Key result
During postmortem aging of pork, intact 290 kDa FLNC was rapidly degraded to a 280 kDa band, a process that could be inhibited by both μ-calpain and caspase-3 inhibitors.
Why the study?
Filamin C was hypothesized to colocalize with specific binding partners in pork tissues, with calpain and caspase assumed responsible for its postmortem degradation.
Both μ-calpain and caspase-3 are involved in the postmortem degradation of filamin C in porcine skeletal muscle.
FLNC degradation pathways may modulate pork tenderness; leaves open targeted inhibition strategies pending controlled trials.
The filamin C (FLNC) was hypothesized to be colocalized with its certain binding partners in pork tissues and calpain as well as caspase was assumed responsible for the postmortem degradation of FLNC. Therefore, the specific distribution of pork FLNC and its degradation pattern during postmortem aging were investigated in this study. The longissimus thoracis muscles from 12 pigs were removed from the carcasses and then aged at 4 °C for 1, 6, 12, 24, 72, and 168 h, respectively. The FLNC signals appeared to localize in subsarcolemmal areas by cross-sectional images, while the localization was found surrounding the myofibrils at the level of the Z-discs in longitudinal sections. FLNC displayed a highly overlapped spatial colocalization with actin or integrin. Western blot results showed that the intact 290 kDa FLNC was rapidly degraded to produce an approximately 280 kDa band. An almost overlapped distribution pattern was observed between FLNC and μ-calpain or caspase-3 in porcine skeletal muscle cells. Moreover, both the μ-calpain inhibitor and the caspase-3 inhibitor could inhibit the degradation of FLNC in porcine LT muscles during postmortem aging.
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Du et al. (2023) studied Postmortem aging of pork (n=12). Postmortem aging and protease inhibitors was evaluated on FLNC distribution and degradation pattern. During postmortem aging of pork, intact 290 kDa FLNC was rapidly degraded to a 280 kDa band, a process that could be inhibited by both μ-calpain and caspase-3 inhibitors.
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