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Updated: Feb 17, 2026

Ex Vivo Assessment of Contractility, Fatigability and Alternans in Isolated Skeletal Muscles
Published on: November 1, 2012
The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during
Changyu Zhou1, Ying Wang1, Daodong Pan1
1Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
Abstract:
Breast muscles of twenty-four Eastern Zhejiang White Geese were randomly divided into three groups: control, Cytochalasin B (Cyt B) and Jasplakinolide (Jasp) treatments during postmortem conditioning. The myofibrillar fraction index (MFI), actin filaments and the levels of F-actin, G-actin and actin associated proteins (cofilins and tropomodulins) during conditioning were investigated. In control, the degraded tropomodulins, increased G-actin and disrupted actin filaments were observed at 4 and 7days; the increase of MFI and decrease of F-actin content were shown during conditioning. Cyt B treatments accelerated the transformation from F-actin to G-actin, weakened actin filaments and increased MFI compared to the control, while Jasp gained the opposite effect against Cyt B. We concluded that depolymerization of actin filaments regulated by tropomodulins contributed to myofibrillar fraction during conditioning. This work provided a new pathway of tenderization by the depolymerization of actin filaments.
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