ATP citrate lyase in cholinergic nerve endings.

Autor: Szutowicz, A., Stcepień, M., Bielarczyk, H., Kabata, J., Lysiak, W.
Zdroj: Neurochemical Research; Jul1982, Vol. 7 Issue 7, p799-810, 12p
Abstrakt: The activity of ATP-citrate lyase in homogenates of five selected rat brain regions varied from 2.93 to 6.90 nmol/min/mg of protein in the following order: cerebellum < hippocampus < parietal cortex < striatum < medulla oblongata and that of the choline acetyltransferase from 0.15 to 2.08 nmol/min/mg of protein in cerebellum < parietal cortex < hippocampus=medulla oblongata < striatum. No substantial differences were found in regional activities of lactate dehydrogenase, pyruvate dehydrogenase, citrate synthase or acetyl-CoA synthase. High values of relative specific activities for both choline acetyltransferase and ATP-citrate lyase were found in synaptosomal and synaptoplasmic fractions from regions with a high content of cholinergic nerve endings. There are significant correlations between these two enzyme activities in general cytocol (S), synaptosomal (B) and synaptoplasmic (B) fractions from the different regions ( r=0.92-0.99). These data indicate that activity of ATP-citrate lyase in cholinergic neurons is several times higher than that present in glial and noncholinergic neuronal cells. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index