# Proteomic Analysis of Thin Filament Components Elucidates Changes in Spastic Muscle Sarcomere After Stroke

**Authors:** Yun He, Guangrun Liu, Junxi Wu, Xiaolin Jiang, Shengbo Yang

PMC · DOI: 10.3390/ijms262110356 · 2025-10-24

## TL;DR

This study investigates how stroke affects muscle proteins in spastic muscles, identifying specific changes in thin filament proteins over time.

## Contribution

The study provides new insights into the proteomic changes in spastic muscle sarcomeres following a stroke.

## Key findings

- Significant changes in cytoskeletal protein expressions were observed in stroke-affected gastrocnemius muscles.
- Proteomic analysis revealed specific upregulated and downregulated proteins in thin filaments at different post-stroke time points.
- Altered proteins may contribute to changes in spastic muscle sarcomere structure after stroke.

## Abstract

This study analyzed the changes in the composition of thin filaments in spastic muscles after stroke to investigate the mechanism underlying changes in the sarcomeres. Twenty-four rats were randomly divided into four groups: normal, and 3, 6, and 9 days after stroke. A model of post-stroke gastrocnemius muscle spasm was created. Quantitative proteomic procedure and bioinformatics analysis revealed significant changes in cytoskeletal protein expressions in gastrocnemius muscles of each stroke group, particularly those on thin filaments. On the 3rd day after stroke, proteins upregulated within the thin filaments included actin-binding LIM protein 1, tropomyosin 3, leiomodin 2, drebrin-like protein, parvin beta, capping actin protein-gelsolin like, actinin alpha 2, and PDZ-LIM-domain protein 1, while downregulated proteins included tropomyosin 1, gelsolin, actinin alpha 3, and PDZ-LIM-domain protein 7. On the sixth day, upregulation of tropomyosin 2 was newly added while parvin alpha, destrin, PDZ-LIM-domain protein 3, leiomodin 3 were downregulated. On the 9th day, actinin alpha 2, PDZ-LIM-domain protein 7, and cofilin 2 were downregulated. These altered proteins are capable of promoting actin filament elongation and regulating Z-disc growth, and changes in their expression may be responsible for the changes in spastic muscle sarcomere after stroke.

## Linked entities

- **Proteins:** TPM1 (tropomyosin 1), LOC6036071 (gelsolin, cytoplasmic), TPM2 (tropomyosin 2), dstn.S (destrin, actin depolymerizing factor S homeolog), CFL2 (cofilin 2)
- **Diseases:** stroke (MONDO:0005098)
- **Species:** Mus musculus (taxon 10090)

## Full-text entities

- **Genes:** Dstn (destrin, actin depolymerizing factor) [NCBI Gene 502674], Actn2 (actinin alpha 2) [NCBI Gene 291245], Gsn (gelsolin) [NCBI Gene 296654], Dbnl (drebrin-like) [NCBI Gene 83527] {aka Sh3p7, abp1}, Lmod2 (leiomodin 2) [NCBI Gene 296935], Tpm2 (tropomyosin 2) [NCBI Gene 500450], Actn3 (actinin alpha 3) [NCBI Gene 171009], Ablim1 (actin-binding LIM protein 1) [NCBI Gene 307989] {aka RGD1565768}, Parva (parvin, alpha) [NCBI Gene 57341] {aka Actp}, Lmod3 (leiomodin 3) [NCBI Gene 500267] {aka RGD1564924}, Cfl2 (cofilin 2) [NCBI Gene 366624], Parvb (parvin, beta) [NCBI Gene 362973], Tpm3 (tropomyosin 3) [NCBI Gene 117557] {aka TM30nm, Tpm5}
- **Diseases:** muscle spasm (MESH:D013035), Spastic Muscle Sarcomere (MESH:D009128), Stroke (MESH:D020521)
- **Species:** Rattus norvegicus (brown rat, species) [taxon 10116]

## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12610565/full.md

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Source: https://tomesphere.com/paper/PMC12610565