Axoglial Adhesion by Cadm4 Regulates CNS Myelination.

Neuron (2018-12-16)
Nimrod Elazar, Anya Vainshtein, Neev Golan, Bharath Vijayaragavan, Nicole Schaeren-Wiemers, Yael Eshed-Eisenbach, Elior Peles

The initiation of axoglial contact is considered a prerequisite for myelination, yet the role cell adhesion molecules (CAMs) play in mediating such interactions remains unclear. To examine the function of axoglial CAMs, we tested whether enhanced CAM-mediated adhesion between OLs and neurons could affect myelination. Here we show that increased expression of a membrane-bound extracellular domain of Cadm4 (Cadm4dCT) in cultured oligodendrocytes results in the production of numerous axoglial contact sites that fail to elongate and generate mature myelin. Transgenic mice expressing Cadm4dCT were hypomyelinated and exhibit multiple myelin abnormalities, including myelination of neuronal somata. These abnormalities depend on specific neuron-glial interaction as they were not observed when these OLs were cultured alone, on nanofibers, or on neurons isolated from mice lacking the axonal receptors of Cadm4. Our results demonstrate that tightly regulated axon-glia adhesion is essential for proper myelin targeting and subsequent membrane wrapping and lateral extension.

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Product Description

Deoxyribonuclease I from bovine pancreas, lyophilized powder, Protein ≥85 %, ≥400 Kunitz units/mg protein
Bovine Serum Albumin, heat shock fraction, protease free, essentially globulin free, pH 7, ≥98%
N-acetylcysteine amide, ≥98% (HPLC)
Poly-L-lysine hydrobromide, mol wt 70,000-150,000 by viscosity
Hydrocortisone-Water Soluble, BioReagent, suitable for cell culture
D-Lysine, ≥98% (HPLC)
Anti-OPALIN antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

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