Modulating lipid and glucose metabolism by glycosylated kaempferol rich roasted leaves of Lycium chinense via upregulating adiponectin and AMPK activation in obese mice-induced type 2 diabetes. (September 2020)

• Record Type: Journal Article
• Authors: Choi, Eun-Hye; Chun, Yoon-Seok; Kim, Jongkyu; Ku, Sae-Kwang; Jeon, Suwon; Park, Tae-Sik; Shim, Soon-Mi
• Is Part Of: Journal of functional foods. Volume 72(2020)
• Publication Date: 2020-09
• Subjects: The roasted leaves of Lycium chinense -- Glycosylated kaempferol -- High fat diet obese mice -- Anti-obese effect -- Adiponectin -- AMPK; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2020.104072
• Languages: English
• ISSNs: 1756-4646

Abstract

Graphical abstract: Highlights: Roasted leaves of Lycium chinense (rLF) enhanced glycosylated kaempferol. rLF decreased leptin and sterol response element-binding protein 1c expression. rLF upregulated activity of adiponectin and AMP-activated protein kinase α. It is a potential ingredient to prevent obese-induced type 2 diabetes damages. Abstract: The aim of the study was to elucidate the protective action of roasted Lycium chinense (rLF) enhanced kaempferol glycosides as bioactive components from obese-induced type 2 diabetes mice by investigating the histopathological, biochemical, and transcriptional analyses in blood, liver, and adipose tissue. The rLF extract significantly decreased the hypertrophy of fat deposition, pancreatic hyperplasia, hyperinsulinemia, hepatocellular steatosis, and nephropathy in a dose dependent manner ( p < 0.01). However, rLF increased the expression of adiponectin while decreased leptin and sterol response element-binding protein 1c (SREBP1c) expression. rLF also upregulated the expression of AMP-activated protein kinase α1 (AMPKα1) and AMPKα2. The results from this study suggested that rLF extract could be an effective ingredient to prevent obese-induced type 2 diabetes damages by enhancing both adiponectin-induced signaling and AMPK activity in the liver.