Effect of the calpain inhibitor E-64-d on the degradation of α-fodrin in damaged muscle Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/rb68xh148

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  • We hypothesized that calpain activity is elevated in response to muscle damage. To test this hypothesis, we examined the degradation of α-fodrin into its 150 and 145 kDa fragments following either 20 eccentric or isometric contractions. In addition, experiments were performed in the presence or absence of E-64-d, a calpain inhibitor. Both EDL and SOL muscles displayed significant differences (p<0.003 and p<0.002 respectively) between the raw and normalized 150 and 145 kDa α-fodrin fragments of the DMSO + E-64-d compared to the other bath treatments. Based on our model of exercise-induced muscle damage, we expected to see greater levels of 150 and 145 kDa α-fodrin fragments in those muscles that performed the eccentric protocol. However, there was no evidence that eccentric muscle damage increased the levels of 150 and 145 kDa α-fodrin fragments over the levels observed in the isometric trials. These findings suggest that the magnitude of damage was insufficient to activate calpains.
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  • description.provenance : Approved for entry into archive by Julie Kurtz(julie.kurtz@oregonstate.edu) on 2006-05-16T19:08:34Z (GMT) No. of bitstreams: 1 Jeff Boyd-Thesis.pdf: 464645 bytes, checksum: 2c561e75c8c7b7c30709708272e65fef (MD5)
  • description.provenance : Made available in DSpace on 2006-05-23T17:29:31Z (GMT). No. of bitstreams: 1 Jeff Boyd-Thesis.pdf: 464645 bytes, checksum: 2c561e75c8c7b7c30709708272e65fef (MD5)
  • description.provenance : Submitted by Jeffrey Boyd (boydje@onid.orst.edu) on 2006-05-05T18:24:54Z No. of bitstreams: 1 Jeff Boyd-Thesis.pdf: 464645 bytes, checksum: 2c561e75c8c7b7c30709708272e65fef (MD5)

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