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

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 () and Ki-Sun Kwon ()
Additional contact information
Seung-Min Lee: Korea Research Institute of Bioscience and Biotechnology (KRIBB)
Seol Hee Lee: Korea Research Institute of Bioscience and Biotechnology (KRIBB)
Youngae Jung: Korea Basic Science Institute
Younglang Lee: Aventi Inc.
Jong Hyun Yoon: Korea Research Institute of Bioscience and Biotechnology (KRIBB)
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)
Geum-Sook Hwang: Korea Basic Science Institute
Kwang-Pyo Lee: Korea Research Institute of Bioscience and Biotechnology (KRIBB)
Ki-Sun Kwon: Korea Research Institute of Bioscience and Biotechnology (KRIBB)

Nature Communications, 2020, vol. 11, issue 1, 1-15

Abstract: 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.

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-020-19501-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19501-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-19501-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().