Abstract— Axoplasmic transport in guanethidine sympathectomized and control rats was investigated by monitoring the accumulations of various enzyme activities proximal to a ligature placed on the sciatic nerve. Sympathectomy affected the accumulations of three different mitochondrial enzymes quite differently: the accumulation of monoamine oxidase (MAO, EC 220.127.116.11) activity was inhibited 65% or more, that of hexokinase (HK, EC 18.104.22.168) activity was only inhibited 26%, while accumulation of glutamic dehydrogenase (GDH, EC 22.214.171.124) activity was unaffected by Sympathectomy. Accumulation of AChE (EC 126.96.36.199) activity was depressed 40%, but accumulations of the activities of the lysosomal enzyme, acid phosphatase (acid P'tase, EC 188.8.131.52), and of the cytosolic enzyme, choline acetyltransferase (CAT, EC 184.108.40.206) were unchanged. Despite impressive inhibition of MAO accumulation, the intrinsic activity of this enzyme in sciatic nerve was unaffected by Sympathectomy. The existence in nerve of isozymes of MAO was demonstrated using the inhibitors clorgyline and deprenyl. Transported MAO activity was almost entirely type A; intrinsic activity was 2/3 type A and 1/3 type B. The differential response of the accumulations of the three mitochondrial enzyme activities measured was interpreted to indicate the existence, within neurons, of mitochondria with different enzyme complements.
|Number of pages||5|
|Journal||Journal of Neurochemistry|
|State||Published - Mar 1978|