Analysis of myelin proteins in sympathetic peripheral nerve of adult rats.

Biochemical analyses of myelin proteins in rat sympathetic peripheral nerve were correlated with morphological observations. Myelin proteins in superior cervical ganglia (SCG) and the paravertebral (thoraco-lumbar) chain of ganglia were quantitated by immunoassays and examined qualitatively by Western blotting. The results were compared to those obtained on sciatic nerves from the same animals. In rats aged one year, the concentrations of PO glycoprotein and myelin basic protein (MBP) in SCG were about 1% of those in sciatic nerve, consistent with the relatively low numbers of myelinated fibers in sympathetic nerve. The relative concentration of myelin-associated glycoprotein (MAG) was higher, being 6.7% of that in sciatic nerve. The latter finding is probably due to the greater proportion of MAG-containing membranes (periaxonal, paranodal, and Schmitt-Lanterman incisures) in myelinated fibers of the SCG, in which the internodes are both short and thinly myelinated. The proportion of the 21 kDa, 18 kDa and 17 kDa forms of MBP relative to the 14 kDa form was much higher in SCG than in sciatic nerve, probably reflecting the fact that myelin formation continues actively during adult life in the ganglia, whereas the deposition of myelin is complete at a much earlier age in somatic nerves. The levels of myelin proteins were 2- to 3-fold higher in the paravertebral chain ganglia. These studies indicate that quantitation of myelin proteins in sparsely myelinated sympathetic nerve tissue is feasible and provide a baseline for further studies on the control of myelination in sympathetic nerve during adult life.