The frog neuromuscular junction is a unique model that allowed us to selectively remove cellular components from the neuromuscular junction and create preparations with varying degrees of nerve terminal stability. We found further evidence that frog terminal Schwann cells communicate with their cellular partners, as terminal Schwann cells responded with changes in number or morphology as a result of changes in synaptic integrity. Terminal Schwann cells divided at synaptic sites in response to a regenerating nerve terminal. Terminal Schwann cells also had morphological changes in response to changes in status of their cellular partners; they extended processes in response to removal of the nerve terminal. Orientation and length of these processes was profoundly affected by the presence or absence of muscle fiber and nerve terminal. Similar to observations at the mammalian neuromuscular junction, terminal Schwann cells appear to play a role in reinnervation, as frequently regenerating nerve terminals were within the confines of terminal Schwann cells and their processes. I also investigated the organization of actin within preparations with varying amounts of nerve terminal stability, including developing nerve terminals and regenerating adult nerve terminals that were forming either stable or unstable connections. Previously, F-actin stained target-deprived nerve terminals in a ladder-like pattern and was concentrated in the nonrelease domains (Dunaevsky and Connor 2000). I found that β-actin was similarly distributed and localized to the nonrelease domains of nerve terminals at intact neuromuscular junctions. Further, association of actin with these particular domains appeared to be important for nerve terminal stability. As nerve terminals acquired increasing stability during development, they acquired this domain specific distribution of F-actin. Additionally, although synaptic sites with stable regenerating nerve terminal acquired this ladder-like pattern of F-actin, it was very rare for unstable regenerating nerve terminals to do so. I also tested the dynamic nature of F-actin with pharmacological perturbation. F-actin at nonrelease domains was found to be very stable. This stability of the F-actin based cytoskeleton further suggests that F-actin at the nonrelease domains of nerve terminals may play a role in the stability of motor nerve terminals.
| Identifer | oai:union.ndltd.org:UMASS/oai:scholarworks.umass.edu:dissertations-3825 |
| Date | 01 January 2003 |
| Creators | Kralian, Susan M |
| Publisher | ScholarWorks@UMass Amherst |
| Source Sets | University of Massachusetts, Amherst |
| Language | English |
| Detected Language | English |
| Type | text |
| Source | Doctoral Dissertations Available from Proquest |
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