Protein and glycoprotein composition of myelin subfractions from the developing rat optic nerve and tract.

Abstract

Abstract: The rat optic nerve and tract (representing a relatively homogeneous part of the CNS) were utilised for a detailed examination of the protein and glycoprotein composition of developing myelin membranes. Animals aged from 5 days through to adulthood were used. Myelin fractions could first be isolated from the nerve 8 days after birth and the yield increased until 60 days of age, before declining slightly to the adult level; a similar (but possibly slightly delayed) pattern was apparent for the optic tract. The homogeneity of optic nerve myelin (compared with that from brain and spinal cord) was demonstrated by zonal centrifugation on continuous sucrose‐density gradients; myelin from both 20‐day and adult animals exhibited narrow, Gaussian‐like distributions, with 19–22% of the total myelin at the population modes. During development, the myelin density profile was shifted to a denser region of the sucrose gradients. Micro‐polyacrylamide gel electrophoretic analyses of “light” and “heavy” myelin subfractions from both optic nerve and tract indicated that the gross developmental changes in protein composition were similar to those previously described for myelin prepared from larger CNS areas, particularly the forebrain. The glycoprotein components of the myelin fractions were stained directly on micro‐gels using fluorescein isothiocyanate‐labelled concanavalin A. The relative proportion of the major high‐molecular‐weight glycoprotein decreased rapidly during the early phases of myelination. A number of lower‐molecular‐weight glycoproteins were also apparent; the proportions of these varied during development and in light and heavy myelin subfractions, but definitive data are not available to determine whether they are components of the myelin sheath or of contaminating membranes.