Related Experiment Video

Updated: Aug 16, 2025

Measurement of Insulin- and Contraction-Stimulated Glucose Uptake in Isolated and Incubated Mature Skeletal Muscle from Mice
08:01

Measurement of Insulin- and Contraction-Stimulated Glucose Uptake in Isolated and Incubated Mature Skeletal Muscle from Mice

Published on: May 16, 2021

5.9K

Ginsenoside CK improves skeletal muscle insulin resistance by activating DRP1/PINK1-mediated mitophagy

Weili Li1, Haiyang Li1, Lujuan Zheng1

  • 1Engineering Research Center of Glycoconjugates of Ministry of Education, Jilin Provincial Key Laboratory of Chemistry and Biology of Changbai Mountain Natural Drugs, School of Life Sciences, Northeast Normal University, Changchun, China. fanyy033@nenu.edu.cn.

Food & Function
|December 23, 2022
PubMed

Insights

Ginsenoside CK improves skeletal muscle insulin sensitivity, combating hyperglycemia and type 2 diabetes. This compound enhances mitochondrial function and glucose uptake via mitophagy activation.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Metabolic Diseases

Background:

  • Skeletal muscle insulin resistance is a primary driver of type 2 diabetes.
  • Mitochondrial dysfunction is central to skeletal muscle insulin resistance.
  • Ginsenoside CK, a ginseng compound, has potential therapeutic effects, but its mechanism in skeletal muscle insulin resistance is underexplored.

Purpose of the Study:

  • To investigate the effects and underlying mechanisms of Ginsenoside CK on skeletal muscle insulin resistance.

Main Methods:

  • Utilized C2C12 cell models induced by fatty acids.
  • Assessed insulin sensitivity, glucose uptake, and glycogen synthesis.
  • Analyzed mitochondrial dynamics, membrane potential, and mitophagy activation.
  • Investigated the role of DRP1/PINK1 pathway in Ginsenoside CK-induced mitophagy.

Main Results:

  • Ginsenoside CK significantly enhanced skeletal muscle insulin sensitivity, reducing hyperglycemia and insulin resistance.
  • CK improved mitochondrial fusion/fission balance, boosted fatty acid oxidation, and promoted GLUT4 translocation.
  • CK ameliorated mitochondrial membrane potential damage through mitophagy activation, with DRP1/PINK1 identified as the key pathway.

Conclusions:

  • Ginsenoside CK effectively improves skeletal muscle insulin sensitivity by enhancing mitochondrial quality and glucose metabolism.
  • The mechanism involves regulating mitochondrial dynamics and activating mitophagy via the DRP1/PINK1 pathway.
  • Ginsenoside CK shows promise as a therapeutic agent for type 2 diabetes.

More Related Videos

Protection of H9c2 Myocardial Cells from Oxidative Stress by Crocetin via PINK1/Parkin Pathway-Mediated Mitophagy07:40

Protection of H9c2 Myocardial Cells from Oxidative Stress by Crocetin via PINK1/Parkin Pathway-Mediated Mitophagy

Published on: May 26, 2023

1.2K
Glucose Uptake Measurement and Response to Insulin Stimulation in In Vitro Cultured Human Primary Myotubes08:03

Glucose Uptake Measurement and Response to Insulin Stimulation in In Vitro Cultured Human Primary Myotubes

Published on: June 25, 2017

20.1K

Related Concept Videos

Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
1.4K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.8K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
6.5K
Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a...
230