Date of Award
Doctor of Philosophy
Genetics, Development and Cell Biology
The lan 3-6 monoclonal antibody recognizes a subpopulation of peripheral neurons whose afferents segregate into a single fascicle within the developing leech central nervous system. The lan 3-6 monoclonal antibody was used to isolate a clone encoding a novel protein, calsensin, which contains two EF-hand calcium-binding domains. In situ hybridizations with calsensin riboprobes, Western blots of lan 3-6 monoclonal antibody immunoprecipitations, and immunohistochemistry with polyclonal antibodies generated against a partially-purified calsensin fusion protein confirmed that the sequence encoding the lan 3-6 antigen has been identified. Partially-purified calsensin fusion protein binds [superscript]45Ca[superscript]2+ in vitro, suggesting that the calsensin calcium-binding domains are likely to function in vivo. Immunoaffinity purification with lan 3-6 antibodies resulted in the copurification of a 200,000 M[subscript] r protein with calsensin in two different leech species. Thus the molecular features and interactions of calsensin and its limited distribution to axons forming a single fascicle are consistent with the hypothesis that it may mediate calcium-dependent signal transduction events in the growth cones and axons leading to specific pathway selection.
Digital Repository @ Iowa State University, http://lib.dr.iastate.edu/
Kristen Kay Briggs
Briggs, Kristen Kay, "Calsensin, a novel calcium-binding protein expressed in a subset of peripheral leech neurons fasciculating in a single axon tract " (1995). Retrospective Theses and Dissertations. 10885.