Distribution and Degradation of Pork Filamin during Postmortem Aging.
Tongyao DuChao MaZixu WangYuejing HaoWangang ZhangPublished in: Journal of agricultural and food chemistry (2023)
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.
Keyphrases
- induced apoptosis
- cross sectional
- skeletal muscle
- cell death
- gene expression
- endoplasmic reticulum stress
- signaling pathway
- oxidative stress
- type diabetes
- heat shock protein
- insulin resistance
- south africa
- adipose tissue
- high resolution
- hepatitis c virus
- cell proliferation
- transcription factor
- dna binding
- hiv infected
- binding protein
- single molecule