Abstract
Insulin receptor associated kinase activity and its relationships with the insulin resistance of streptozotocin-induced diabetes were investigated in rats, using solubilized, partially purified insulin receptors from liver membranes. Insulin receptor kinase activity was measured by means of both autophosphorylation and phosphorylation of the exogenous substrate Glu4: Tyr1. Diabetes was associated with a 45% reduction in kinase activity, in the same number of insulin receptors, with no change in insulin binding affinity. To investigate the independent roles of hyperglycemia and hypoinsulinemia on the observed impairment of receptor kinase activity, diabetic rats were fasted for 24 h in order to normalize blood glucose levels only. After this short fast, no change in kinase activity, from the values measured in fed diabetic animals, was observed. Our findings suggest that streptozotocin diabetes is associated with a reduction of insulin receptor kinase activity, which a short fast is not able to reverse.
| Original language | English |
|---|---|
| Pages (from-to) | 850-856 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 140 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 14 1986 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Insulin receptor autophosphorylation and kinase activity in streptozotocin diabetic rats. Effect of a short fast. / Gherzi, Roberto; Andraghetti, Gabriella; Ferrannini, Eleuterio; Cordera, Renzo.
In: Biochemical and Biophysical Research Communications, Vol. 140, No. 3, 14.11.1986, p. 850-856.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Insulin receptor autophosphorylation and kinase activity in streptozotocin diabetic rats. Effect of a short fast
AU - Gherzi, Roberto
AU - Andraghetti, Gabriella
AU - Ferrannini, Eleuterio
AU - Cordera, Renzo
PY - 1986/11/14
Y1 - 1986/11/14
N2 - Insulin receptor associated kinase activity and its relationships with the insulin resistance of streptozotocin-induced diabetes were investigated in rats, using solubilized, partially purified insulin receptors from liver membranes. Insulin receptor kinase activity was measured by means of both autophosphorylation and phosphorylation of the exogenous substrate Glu4: Tyr1. Diabetes was associated with a 45% reduction in kinase activity, in the same number of insulin receptors, with no change in insulin binding affinity. To investigate the independent roles of hyperglycemia and hypoinsulinemia on the observed impairment of receptor kinase activity, diabetic rats were fasted for 24 h in order to normalize blood glucose levels only. After this short fast, no change in kinase activity, from the values measured in fed diabetic animals, was observed. Our findings suggest that streptozotocin diabetes is associated with a reduction of insulin receptor kinase activity, which a short fast is not able to reverse.
AB - Insulin receptor associated kinase activity and its relationships with the insulin resistance of streptozotocin-induced diabetes were investigated in rats, using solubilized, partially purified insulin receptors from liver membranes. Insulin receptor kinase activity was measured by means of both autophosphorylation and phosphorylation of the exogenous substrate Glu4: Tyr1. Diabetes was associated with a 45% reduction in kinase activity, in the same number of insulin receptors, with no change in insulin binding affinity. To investigate the independent roles of hyperglycemia and hypoinsulinemia on the observed impairment of receptor kinase activity, diabetic rats were fasted for 24 h in order to normalize blood glucose levels only. After this short fast, no change in kinase activity, from the values measured in fed diabetic animals, was observed. Our findings suggest that streptozotocin diabetes is associated with a reduction of insulin receptor kinase activity, which a short fast is not able to reverse.
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U2 - 10.1016/0006-291X(86)90712-6
DO - 10.1016/0006-291X(86)90712-6
M3 - Article
C2 - 3022736
AN - SCOPUS:0023001632
VL - 140
SP - 850
EP - 856
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -