| Abstract No.: | A-B1059 |
| Country: | Canada |
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| Title: | TESTING THE MINIMAL REQUIREMENTS FOR MYELIN FORMATION IN THE FRUIT FLY, DROSOPHILA MELANOGASTER. |
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| Authors/Affiliations: | 1 Patrick Cafferty*; 1 Vanessa Auld;
1 University of British Columbia, Vancouver, BC, Canada
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| Content: | Rationale: Invertebrate axons are ensheathed by glial cells but lack myelin. The underlying development of glial cells is highly conserved between Drosophila and mammalian glia, including shared mechanisms of differentiation, migration, and sheath formation. The absence of myelin makes the Drosophila nervous system a valuable testing ground to examine the minimal protein requirements necessary to build myelin-like structures. We are testing the potential roles for myelin formation of two transmembrane proteins that appeared early on in the evolution of myelin: Protein Zero (P0) and Proteolipid Protein (PLP) by expressing these proteins in the Drosophila nervous system. Understanding the minimal requirements for myelin formation is required in order to tackle the challenge of regenerating myelin in patients with degenerative disease such as Multiple Sclerosis.
Hypothesis: We hypothesize that expression of P0 or PLP may be sufficient to cause nonmyelinating Drosophila glia to take on more myelin-like structures.
Objectives: To identify the minimal protein requirements for myelin formation
Materials and Methods: We have generated transgenic fly lines that express P0 and PLP. The human genes are under the control of Drosophila glial-specific promoters to drive expression in developing glia.
Results: Western blotting and immunohistochemistry of embryos has shown that P0 and PLP can indeed be expressed in Drosophila. The expression of the human proteins is not toxic to the Drosophila glia and the proteins are correctly targeted to the glial membranes. Our preliminary data suggests that the expression of PLP but not P0 results in an increase in glial membrane adhesion. In a small number of nerve roots in larva that express PLP, we observed a stacking of glial membranes not found in wild-type nerve roots. We will conduct further analysis of P0 and PLP-expressing and wild-type larva to confirm our initial results. Specifically, we will use immunogold labeled antibodies to detect individual glial cells that express P0 or PLP and quantify the number of stained cells that exhibit unusual membrane adhesion structures with TEM.
Conclusion: Our preliminary data suggests that expression of PLP but not P0 is sufficient to increase adhesion of glial cell membranes. |
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