Myelin-specific glycoprotein was identified and isolated by using one of lectins, called peanut agglutinin. This myelin-specific glycoprotein showed developmental shift in its expression. It was expressed on the ependymal cells in the fetal brain, disappeared just before the initiation of myelination, and again expressed on myelin structures in the matured brain. Oligodendroglia isolated from rat brain also expressed this glycoprotein. Thus, this glycoprotein is possibly a differentiation marker associated with the process of myelin formation. This glycoprotein showed molecular weights of 130, 000 and 110, 000, and had highly agglutinating nature, which isthe common molecular nature of various adhesive proteins in nervous tissue, such as neural cell adhesive molecule and myelin-associated glycoprotein. These adhesive molecules are considered to be important in the molecular events, such as intercellular interactions and the construction of nervous tissue. Two proteins were found to bind with this glycoprotein in the brain by affinity chromatography. The presence of the specific binding protein suggests that this adhesive myelin-specific glycoprotein is a molecular signal on the surface of myelin membrane.
This myelin glycoprotein was also detected on human cell lines which are derived from T cell leukemia as well as thymocytes. Considering the fact that many other molecules are commonly expressed both in nervous tissue and cells of lymphocyte lineage, these two tissues may be using quite similar set of surface molecules as signals for their histogenesis or functions.
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