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| DC Field | Value | Language |
|---|---|---|
| dc.contributor | Widrick, Jeffrey J. | - |
| dc.contributor | Wilcox, Anthony | - |
| dc.contributor | Bella, Deborah | - |
| dc.contributor | Levenson, Rick | - |
| dc.date | 2006-05-23T17:29:31Z | - |
| dc.date | 2006-05-23T17:29:31Z | - |
| dc.date | 2006-04-06 | - |
| dc.date | 2006-05-23T17:29:31Z | - |
| dc.date.accessioned | 2013-10-16T07:36:04Z | - |
| dc.date.available | 2013-10-16T07:36:04Z | - |
| dc.date.issued | 2013-10-16 | - |
| dc.identifier | http://hdl.handle.net/1957/1940 | - |
| dc.identifier.uri | http://koha.mediu.edu.my:8181/xmlui/handle/1957/1940 | - |
| dc.description | Graduation date: 2006 | - |
| dc.description | 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. | - |
| dc.language | en_US | - |
| dc.subject | calpain | - |
| dc.subject | E-64-d | - |
| dc.subject | eccentric muscle damage | - |
| dc.title | Effect of the calpain inhibitor E-64-d on the degradation of α-fodrin in damaged muscle | - |
| dc.type | Thesis | - |
| Appears in Collections: | ScholarsArchive@OSU | |
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