μ-Calpain is involved in the postmortem proteolysis of gizzard smooth muscle

Chang, Ya‐Shiou; Stromer, Marvin H.; Chou, Rong‐Ghi R.

doi:10.1016/j.foodchem.2013.01.075

Cited by 16 publications

(12 citation statements)

References 29 publications

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“…The loss of the native band (alpha-tubulin) and the detection of degradation products (GAPDH, alpha-actinin) occurred in a similar manner and particularly in late PMIs. These findings confirm results of previous studies with different species such as pigs [ 36 ], mice [ 10 ], rats [ 37 , 39 ], geese and ducks [ 40 ], and also humans [ 10 , 25 ].…”

Section: Discussionsupporting

confidence: 91%

Dismembered porcine limbs as a proxy for postmortem muscle protein degradation

et al. 2021

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The estimation of the postmortem interval (PMI) is of critical importance in forensic routine. The most frequently applied methods, however, are all restricted to specific time periods or must be excluded under certain circumstances. In the last years it has been shown that the analysis of muscle protein degradation has the potential to contribute to according delimitations in practice. In particular, upon biochemical analysis, the specific time points of degradation events provide reasonable markers for PMI delimitation. Nevertheless, considerable research is yet required to increase the understanding of protein decomposition and how it is affected by individual and environmental influencing factors. This is best investigated under standardized conditions, however, a considerate selection of proxies, regarding costs, effort, and expected outcome is required. Here, we use pigs to compare muscle protein decomposition in whole bodies and dismembered body parts (amputated hind limbs). Not only do experiments on body parts reduce the costs and allow easier handling in basic research, but also they aid to investigate the practical application of PMI estimation in dismembered body parts, or other extensive injuries, which are not unusual scenarios in crime investigation. Specifically, we investigated whether there are differences in the degradation rates of selected muscle proteins, sampled from dismembered legs and from hind limbs attached to whole pig bodies. Our results show distinct time-dependent degradation patterns of muscle proteins in a predictable manner regardless of sample origin. We are able to demonstrate that amputated hind limbs are suitable proxies for the analysis of muscle protein degradation, especially to investigate certain influencing factors and establish according standardized models.

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Section: Discussionsupporting

confidence: 91%

Dismembered porcine limbs as a proxy for postmortem muscle protein degradation

et al. 2021

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“…Also, unautolyzed (upper) and autolyzed (lower) calpain-1 show in BM samples (Figure 3), similar to previous studies in porcine (Pomponio & Ertbjerg, 2012;Pomponio et al, 2008) and goose (Chang et al, 2019) muscle. The putative calpain-2 band is similar to a band reported in previous studies of goose gizzard smooth muscle (Chang, Stromer, & Chou, 2013).…”

Section: Calpain Activity In 0-day Bm and Lm Samplessupporting

confidence: 86%

Calpain activation and proteolysis in postmortem goose muscles

Chang

Stromer

et al. 2020

Animal Science Journal

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Meat tenderness is considered as the most important criterion for meat quality by consumers and can be improved by the actions of endogenous proteases, mainly calpains, during postmortem storage at 0-5°C. The purpose of this study, therefore, was to examine the postmortem calpain activation and proteolysis in breast (BM) and leg and thigh (LM) muscles of White Roman goose. BM and LM were taken from goose carcasses (n = 15) at 0 (10-15 min postmortem), 1, 3, and 7 days of storage at 5°C. The decrease in postmortem pH, calpain-1 and-11 activities, and contents of the calpain-1 80 kDa subunit and desmin was more rapid (p < .05) in BM than in LM. Our results show that postmortem proteolysis was more extensive in BM than in LM of White Roman goose, not only because the difference in fiber type composition between two muscles, but because the rate and extent of calpain activation were greater in BM as well. These results may provide useful information to optimize meat processing for different muscles in goose industry.

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“…When sufficient free Ca 2+ is provided after slaughter, the calpains will be activated. In poultry, l-calpain was more sensitive to Ca 2+ than that in livestock and its activation and autolysis have been reported (Chang & Chou 2012;Chang et al 2013). Therefore, m-calpain is believed unlikely to play a role in postmortem tenderization of mammals Goll et al 2003).…”

Section: Introductionmentioning

confidence: 96%

“…Therefore, m-calpain is believed unlikely to play a role in postmortem tenderization of mammals Goll et al 2003). In poultry, l-calpain was more sensitive to Ca 2+ than that in livestock and its activation and autolysis have been reported (Chang & Chou 2012;Chang et al 2013). Moreover, unlike m-calpain in mammals, the Ca 2+ requirements for activating l/m-calpain could be within physiological Ca 2+ concentrations in chicken muscle during aging, which means it could be activated and play a part in meat quality changes Melody et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Involvement of μ/m‐calpain in the proteolysis and meat quality changes during postmortem storage of chicken breast muscle

Zhao

Xing

Huang

et al. 2017

Animal Science Journal

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The objective of this study was to investigate the role of calpain isotypes, especially poultry-specific μ/m-calpain in the proteolysis and meat quality changes of chicken breast muscle during postmortem storage. Calpain activity was detected by casein zymography, while the degradation of titin, desmin and Troponin-T was analyzed by sodium dodecyl sulfate - polyacrylamide gel electrophoresis and western blot. Meat quality indicators such as water holding capacity and tenderness were also studied. The correlation analysis between calpain activity, proteolysis and the changes in meat quality indicators indicated that there were strong correlations for μ-calpain during the first 12 h of storage, while such strong correlations for μ/m-calpain were only found in samples stored from 12 h to 7 days. Our study suggested that μ-calpain played a major role in meat quality changes while μ/m-calpain could also be involved but played a limited role in the proteolysis and meat quality changes during 12 h to 7 days postmortem storage of chicken breast muscle.

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μ-Calpain is involved in the postmortem proteolysis of gizzard smooth muscle

Cited by 16 publications

References 29 publications

Dismembered porcine limbs as a proxy for postmortem muscle protein degradation

Dismembered porcine limbs as a proxy for postmortem muscle protein degradation

Calpain activation and proteolysis in postmortem goose muscles

Involvement of μ/m‐calpain in the proteolysis and meat quality changes during postmortem storage of chicken breast muscle

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