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Glucose Uptake Measurement and Response to Insulin Stimulation in In Vitro Cultured Human Primary Myotubes

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Published on: June 25, 2017

Signaling pathways mediating insulin-stimulated glucose transport.

S A Summers¹, V P Yin, E L Whiteman

¹Howard Hughes Medical Institute, Cox Institute, University of Pennsylvania Medical School, Philadelphia, Pennsylvania 19104, USA. birnbaum@hhmi.upenn.edu

Annals of the New York Academy of Sciences

|June 8, 2000

Summary

Insulin accelerates sugar uptake in cells. Phosphatidylinositol 3-kinase and Akt/PKB are key signaling molecules, though Akt/PKB's role in glucose transport is debated, with ceramide potentially influencing this process.

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Area of Science:

Biochemistry
Cellular Metabolism
Endocrinology

Background:

Insulin regulates glucose uptake in muscle and adipose tissue.
The precise molecular mechanisms of insulin action are still being investigated.
Phosphatidylinositol 3-kinase (PI3K) is crucial for insulin-stimulated glucose uptake.

Purpose of the Study:

To investigate the role of Akt/PKB in insulin's metabolic actions.
To explore the controversial involvement of Akt/PKB in glucose transport.
To examine the effect of ceramide on insulin signaling pathways.

Main Methods:

Analysis of insulin signaling cascades.
Investigation of phosphatidylinositol 3-kinase activity.
Assessment of Akt/PKB activation and glucose transport.
Use of soluble ceramide analogues.

Main Results:

PI3K is essential for insulin to stimulate hexose uptake in adipocytes.
Akt/PKB is activated in a PI3K-dependent manner by insulin.
Ceramide analogues inhibit both Akt/PKB activation and insulin-stimulated glucose transport.

Conclusions:

Akt/PKB is implicated as a mediator of insulin's metabolic effects.
Ceramide's antagonism suggests a link between ceramide, Akt/PKB, and glucose transport.
Further research is needed to fully clarify Akt/PKB's role in insulin-driven glucose uptake.