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A Preclinical Model of Sepsis-Induced Myopathy with Disuse in Mice

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BCATm deficiency ameliorates endotoxin-induced decrease in muscle protein synthesis and improves survival in septic

Charles H Lang¹, Christopher J Lynch, Thomas C Vary

¹Department of Cellular and Molecular Physiology, and Surgery, Pennsylvania State University College of Medicine, Hershey, Pennsylvania, USA. clang@psu.edu

American Journal of Physiology. Regulatory, Integrative and Comparative Physiology

|June 18, 2010

Summary

Inhibiting branched-chain amino acid (BCAA) breakdown preserves muscle protein synthesis during sepsis. This strategy, by boosting BCAAs, protects against endotoxin-induced muscle wasting and improves survival in mice.

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Area of Science:

Biochemistry
Physiology
Molecular Biology

Background:

Sepsis and endotoxin (LPS) reduce skeletal muscle protein synthesis by decreasing mammalian target of rapamycin (mTOR) activity.
Branched-chain amino acids (BCAAs) play a crucial role in regulating protein synthesis and mTOR signaling.

Purpose of the Study:

To investigate if inhibiting BCAA catabolism can prevent the decrease in muscle protein synthesis caused by LPS.
To explore the effects of elevated circulating BCAAs on mTOR complex-1 (mTORC1) activity and inflammatory responses in skeletal muscle during sepsis.

Main Methods:

Utilized wild-type (WT) and mitochondrial branched-chain aminotransferase (BCATm) knockout mice.
Administered Escherichia coli LPS or saline to mice and assessed skeletal muscle protein synthesis, mTORC1 signaling pathway components (e.g., 4E-BP1 phosphorylation, protein-protein interactions), and muscle cytokine levels.
Evaluated 7-day survival and muscle mass following polymicrobial peritonitis in WT and BCATm knockout mice.

Main Results:

BCATm knockout mice exhibited higher basal muscle protein synthesis and increased mTORC1 signaling activation compared to WT mice.
LPS administration decreased muscle protein synthesis in WT mice but was significantly blunted in BCATm knockout mice.
In BCATm knockout mice, LPS treatment led to preserved protein synthesis, associated with enhanced 4E-BP1 phosphorylation and specific mTORC1 protein-protein interactions, and reduced muscle cytokine levels.
BCATm knockout mice showed improved survival and preserved muscle mass after polymicrobial sepsis compared to WT mice.

Conclusions:

Elevating circulating BCAAs by inhibiting BCAA catabolism is sufficient to ameliorate the detrimental effects of LPS on skeletal muscle protein synthesis.
This protective effect is mediated through modulation of protein-protein interactions within the mTORC1 complex.
Inhibition of BCAA catabolism may offer a survival advantage during bacterial infections like sepsis.