggest that insulin receptor protein tyrosine kinase activity can be either activated and inhibited through mechanisms different from insulin binding.
UR - http://www.scopus.com/inward/record.url?scp=0023891512&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023891512&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(88)80452-2
DO - 10.1016/S0006-291X(88)80452-2
M3 - Article
C2 - 2837189
AN - SCOPUS:0023891512
VL - 152
SP - 1474
EP - 1480
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -