Kaempferol-Enhanced Migration and Differentiation of C2C12 Myoblasts via ITG1B/FAK/Paxillin and IGF1R/AKT/mTOR Signaling Pathways.

Autor: Hour TC; Department of Biochemistry, School of Medicine, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan.; Department of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung, 807378, Taiwan., Lan Nhi NT; Department of Biochemistry, School of Medicine, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan., Lai IJ; Department of Nutrition, I-Shou University, Kaohsiung, 82445, Taiwan., Chuu CP; Institute of Cellular and System Medicine, National Health Research Institutes, Miaoli County, 350401, Taiwan., Lin PC; Department of Oral Hygiene, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan., Chang HW; Department of Biochemistry, School of Medicine, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan., Su YF; Department of Biochemistry, School of Medicine, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan., Chen CH; Orthopaedic Research Center and Department of Orthopedics, Kaohsiung Medical University Hospital and Kaohsiung Municipal Ta-Tung Hospital, Kaohsiung Medical University, Kaohsiung, 807378, Taiwan., Chen YK; Department of Nutrition, I-Shou University, Kaohsiung, 82445, Taiwan.
Jazyk: angličtina
Zdroj: Molecular nutrition & food research [Mol Nutr Food Res] 2024 Jul; Vol. 68 (14), pp. e2300685. Date of Electronic Publication: 2024 Jun 11.
DOI: 10.1002/mnfr.202300685
Abstrakt: Scope: Kaempferol (KMP), a bioactive flavonoid compound found in fruits and vegetables, contributes to human health in many ways but little is known about its relationship with muscle mass. The effect of KMP on C2C12 myoblast differentiation and the mechanisms that might underlie that effect are studied.
Methods and Results: This study finds that KMP (1, 10 µM) increases the migration and differentiation of C2C12 myoblasts in vitro. Studying the possible mechanism underlying its effect on migration, the study finds that KMP activates Integrin Subunit Beta 1 (ITGB1) in C2C12 myoblasts, increasing p-FAK (Tyr398) and its downstream cell division cycle 42 (CDC42), a protein previously associated with cell migration. Regarding differentiation, KMP upregulates the expression of myosin heavy chain (MHC) and activates IGF1/AKT/mTOR/P70S6K. Interestingly, pretreatment with an AKT inhibitor (LY294002) and siRNA knockdown of IGF1R leads to a decrease in cell differentiation, suggesting that IGF1/AKT activation is required for KMP to induce C2C12 myoblast differentiation.
Conclusion: Together, the findings suggest that KMP enhances the migration and differentiation of C2C12 myoblasts through the ITG1B/FAK/paxillin and IGF1R/AKT/mTOR pathways. Thus, KMP supplementation might potentially be used to prevent or delay age-related loss of muscle mass and help maintain muscle health.
(© 2024 Wiley‐VCH GmbH.)
Databáze: MEDLINE
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