Gastro-Resistant Insulin Receptor-Binding Peptide from Momordica charantia Improved the Glucose Tolerance in Streptozotocin-Induced Diabetic Mice via Insulin Receptor Signaling Pathway

2017 ◽  
Vol 65 (42) ◽  
pp. 9266-9274 ◽  
Author(s):  
Hsin-Yi Lo ◽  
Chia-Cheng Li ◽  
Feng-Yuan Chen ◽  
Jaw-Chyun Chen ◽  
Chien-Yun Hsiang ◽  
...  
Keyword(s):  
Glucose Tolerance ◽  
Insulin Receptor ◽  
Signaling Pathway ◽  
Receptor Binding ◽  
Momordica Charantia ◽  
Receptor Signaling ◽  
Diabetic Mice ◽  
Binding Peptide ◽  
Insulin Receptor Signaling ◽  
Receptor Signaling Pathway

Pharmacological Regulation of the Insulin Receptor Signaling Pathway Mimics Insulin Action in Cells Transduced with Viral Vectors

2004 ◽  
Vol 15 (11) ◽  
pp. 1101-1108 ◽  
Author(s):  
Gabriella Cotugno ◽  
Roy Pollock ◽  
Pietro Formisano ◽  
Katja Linher ◽  
Francesco Beguinot ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Signaling Pathway ◽  
Insulin Action ◽  
Viral Vectors ◽  
Receptor Signaling ◽  
Insulin Receptor Signaling ◽  
Receptor Signaling Pathway ◽  
Pharmacological Regulation ◽  
In Cells

scholarly journals Activation Of Insulin Receptor Signaling Pathway Using Ligand Microbeads In Mammalian Cells And Isolation Of Receptor-Bead Complex

2021 ◽  
Author(s):  
Sana Ahmed
Keyword(s):  
Insulin Receptor ◽  
Signaling Pathway ◽  
Receptor Activation ◽  
Hydroxyl Group ◽  
Receptor Signaling ◽  
Ph Domain ◽  
Western Blots ◽  
Mammalian Cell Lines ◽  
Insulin Receptor Signaling ◽  
Receptor Signaling Pathway

The study of cell surface receptors and their associated signaling pathways on the plasma membrane are vital in understanding cellular responses. The insulin receptor is a tyrosine kinase that is activated in response to insulin microbeads presented to three mammalian cell lines: CHO, NIH-3T3 and COS-7. Phosphatidylinositol 3-kinase (PI3K) signaling, a major insulin receptor signaling pathway, phosphorylates the 3-position hydroxyl group of the inositol ring of phosphatidylinositol-4,5-biphosphate, resulting in phosphatidylinositol-3,4,5-triphosphate (PIP3) that acts by recruiting specific pleckstrin homology (PH) domain containing proteins to cell membranes. Akt (protein kinase B) containing PH domain gets activated, binds to PIP3 and localizes to the site of receptor activation. The PH domain of Akt was fused to green fluorescent protein (GFP) to create a biosensor for phosphatidylinositol. Confocal microscopy confirmed Akt-PH recruitment to the cell membrane. Immunofluorescence staining (IF) and western blots confirmed insulin receptor and phosphotyrosine activity in cells. The activated insulin receptor complex was captured and isolated by insulin coated microbeads on the surface of cells.

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