Ginsenoside Rb1 regulates CPT1A deacetylation to inhibit intramuscular fat infiltration after rotator cuff tear
Yuesong Yin,
Zili Wang,
Yian Yang,
Minren Shen,
Hai Hu,
Chuanshun Chen,
Hecheng Zhou,
Zheng Li,
Song Wu
Affiliations
Yuesong Yin
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Zili Wang
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Yian Yang
Department of Oncology, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Minren Shen
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Hai Hu
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Chuanshun Chen
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Hecheng Zhou
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China
Zheng Li
NHC Key Laboratory of Carcinogenesis, Cancer Research Institute, School of Basic Medical Sciences, Central South University, Changsha, China; Corresponding author
Song Wu
Department of Orthopaedics, The Third Xiangya Hospital, Central South University, No. 138 Tongzipo Road, Changsha 410013, China; Corresponding author
Summary: Fat infiltration (FI) in the rotator cuff muscle is associated with poor clinical outcomes and failed repair of rotator cuff tears (RCTs) in patients. In this study, we aimed to investigate the function of ginsenoside Rb1 in inhibiting FI in muscles after RCT and its underlying molecular mechanism. After TT modeling, mice treated with Rb1 for 6 weeks showed lower FI in the SS muscle compared with mice in the control groups and those treated with other ginsenoside components. Mechanically, Rb1 binds to the NAD+ domain of SIRT1, activating its expression and enzyme activity. This activation stimulates the deacetylation of CPT1A at site K195, thereby promoting fatty acid β-oxidation in adipocyte cells and improving lipolysis. These findings suggest that Rb1 is a potential therapeutic component for improving the outcomes of patients with RCTs.
