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Related Experiment Video

Updated: Apr 25, 2026

Simultaneous Quantification of Selected Kynurenines Analyzed by Liquid Chromatography-Mass Spectrometry in Medium Collected from Cancer Cell Cultures
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Cancer IDO1-Mediated Tryptophan-Kynurenine Metabolic Reprogramming to Drive Skeletal Muscle Atrophy and Cachexia

Leng Han1, Lingjie Jing1, Xinting Zhu1

  • 1Department of Pharmacy, Shanghai Sixth People's Hospital Affiliated Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Journal of Cachexia, Sarcopenia and Muscle
|April 24, 2026
PubMed
Summary

Indoleamine 2,3-dioxygenase 1 (IDO1) drives muscle wasting in cancer cachexia via the tryptophan-kynurenine pathway. Inhibiting IDO1 with palmatine hydrochloride (PAL) effectively mitigates muscle atrophy, offering a potential therapeutic strategy.

Keywords:
cancer cachexiaindoleamine 2,3‐dioxygenase 1kynureninemetabolic reprogrammingmuscle atrophytryptophan

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Area of Science:

  • Oncology
  • Metabolic pathways
  • Muscle biology

Background:

  • Cancer cachexia causes severe skeletal muscle wasting, impacting patient survival and quality of life.
  • Indoleamine 2,3-dioxygenase 1 (IDO1), involved in tryptophan metabolism, is upregulated in cancers, but its role in lung cancer cachexia is unclear.

Purpose of the Study:

  • To investigate the mechanistic role of Ido1 in cancer cachexia.
  • To evaluate the therapeutic potential of Ido1 inhibition for cancer cachexia.

Main Methods:

  • Lewis lung carcinoma (LLC) mouse models with wild-type, Ido1-overexpressing (Ido1-OE), and Ido1-knockout (Ido1-KO) cells were used.
  • In vivo and in vitro studies assessed muscle mass, tumor growth, metabolic changes, and myotube atrophy.
  • Transcriptomic, metabolomic, western blot, and qPCR analyses were performed. The efficacy of Ido1 inhibitor palmatine hydrochloride (PAL) was verified.

Main Results:

  • Ido1-OE exacerbated tumor growth and cachexia, significantly reducing muscle mass and fiber size.
  • Ido1-OE activated pro-inflammatory and protein degradation pathways (MuRF1/Atrogin1) while suppressing anabolic signaling.
  • Tryptophan depletion and kynurenine (Kyn) accumulation were observed; Kyn induced dose-dependent myotube atrophy, reversed by tryptophan supplementation.
  • PAL treatment reduced muscle atrophy and inhibited MuRF1/Atrogin1, while restoring mTOR signaling and myosin heavy chain expression.

Conclusions:

  • IDO1 accelerates muscle atrophy and cancer cachexia through metabolic reprogramming of the tryptophan-kynurenine pathway.
  • Pharmacological inhibition of IDO1 with PAL effectively mitigates cancer cachexia.
  • IDO1 represents a promising therapeutic target for managing cancer cachexia.