2018
DOI: 10.1016/j.meatsci.2018.03.002
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A new insight into meat toughness of callipyge lamb loins - The relevance of anti-apoptotic systems to decreased proteolysis

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Cited by 39 publications
(22 citation statements)
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“…Accordingly, our results showed higher intensity of HSPB1 band in the myofibrillar subproteome of meat from the E-NM treatment, which was the treatment that showed higher WBSF, and thus a lower tenderization rate. Moreover, the evolution of HSPB1 along meat ageing is in agreement with previous studies in bovine muscles [ 50 , 64 , 65 ] that have demonstrated that muscle HSPB1 increases in abundance shortly after slaughter but decreases during meat storage. Similarly, our results showed a significant decrease ( p < 0.001) of the large HSPA1A with post-mortem ageing.…”
Section: Resultssupporting
confidence: 91%
“…Accordingly, our results showed higher intensity of HSPB1 band in the myofibrillar subproteome of meat from the E-NM treatment, which was the treatment that showed higher WBSF, and thus a lower tenderization rate. Moreover, the evolution of HSPB1 along meat ageing is in agreement with previous studies in bovine muscles [ 50 , 64 , 65 ] that have demonstrated that muscle HSPB1 increases in abundance shortly after slaughter but decreases during meat storage. Similarly, our results showed a significant decrease ( p < 0.001) of the large HSPA1A with post-mortem ageing.…”
Section: Resultssupporting
confidence: 91%
“…Finally, a recent topic of research attracting attention is the impact of apoptotic factors in the activity of calpain and calpastatin. Molecules such as cytochrome C and caspases have been related with sheep meat tenderness and the activation of the calpain/calpastatin system, since an overexpression of these factors leads to tender meat [ 76 ]. On the other hand, heat shock proteins (HSP), when overexpressed, were associated with an increment in sheep toughness.…”
Section: Early Post-mortem Intervention Impact On Sheep Meat Tendernessmentioning
confidence: 99%
“…Moreover, small heat shock proteins (sHSPs) are chaperone proteins produced by organism, which play a protective role in anti-apoptotic activity (Ba et al 2015). sHSPs have been found to be involved in the delay of the ageing tenderising process (i.e., contributing to meat toughness) by inhibiting the onset of apoptosis via possible interactions with multiple apoptotic cascades (e.g., binding directly to Cytc and caspase-3) (Cramer et al 2018). However, its variable expressions in muscles with different ultimate pH (pHu) need further studies (Lomiwes et al 2014a).…”
Section: Ageing Tenderisationmentioning
confidence: 99%