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myo brils (Huff-Lonergan et al. 1996a; Huff-Lonergan and Lonergan, 1999; Carlin et al. 2006). Thus, the proteolytic enzyme -calpain may be, at least in part, responsible for desmin degradation under normal postmortem aging conditions. Whether or not this degradation is truly directly linked to tenderization or is simply an indicator of overall postmortem proteolysis remains to be determined. Filamin Filamin is a large (Mr = 245,000 in skeletal and cardiac muscle) actin-binding protein that exists in numerous cell types (Loo et al. 1998; Thompson et al. 2000; van der Flier et al. 2002). There are several different isoforms of lamin (Hock et al. 1990). The amount of lamin in skeletal and cardiac muscle is very low (approximately 0.1% of the total muscle protein). In skeletal and cardiac muscle, lamin is localized at the periphery of the myo brillar Z-disk, and it may be associated with intermediate laments in these regions (Loo et al. 1998; Thompson et al. 2000; van der Flier et al. 2002). Thus, postmortem degradation of lamin conceivably could disrupt key linkages that serve to help hold myo brils in lateral register. Degradation of lamin may also alter linkages connecting the peripheral layer of myo brils in muscle cells to the sarcolemma by weakening interactions between peripheral myo brillar Z-disks and the sarcolemma via intermediate lament associations or costameres (Robson et al. 1995). A study using myo brils from beef showed that some lamin was degraded to form an approximately 240-kDa degradation product that migrated as a doublet in both myo brils from naturally aged muscle and in -calpaindigested myo brils (Huff-Lonergan et al. 1996a). 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