Hydrolysis of inositol trisphosphate by purified rat brain myelin

Highly purified rat brain myelin was found to hydrolyze inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate, but subsequent hydrolysis of the latter, characteristic of whole brainstem, did not occur. Inositol 1,4,5-trisphosphate 5-phosphatase in myelin was approximately 33% of the level in microsomes and 127% that of the cytosolic fraction from brainstem. The myelin and microsomal enzymes had similar properties, as follows: activation by saponin, requirement for Mg2+ and similar Kact (0.16 and 0.13 mM), Km (8.7 +/- 2.5 and 7.0 +/- 1.0 microM), and pH optima (6.6-6.8). Vmax values were 11.2 +/- 1.0 and 26.3 +/- 2.0 nmol/mg/min for myelin and microsomes, respectively. A possible role for this enzyme in phosphoinositide-mediated signal transduction within myelin and its subcompartments is discussed.