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The HIV-1 Protease Inhibitor Indinavir Impairs Insulin Signalling in HepG2 Hepatoma Cells

The HIV-1 Protease Inhibitor Indinavir Impairs Insulin Signalling in HepG2 Hepatoma Cells

M Schütt, M Meier, M Meyer, J Klein, S P Aries, H H Klein

Diabetologia. 2000 Sep;43(9):1145-8.

PMID: 11043860

Abstract:

Aims/hypothesis:
Patients treated with human immunodeficiency virus-1 protease inhibitors often develop impaired glucose tolerance or diabetes, most likely due to an induction of insulin resistance. We therefore investigated whether the protease inhibitor indinavir alters insulin signalling.
Methods:
We incubated HepG2 cells for 48 h without or with indinavir (100 micromol/l). Subsequently 125I-insulin binding to the cells and the effects of insulin stimulation on insulin-receptor substrate-1-phosphorylation, association of phosphatidylinositol 3-kinase with insulin-receptor substrate-1 and Akt-Thr308-phosphorylation were measured.
Results:
In cells not exposed to indinavir, insulin (100 nmol/l) led to rapid increases of insulin-receptor substrate-1-phosphorylation, association of phosphatidylinositol 3-kinase with insulin-receptor substrate-1 and Akt-phosphorylation during the first 75 s, followed by subsequent decreases. In indinavir-treated cells, these insulin-stimulated increases during the first 75 s were reduced by 30-60% and this was not associated with alterations in cell number or viability, insulin binding to the cells or cellular insulin-receptor substrate-1-content.
Conclusion/interpretation:
Effects of indinavir on initial insulin signalling could cause, or contribute to, the metabolic effects of human immunodeficiency virus-1 protease inhibitors.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241131	HIV Protease Substrate 1			Price

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