Glycerophosphorylcholine phosphocholine phosphodiesterase activity in cultured oligodendrocytes, astrocytes, and central nervous tissue of dysmyelinating rodent mutants.

The levels of GPC phosphocholine phosphodiesterase, pNP phosphocholine phosphodiesterase, CNPase, and UDP galactose: ceramide galactosyltransferase activities were estimated with pure cultures of oligodendrocytes and astrocytes; mixed primary glial cells cultures; C-6 cells; and CNS tissue of the dysmyelinating md rat, the jimpy mouse, and the quaking mouse. The highest activity of GPC and pNP phosphocholine phosphodiesterases as with CNPase and C gal T was found in the pure cultured oligodendrocytes. C-6 cells had very low or undetectable activities for these two phosphodiesterases but possessed very high CNPase activity. The activity of GPC phosphocholine phosphodiesterase was significantly decreased in the CNS tissue of the md rat and the jimpy and the quaking mouse. Similar reductions were observed for the pNP phosphocholine phosphodiesterase, CNPase, and C gal T activities. The selective cellular enrichment in oligodendrocytes of the GPC phosphocholine phosphodiesterase activity and decreases of its activity in three dysmyelinating mutants in the same ratio as for CNPase and C gal T suggest that GPC phosphocholine phosphodiesterase is a myelin marker enzyme and it may reflect the quantity of myelin and oligodendrocyte present.