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CASPR2: Identification of new ligands and possible new roles in the central nervous system

Eva N. Rubio-Marrero
B.S., University of Puerto Rico, MayagŁez - 2011

Thesis Advisor: Davide Comoletti, DVM, PhD
Graduate Program in Cell & Developmental Biology

Child Health Institute of NJ (CHINJ)
Room 4101
New Brunswick

Wednesday, April 6, 2016
10:30 a.m.


Contactin-associated protein-like 2 (CNTNAP2) encodes for the protein CASPR2, a multidomain transmembrane protein belonging to the neurexin superfamily that has been implicated in a broad range of phenotypes including autism spectrum disorder and language impairment. Using biochemical and biophysical techniques, we identified CNTN1 as a new CASPR2 ligand and we show that they associate with micromolar affinity. Interestingly, under the same conditions, CASPR2 does not interact with any of the other contactin family members, including its putative ligand, TAG-1 (contactin 2).
Since CNTN1 is expressed by neurons and oligodendrocytes we hypothesize that CASPR2 may have a function in initiating or maintaining the myelination process. Our in vitro experiments suggest that overexpression of CASPR2 in heterologous cells stimulates oligodendrocytes to contact the transfected cells. Moreover, in vitro and in vivo experiments suggest that, in absence of CASPR2, myelination is impaired. A decrease of mature oligodendrocytes found in the corpus callosum of CASPR2 KO brains may explain the myelination defect. If the role of CASPR2 in myelination is confirmed, the molecular details of its function may lead to better diagnostics, prognostics or treatment options for patients with multiple sclerosis.

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