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Promoting Glut4 Translocation in Diabetes with MGF E-domain Peptides

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Technical Report,01 Jun 2017,30 Nov 2018

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Medical College of Wisconsin Milwaukee United States

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The metabolic changes in diabetes are directly triggered by hyperglycemia and the rate limiting step in glucose uptake is the translocation of the insulin-sensitive glucose transporter protein-4 GLUT4 in insulin sensitive tissues. The purpose of this was to test whether peptide analogs derived from the IGF-1 isoform expressed in muscle known as Mechano-growth factor can function as a bio-therapeutics to modulate of AS160 phosphorylation which is necessary to stimulate GLUT4 function. Using skeletal muscle cell based models, we aimed to define an optimal candidate peptide to test in animal based modes of diabetes. Skeletal muscle myotube cells undergoing membrane depolarization in the presence of 3 mM extracellular calcium are necessary to demonstrate peptide mediated actions. We have found by preventing phosphorylation within the 14-3-3 binding domain of the SA18 peptide blocks Akt mediated inhibition of the RafERK signaling branch following IGF-1 stimulation, whereas phosphorylation within the 14-3-3 binding domain of the SE18 peptide may augment Akt signaling by shutting down RafERK signaling. Consequently, we have defined that the MGF E-domain peptides act as modulators of branches of the IGF-1 signaling pathway through interactions with specific 14-3-3 binding proteins that specifically target c-Raf activity.

Subject Categories:

  • Medicine and Medical Research
  • Biochemistry
  • Genetic Engineering and Molecular Biology

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