Abstract
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 (Irvingia gabonensis) 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. gabonensis. 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.
Highlights
IntroductionProtein tyrosine phosphorylation plays an important role in signal transduction processes involved in cell growth, metabolism, differentiation, and survival [1]
Introduction published maps and institutional affilProtein tyrosine phosphorylation plays an important role in signal transduction processes involved in cell growth, metabolism, differentiation, and survival [1]
Protein tyrosine phosphatases (PTPs) regulateintyrosine phosphorylation associated with signaling events and have been implicated human diseases such as obesity, diabetes, cancer, and inflammatory been implicated in human diseases such as obesity, diabetes, cancer, and inflammatory diseases [35]
Summary
Protein tyrosine phosphorylation plays an important role in signal transduction processes involved in cell growth, metabolism, differentiation, and survival [1]. Protein tyrosine phosphatases (PTPs) along with protein tyrosine kinases control the phosphorylation of tyrosine residues [2]. PTPs serve as important regulators of signaling events and regulate tyrosine phosphorylation by catalyzing the removal of phosphate groups from phosphorylated tyrosine residues in proteins [3,4]. PTPs are involved in human diseases such as obesity, diabetes, cancer, and inflammatory diseases [5,6]. Diverse PTPs, such as PTPN1, PTPN2, PTPN9, PTPN11, PTPRS, and DUSP9, have been reported to attenuate insulin signaling and trigger type 2 diabetes, indicating that PTPs are promising drug targets for the treatment or prevention of type 2 diabetes [6,7,8].
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