Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging

Huang, Ming; Huang, Feng; Xu, Xinglian; Zhou, Guanghong

doi:10.1016/j.foodchem.2008.11.095

Cited by 64 publications

(46 citation statements)

References 30 publications

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“…With the addition of protease inhibitor cocktail-treated (Group B) and the DEVD-fmk treated samples (Group C), the 30 kDa band could not be readily detected until 7 days post mortem, and only then, it accounted for 9% and 7% of that of actin. This is in accordance with the reports by others (Huang et al 2009). In the ultrasound treated Group D, the rate of troponin-T degradation was increased, and on day 7 post mortem, it amounted to 46%, in Group D while Group F also came up to 31% and 26%, respectively.…”

Section: Protein Degradationsupporting

confidence: 94%

“…Tenderness is affected by the composition, organisation of myofibrillar structure, and by muscle integrity. It has been well established that post mortem degradation of specific myofibrillar proteins is closely linked to the structural changes which result in increased tenderness of meat during aging (Taylor et al 1995;Koohmaraie 1996;Geesink et al 2001;Huang et al 2009). Four major proteolytic enzyme systems have been identified in skeletal muscles causing the degradation of proteins into amino acids or small peptides.…”

mentioning

confidence: 99%

“…Four major proteolytic enzyme systems have been identified in skeletal muscles causing the degradation of proteins into amino acids or small peptides. These are lysosomal and proteasomal systems which result in more general proteolysis, while the calpain and caspase systems (Huang et al 2009;Costelli et al 2005) result in a more limited and specific proteolysis and play an important role during the early post mortem stages.…”

mentioning

confidence: 99%

“…Kemp et al (2006) investigated the relevant expression of various caspase types in different porcine skeletal muscles and reported the direct involvement of the caspase family in meat tenderisation. Moreover, Huang et al (2009) made use of DEVD-CHO (N-acetylAsp-Glu-Val-Asp-CHO), a selective inhibitor of caspase-3, and showed that it dramatically reduced the degradation of the skeletal proteins, such as nebulin, titin, troponin-T, and desmin, while the activity of calpain was not affected. Chen et al (2011) used apoptosis inducers, camptothecin and etoposide as well as Ca 2+ and found that myofibrillar decomposition and proteolysis were both accelerated by the use of each of the three apoptosis inducers.…”

mentioning

confidence: 99%

“…As a result of the high activity of caspase-3 during the early post mortem conditioning period, it is likely that caspase-3 contributes to the degradation of skeletal muscle proteins (Chen et al 2011). Therefore, it has been suggested that the degradation of skeletal muscle proteins should not be solely ascribed to the calpain system, and that the caspase family may play an important role in post mortem tenderisation (Huang et al 2009;Chen et al 2011).…”

mentioning

confidence: 99%

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Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

Xiong¹,

ZhanG²,

ZhanG³

et al. 2012

Czech J. Food Sci.

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The potential contribution of mechanical disruption by ultrasonics and endogenous proteolytic enzymes on the tenderisation of hen muscle were investigated. The importance of endogenous enzymes was evaluated using various specific inhibitors. Freshly obtained breast muscles of culled hens, from the 6 groups investigated were treated with different proteolytic enzyme inhibitors and/or ultrasonics, group was treated with different methods, and then stored at 4°C for 0, 1, 3, and 7 days. Shear force decreased by 1.19 kg, and shear force and cooking loss were reduced by 0.69 kg and 4.27%, respectively, in the incorporated group treatment. The calpastatin activity was affected by all treatments except in the Z-DEVD-fmk-treated group, caspase-3 activity decreased in Z-DEVD-fmk-treated group. Therefore, the results suggest that ultrasonics and endogenous proteases contributed to muscle degradation, thereby improving hen meat tenderness and decreasing the cooking loss. Thus muscle degradation, tenderness, and water-retaining properties of hens were improved by a combination of ultrasound and exogenous proteolytic enzyme inhibitors.

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Section: Protein Degradationsupporting

confidence: 94%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

Xiong¹,

ZhanG²,

ZhanG³

et al. 2012

Czech J. Food Sci.

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Proteomics and metabolomics combined study on endopathic changes of water‐soluble precursors in Tan lamb during postmortem aging

Chen

You

Luo

2022

Food Science & Nutrition

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Tan lamb is highly recommended breed in China. It is of great significance to understand the underlying mechanism of how water‐soluble flavor precursors metabolize in Tan lamb muscles during the postmortem aging period. In this study, we investigated the muscle pH, lactate dehydrogenase (LDH) activity, and the variations in water‐soluble flavor‐related metabolites. The proteome changes were profiled to provide insights into the biochemical changes affecting accumulation of water‐soluble flavor precursors in different aging stages (days 0, 4, and 8). The results indicated that pH value considerably decreased from day 0 to day 4, and increased from day 4 to day 8 (p < .05). The activity of LDH significantly increased from day 0 to day 4, and decreased from day 4 to day 8 (p < .05). Postmortem glycolysis was activated in 4 days, which directly affected the variations in metabolic enzymes and triggered the accumulation of flavor‐related carbohydrates. The free amino acids accumulated due to hydrolysis of structural proteins, with 3‐hydroxy‐L‐proline, aspartic acid, and methionine increasing from day 0 to day 4, and aspartic acid, serine, threonine, tyrosine, phenylalanine, and D‐phenylalanine from day 4 to day 8. The inosine and hypoxanthine accumulated due to the degradation of ATP. The results of the present study provide insightful information, revealing the differences in biochemical attributes in Tan lamb muscles caused by postmortem aging.

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Cells Shrinkage and Phosphatidylserine Externalization in Post Mortem Muscle by Fluorescence Microscopy

Becila¹,

Boudida²,

Gagaoua³

et al. 2016

Springer Proceedings in Physics

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Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging

Cited by 64 publications

References 30 publications

Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

Proteomics and metabolomics combined study on endopathic changes of water‐soluble precursors in Tan lamb during postmortem aging

Cells Shrinkage and Phosphatidylserine Externalization in Post Mortem Muscle by Fluorescence Microscopy

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