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February 8, 2026Journal of Cachexia Sarcopenia and Muscle0 citationsOpen Access

Largely Distinct Post‐Translational Modifications Differentiate Skeletal Muscle Wasting Caused by Cancer, Dexamethasone and Aging

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ASAnna StephanFGFlávia A. GraçaSPSuresh Poudel

Key Result

P27 dihydroxylation of Lrpprc declines ~20% in muscle wasting from cancer, dexamethasone, and aging, and mimicking this reduction decreases muscle force by 23-39%.

Key Points

  • The aim is to analyze post-translational modifications in muscle wasting caused by cancer, dexamethasone, and aging.
  • Utilized JUMPptm pipeline to recover modified peptides
  • Conducted tandem mass spectrometry analyses on muscle from mice with different atrophic stimuli
  • Electroporated dihydroxylation-resistant Lrpprc variant into mice to assess muscle force
  • Identified several stimulus-specific post-translational modifications
  • P27 dihydroxylation of Lrpprc decreases under all atrophy stimuli
  • Electroporation of Lrpprc P27A reduces muscle force significantly in both young and old mice
  • Lrpprc P27A impairs expression of muscle strength-related genes
  • Reduced myofibre size observed in old mice with Lrpprc P27A

Structured PICO

P
Population
Mice with skeletal muscle wasting induced by cancer, dexamethasone, and aging
I
Intervention
Electroporation of dihydroxylation-resistant Lrpprc P27A
C
Comparator
Contralateral electroporation of Lrpprc WT or GFP
O
Outcome
Muscle force and post-translational modifications (PTMs)surrogate

A decline in P27 dihydroxylation of Lrpprc is a shared marker of skeletal muscle wasting across diverse catabolic stimuli and contributes to muscle weakness.

Abstract

ABSTRACT Background Skeletal muscle wasting and weakness are prominent disease features. Originally considered to arise from common transcriptional changes, recent analyses demonstrated that different stimuli induce muscle wasting via largely distinct mRNA and protein changes. Methods Here, we examined the post‐translational modifications (PTMs) associated with muscle wasting induced by cancer ( n = 15 078), dexamethasone ( n = 15 078) and aging ( n = 8777) in mice by utilising the JUMPptm pipeline to recover modified peptides from TMT (tandem mass tag) mass spectrometry analyses. Results We find that most PTMs that are significantly regulated are stimulus‐specific and that only a few are cross‐shared ( n = 10; p 0.05) on muscle force in young and old mice. Mechanistically, Lrpprc P27A does not affect proteostasis and mitochondrial function compared to control Lrpprc WT but impairs (> 60% decline; p < 0.05) the expression of genes necessary for muscle strength, including the apelin receptor Aplnr and Col6a2/6 collagens. Moreover, Lrpprc P27A reduces type 2b myofibre size (13% decline; p < 0.01) in old but not in young age. Conclusions These analyses identify atrophy‐associated PTMs that provide refined biomarkers for fingerprinting the atrophic stimulus. Although most PTMs are stimulus‐specific, P27 dihydroxylation of Lrpprc declines during muscle wasting induced by cancer, dexamethasone and aging, suggesting that this is a general atrophy marker. Experimental up‐regulation of the atrophy‐mimicking variant Lrpprc P27A reduces muscle force compared to wild‐type Lrpprc in young and old mice, suggesting that atrophy‐associated P27 dihydroxylation contributes to disease‐associated muscle weakness.

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Cite This Study

Stephan et al. (2026) studied this question. P27 dihydroxylation of Lrpprc declines ~20% in muscle wasting from cancer, dexamethasone, and aging, and mimicking this reduction decreases muscle force by 23-39%.

synapsesocial.com/papers/698828ab0fc35cd7a8848511https://doi.org/10.1002/jcsm.70220
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