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FABP3-mediated membrane lipid saturation alters fluidity and induces ER stress in skeletal muscle with aging

Author

Listed:
  • Seung-Min Lee

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB))

  • Seol Hee Lee

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB)
    Korea University of Science and Technology)

  • Youngae Jung

    (Korea Basic Science Institute)

  • Younglang Lee

    (Aventi Inc.)

  • Jong Hyun Yoon

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB)
    Korea University of Science and Technology)

  • Jeong Yi Choi

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB))

  • Chae Young Hwang

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB))

  • Young Hoon Son

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB))

  • Sung Sup Park

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB)
    Korea University of Science and Technology)

  • Geum-Sook Hwang

    (Korea Basic Science Institute)

  • Kwang-Pyo Lee

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB)
    Korea University of Science and Technology
    Aventi Inc.)

  • Ki-Sun Kwon

    (Korea Research Institute of Bioscience and Biotechnology (KRIBB)
    Aventi Inc.
    Korea University of Science and Technology)

Abstract

Sarcopenia is characterized by decreased skeletal muscle mass and function with age. Aged muscles have altered lipid compositions; however, the role and regulation of lipids are unknown. Here we report that FABP3 is upregulated in aged skeletal muscles, disrupting homeostasis via lipid remodeling. Lipidomic analyses reveal that FABP3 overexpression in young muscles alters the membrane lipid composition to that of aged muscle by decreasing polyunsaturated phospholipid acyl chains, while increasing sphingomyelin and lysophosphatidylcholine. FABP3-dependent membrane lipid remodeling causes ER stress via the PERK-eIF2α pathway and inhibits protein synthesis, limiting muscle recovery after immobilization. FABP3 knockdown induces a young-like lipid composition in aged muscles, reduces ER stress, and improves protein synthesis and muscle recovery. Further, FABP3 reduces membrane fluidity and knockdown increases fluidity in vitro, potentially causing ER stress. Therefore, FABP3 drives membrane lipid composition-mediated ER stress to regulate muscle homeostasis during aging and is a valuable target for sarcopenia.

Suggested Citation

  • Seung-Min Lee & Seol Hee Lee & Youngae Jung & Younglang Lee & Jong Hyun Yoon & Jeong Yi Choi & Chae Young Hwang & Young Hoon Son & Sung Sup Park & Geum-Sook Hwang & Kwang-Pyo Lee & Ki-Sun Kwon, 2020. "FABP3-mediated membrane lipid saturation alters fluidity and induces ER stress in skeletal muscle with aging," Nature Communications, Nature, vol. 11(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19501-6
    DOI: 10.1038/s41467-020-19501-6
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    Cited by:

    1. Jin-Hyuck Jeong & Jun-Seok Han & Youngae Jung & Seung-Min Lee & So-Hyun Park & Mooncheol Park & Min-Gi Shin & Nami Kim & Mi Sun Kang & Seokho Kim & Kwang-Pyo Lee & Ki-Sun Kwon & Chun-A. Kim & Yong Ryo, 2023. "A new AMPK isoform mediates glucose-restriction induced longevity non-cell autonomously by promoting membrane fluidity," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Justin G. Boyer & Jiuzhou Huo & Sarah Han & Julian R. Havens & Vikram Prasad & Brian L. Lin & David A. Kass & Taejeong Song & Sakthivel Sadayappan & Ramzi J. Khairallah & Christopher W. Ward & Jeffery, 2022. "Depletion of skeletal muscle satellite cells attenuates pathology in muscular dystrophy," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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