TitleThe role of E-cadherin in the regulation of myelination in the peripheral nervous system
NameDesai, Darshan (author), Kim, Haesun A (chair), Friedman, Wilma j (internal member), Jonakait, G. Miller (internal member), Melendez-Vasquez, Carmen V (outside member), Rutgers University, Graduate School - Newark,
DescriptionIn the mammalian nervous system, saltatory conduction is necessary for rapid velocities of action potentials down long axonal trunks. Myelination is the key to this near instantaneous transmission of signals. Oligodendrocytes of the central nervous system and Schwann cells of the peripheral nervous system, are the cells that myelinate axons. While there is some understanding of how these cells concentrically wrap their plasma membranes around the axon to form this insulative layer, the precise induction mechanism is not clearly determined. A potential molecule involved in this process is E-cadherin, which has been previously identified to be localized to regions of compact myelin and various adhesion enriched areas. This study focuses on the role of E-cadherin, a member of the classical cadherin family of calcium dependent adhesion molecules, and its role in the initiation of myelination in the Schwann cells. Protein lysates of rat sciatic nerve demonstrate that expression of E-cadherin was shown to increase with development and that E-cadherin associated with ErbB2, a receptor tyrosine kinase known to function in Schwann cell development, promotes proliferation and myelination. Knockdown of E-cadherin has a negative effect on myelination in vitro, while ectopic expression of E-cadherin induces myelination. Additionally, upon perturbation of beta catenin binding to E-cadherin, enhanced proliferation and myelination was observed. This enhancement was found specifically in Superior Cervical Ganglion neurons (SCG), suggesting that beta-catenin coupling may also have an effect in myelination through an un-determined cadherin-catenin mechanism. These results suggest that cadherins have a critical role in the complex process of myelination.
NoteIncludes bibliographical references
Noteby Darshan J. Desai
CollectionGraduate School - Newark Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.