Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases

Protein tyrosine phosphatases (PTPs), along with protein tyrosine kinases, control signaling pathways involved in cell growth, metabolism, differentiation, proliferation, and survival. Several PTPs, such as PTPN1, PTPN2, PTPN9, PTPN11, PTPRS, and DUSP9, disrupt insulin signaling and trigger type 2 d...

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Main Authors: Sun-Young Yoon, Jinsoo Kim, Bum Soo Lee, Su Cheol Baek, Sang J. Chung, Ki Hyun Kim
Format: Article
Language:English
Published: MDPI AG 2022-02-01
Series:Biomolecules
Subjects:
Online Access:https://www.mdpi.com/2218-273X/12/2/321
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author Sun-Young Yoon
Jinsoo Kim
Bum Soo Lee
Su Cheol Baek
Sang J. Chung
Ki Hyun Kim
author_facet Sun-Young Yoon
Jinsoo Kim
Bum Soo Lee
Su Cheol Baek
Sang J. Chung
Ki Hyun Kim
author_sort Sun-Young Yoon
collection DOAJ
description Protein tyrosine phosphatases (PTPs), along with protein tyrosine kinases, control signaling pathways involved in cell growth, metabolism, differentiation, proliferation, and survival. Several PTPs, such as PTPN1, PTPN2, PTPN9, PTPN11, PTPRS, and DUSP9, disrupt insulin signaling and trigger type 2 diabetes, indicating that PTPs are promising drug targets for the treatment or prevention of type 2 diabetes. As part of an ongoing study on the discovery of pharmacologically active bioactive natural products, we conducted a phytochemical investigation of African mango (<i>Irvingia gabonensis</i>) using liquid chromatography–mass spectrometry (LC/MS)-based analysis, which led to the isolation of terminalin as a major component from the extract of the seeds of <i>I. gabonensis</i>. The structure of terminalin was characterized by spectroscopic methods, including one-dimensional (1D) and two-dimensional (2D) nuclear magnetic resonance (NMR) and high-resolution (HR) electrospray ionization (ESI) mass spectroscopy. Moreover, terminalin was evaluated for its antidiabetic property; terminalin inhibited the catalytic activity of PTPN1, PTPN9, PTPN11, and PTPRS in vitro and led to a significant increase in glucose uptake in differentiated C2C12 muscle cells, indicating that terminalin exhibits antidiabetic effect through the PTP inhibitory mechanism. These findings suggest that terminalin derived from African mango could be used as a functional food ingredient or pharmaceutical supplement for the prevention of type 2 diabetes.
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spelling doaj.art-4ed271b680b1431e89d177e61c5fd28c2023-11-23T19:00:03ZengMDPI AGBiomolecules2218-273X2022-02-0112232110.3390/biom12020321Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine PhosphatasesSun-Young Yoon0Jinsoo Kim1Bum Soo Lee2Su Cheol Baek3Sang J. Chung4Ki Hyun Kim5Department of Cosmetic Science, Kwangju Women’s University, Gwangju 62396, KoreaSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, KoreaSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, KoreaSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, KoreaSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, KoreaSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, KoreaProtein tyrosine phosphatases (PTPs), along with protein tyrosine kinases, control signaling pathways involved in cell growth, metabolism, differentiation, proliferation, and survival. Several PTPs, such as PTPN1, PTPN2, PTPN9, PTPN11, PTPRS, and DUSP9, disrupt insulin signaling and trigger type 2 diabetes, indicating that PTPs are promising drug targets for the treatment or prevention of type 2 diabetes. As part of an ongoing study on the discovery of pharmacologically active bioactive natural products, we conducted a phytochemical investigation of African mango (<i>Irvingia gabonensis</i>) using liquid chromatography–mass spectrometry (LC/MS)-based analysis, which led to the isolation of terminalin as a major component from the extract of the seeds of <i>I. gabonensis</i>. The structure of terminalin was characterized by spectroscopic methods, including one-dimensional (1D) and two-dimensional (2D) nuclear magnetic resonance (NMR) and high-resolution (HR) electrospray ionization (ESI) mass spectroscopy. Moreover, terminalin was evaluated for its antidiabetic property; terminalin inhibited the catalytic activity of PTPN1, PTPN9, PTPN11, and PTPRS in vitro and led to a significant increase in glucose uptake in differentiated C2C12 muscle cells, indicating that terminalin exhibits antidiabetic effect through the PTP inhibitory mechanism. These findings suggest that terminalin derived from African mango could be used as a functional food ingredient or pharmaceutical supplement for the prevention of type 2 diabetes.https://www.mdpi.com/2218-273X/12/2/321protein tyrosine phosphatases (PTPs)PTPN1PTPN9PTPN11PTPRStype 2 diabetes
spellingShingle Sun-Young Yoon
Jinsoo Kim
Bum Soo Lee
Su Cheol Baek
Sang J. Chung
Ki Hyun Kim
Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
Biomolecules
protein tyrosine phosphatases (PTPs)
PTPN1
PTPN9
PTPN11
PTPRS
type 2 diabetes
title Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
title_full Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
title_fullStr Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
title_full_unstemmed Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
title_short Terminalin from African Mango (<i>Irvingia gabonensis</i>) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases
title_sort terminalin from african mango i irvingia gabonensis i stimulates glucose uptake through inhibition of protein tyrosine phosphatases
topic protein tyrosine phosphatases (PTPs)
PTPN1
PTPN9
PTPN11
PTPRS
type 2 diabetes
url https://www.mdpi.com/2218-273X/12/2/321
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