Differential effect of colchicine upon the entry of proteins into myelin and myelin related membranes.

Brain slices from 20 day old rats were incubated with radioactive aminoacids in the presence and absence of 500 microM colchicine and the appearance of labeled proteins in myelin and in a myelin-like fraction (SN4 fraction) was measured. In the presence of the inhibitor, the entry of proteolipid proteins was decreased to 55% in myelin and to 45% in SN4 fraction with reference to control values while the entry of basic proteins and other minor protein components was unaffected in both fractions. The synthesis of proteolipid proteins was not affected by the presence of colchicine; moreover, a slight accumulation of these proteins was observed in microsomes. The results suggest that the microtubular system is involved in the transport of proteolipid proteins from their site of synthesis to their site of deposition and that the various types of myelin proteins follow different transport routes to enter into this special type of membrane.