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Identification of Cyanidin-3-arabinoside Extracted from Blueberry as a Selective Protein Tyrosine Phosphatase 1B Inhibitor

Tian JL, Liao XJ, Wang YH, Si X, Shu C, Gong ES, Xie X, Ran XL, Li B

Journal of agricultural and food chemistry · 52 citas

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Cómo se estudió

Diseño
Estudio in vitro o de mecanismos (clasificado por nuestro filtro de IA)
Estudiado en
Células o muestras de laboratorio
Resultado principal
Solo mecanismos

Quién lo pagó

Financiación
Financiación independiente
Gobierno
National Natural Science Foundation of China
Gobierno
Natural Science Foundation of Liaoning Province
Gobierno
Shenyang Science and Technology Bureau
Universidad u hospital
Shenyang Agricultural University
Gobierno
Key Laboratory of Fruit and Vegetable Processing, Ministry of Agriculture
Gobierno
Department of Human Resources of Liaoning Province
Gobierno
Liaoning Province
Gobierno
Innovative Talent Support Program for Institution of Higher Learning of Liaoning Province
Subvenciones
Natural Science Foundation of Liaoning Province (20180550776); Shenyang Agricultural University (880418027); National Natural Science Foundation of China (31671863); Shenyang Science and Technology Bureau (RC170247)

Según 8 financiadores declarados.

Publicación

Publicado
2019-11-19 · J Agric Food Chem · vol. 67 · número 49 · págs. 13624–13634
Editorial
American Chemical Society
Citado
73 citas · más que el 92% de estudios similares · 2.8× el promedio de su campo
Impacto
Entre el 10 % más citado de su campo
Referencias
30 trabajos
Acceso
De pago
Áreas de investigación
Protein Tyrosine Phosphatases · Microbial Metabolites in Food Biotechnology · Seaweed-derived Bioactive Compounds
Palabras clave
Oleanolic acid, Chemistry, Biochemistry, Protein tyrosine phosphatase, IC50, Phosphatase, Protein kinase B, GSK-3, Enzyme, Pharmacology, Phosphorylation, Biology, In vitro
MeSH
humans, fruit, anthocyanins, glucosides, plant extracts, enzyme inhibitors, molecular structure, kinetics, protein tyrosine phosphatase, non-receptor type 1, phosphatidylinositol 3-kinases, molecular docking simulation, blueberry plants

9 autores

  • Jinlong Tian🇨🇳Shenyang Agricultural University
  • Xiao-Jun Liao🇨🇳Beijing Advanced Innovation Center for Food Nutrition and Human Health; China Agricultural University
  • Yuehua Wang🇨🇳Shenyang Agricultural University
  • Xu Si🇨🇳Shenyang Agricultural University
  • Chi Shu🇨🇳Shenyang Agricultural University
  • Er Sheng Gong🇨🇳Shenyang Agricultural University
  • Xu Xie🇨🇳Shenyang Agricultural University
  • Xu-Long Ran🇨🇳Shenyang Agricultural University
  • Bin Li🇨🇳 · autor de correspondenciaShenyang Agricultural University

Resumen

El texto original del estudio, en el idioma en que se publicó.

Protein tyrosine phosphatase 1B (PTP1B) is an important target for type 2 diabetes. PTP1B inhibitors can reduce blood glucose levels by increasing insulin sensitivity. Anthocyanins often play a hypoglycemic effect, but the research about them have mainly focused on glucosidase. At present, the research about protein tyrosine phosphatase 1B (PTP1B) target is less, and the corresponding molecular mechanism is still unclear. Therefore, in this present study, anthocyanins isolated from blueberry were used to study the inhibitory activity on PTP1B. The isolated cyanidin-3-arabinoside (Cya-3-Ara) exhibited a better inhibitory activity with IC50 = 8.91 ± 0.63 μM, which was higher than the positive control (oleanolic acid, IC50 = 13.9 ± 1.01 μM), and the mechanism of PTP1B inhibition was reversible mixed pattern. The structure-activity relationship (SAR) between anthocyanins and PTP1B inhibition was investigated. The enzyme activity inhibition and molecular docking showed that anthocyanins had high selectivity for PTP1B inhibition. Further study showed that Cya-3-Ara could promote glycogen synthesis through ameliorating PTP1B-involved IRS-1/PI3K/Akt/GSK3β pathways. Cya-3-Ara could also be regarded as a synergistic inhibitor (CI ≤ 0.54) of oleanolic acid to obtain a better inhibitory effect on PTP1B. Taken together, our study clearly illustrates the SAR between anthocyanins and PTP1B inhibition and the mechanism of Cya-3-Ara in the insulin signaling pathway.

Resumen vía Europe PMC. Los derechos de autor siguen siendo de los autores o la editorial.

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