Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala (IAVPGEVA), Ile-Ala-Val-Pro-Thr-Gly-Val-Ala (IAVPTGVA) and Leu-Pro-Tyr-Pro (LPYP), three peptides deriving from soy glycinin hydrolysis, are known to regulate cholesterol metabolism in human hepatic HepG2 cells. We have recently demonstrated that the mechanism of acti...
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doaj-f528d29d658a4807ad69ab2a6f67160e2020-11-24T21:57:44ZengMDPI AGInternational Journal of Molecular Sciences1422-00672015-11-011611273622737010.3390/ijms161126029ijms161126029Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 CellsCarmen Lammi0Chiara Zanoni1Anna Arnoldi2Department of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, ItalyDepartment of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, ItalyDepartment of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, ItalyIle-Ala-Val-Pro-Gly-Glu-Val-Ala (IAVPGEVA), Ile-Ala-Val-Pro-Thr-Gly-Val-Ala (IAVPTGVA) and Leu-Pro-Tyr-Pro (LPYP), three peptides deriving from soy glycinin hydrolysis, are known to regulate cholesterol metabolism in human hepatic HepG2 cells. We have recently demonstrated that the mechanism of action involves the activation of adenosine monophosphate-activated protein kinase (AMPK). This fact suggested a potential activity of the same peptides on glucose metabolism that prompted us to also investigate this aspect in the same cells. After treatment with IAVPGEVA, IAVPTGVA and LPYP, HepG2 cells were analyzed using a combination of molecular techniques, including western blot analysis, glucose uptake experiments and fluorescence microscopy evaluation. The results showed that these peptides are indeed able to enhance the capacity of HepG2 cells to uptake glucose, via glucose transporter 1 GLUT1 and glucose transporter 4 GLUT4 activation, through the stimulation of protein kinase B Akt and adenosine monophosphate-activated protein kinase AMPK pathways, both involved in glucose metabolism.http://www.mdpi.com/1422-0067/16/11/26029bioactive peptidesfunctional foodsglucose uptakeHepG2 cell lineplant proteins |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Carmen Lammi Chiara Zanoni Anna Arnoldi |
spellingShingle |
Carmen Lammi Chiara Zanoni Anna Arnoldi Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells International Journal of Molecular Sciences bioactive peptides functional foods glucose uptake HepG2 cell line plant proteins |
author_facet |
Carmen Lammi Chiara Zanoni Anna Arnoldi |
author_sort |
Carmen Lammi |
title |
Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells |
title_short |
Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells |
title_full |
Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells |
title_fullStr |
Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells |
title_full_unstemmed |
Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells |
title_sort |
three peptides from soy glycinin modulate glucose metabolism in human hepatic hepg2 cells |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2015-11-01 |
description |
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala (IAVPGEVA), Ile-Ala-Val-Pro-Thr-Gly-Val-Ala (IAVPTGVA) and Leu-Pro-Tyr-Pro (LPYP), three peptides deriving from soy glycinin hydrolysis, are known to regulate cholesterol metabolism in human hepatic HepG2 cells. We have recently demonstrated that the mechanism of action involves the activation of adenosine monophosphate-activated protein kinase (AMPK). This fact suggested a potential activity of the same peptides on glucose metabolism that prompted us to also investigate this aspect in the same cells. After treatment with IAVPGEVA, IAVPTGVA and LPYP, HepG2 cells were analyzed using a combination of molecular techniques, including western blot analysis, glucose uptake experiments and fluorescence microscopy evaluation. The results showed that these peptides are indeed able to enhance the capacity of HepG2 cells to uptake glucose, via glucose transporter 1 GLUT1 and glucose transporter 4 GLUT4 activation, through the stimulation of protein kinase B Akt and adenosine monophosphate-activated protein kinase AMPK pathways, both involved in glucose metabolism. |
topic |
bioactive peptides functional foods glucose uptake HepG2 cell line plant proteins |
url |
http://www.mdpi.com/1422-0067/16/11/26029 |
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