| dc.contributor.author | Krueger-Naug, Anne Marie Renee. | en_US |
| dc.date.accessioned | 2014-10-21T12:37:09Z | |
| dc.date.available | 2002 | |
| dc.date.issued | 2002 | en_US |
| dc.identifier.other | AAINQ75701 | en_US |
| dc.identifier.uri | http://hdl.handle.net/10222/55852 | |
| dc.description | Heat shock proteins are a diverse group of evolutionarily conserved proteins that are found in all organisms. The small heat shock protein Hsp27 is constitutively expressed in many neurons of the brainstem and spinal cord, is strongly induced in glial cells in response to ischemia, seizures, or spreading depression, and is selectively induced in peripheral neurons after axotomy. This thesis examined the cell-type specific and stress-dependent expression of Hsp27 in the rat central nervous system following hyperthermic treatment and following transection of the optic nerve. | en_US |
| dc.description | The expression of Hsp27 was examined in brains of adult rats from 1.5 hours to 6 days after brief hyperthermic stress (core body temperature of 42°C for 15 min). Twenty-four hours following hyperthermia, Western blot analysis showed that Hsp27 was elevated in the cerebral cortex, hippocampus, cerebellum and brainstem. Immunohistochemistry for Hsp27 revealed a time-dependent, but transient, increase in the level of Hsp27 immunoreactivity in several types of neuroglia and in specific neuronal populations. The pattern of neuronal Hsp27 immunoreactivity suggests that some of the activated cells are involved in physiological responses related to body fluid homeostasis and temperature regulation. | en_US |
| dc.description | Hsp27 has recently been shown to play a role in sensory neuron survival following peripheral nerve axotomy (Lewis et al., 1999). To investigate the role of Hsp27 in injured central nervous system sensory neurons, the induction and cell-specific expression of Hsp27 was studied in rat retinal ganglion cells from 1--28 days after optic nerve transection. The results of this work demonstrated that transection of the optic nerve induced the expression of Hsp27 in three distinct regions of the rat visual system: sensory retinal ganglion cells in the eye, glial cells of the optic tract, and astrocytes in the optic layer of the superior colliculus. Hsp27 may be associated with enhanced survival of a subset of retinal ganglion cells, providing evidence of a protective role for Hsp27 in central nervous system neuronal injury. | en_US |
| dc.description | In addition, the administration of the neurotrophin BDNF at the time of optic nerve transection was shown to delay retinal ganglion cell death and also to suppress retinal ganglion cell expression of Hsp27. These results indicate that exogenously applied protective molecules may interfere with other endogenous cell survival pathways important for the long-term survival of some neurons following injury. | en_US |
| dc.description | Thesis (Ph.D.)--Dalhousie University (Canada), 2002. | en_US |
| dc.language | eng | en_US |
| dc.publisher | Dalhousie University | en_US |
| dc.publisher | | en_US |
| dc.subject | Biology, Anatomy. | en_US |
| dc.subject | Biology, Neuroscience. | en_US |
| dc.title | Cell type-specific and stress-dependent expression of the small heat shock protein Hsp27 in the adult rat central nervous system. | en_US |
| dc.type | text | en_US |
| dc.contributor.degree | Ph.D. | en_US |
