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ATP citrate lyase in cholinergic nerve endings

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Abstract

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 (S3), synaptosomal (B) and synaptoplasmic (Bs) 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.

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Authors and Affiliations

  1. Department of Clinical Biochemistry Institute of Pathology, Medical Academy, 80-211, Gdansk, Poland

    A. Szutowicz, M. Stcepień, H. Bielarczyk, J. Kabata & W. Lysiak

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  1. A. Szutowicz
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  2. M. Stcepień
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  3. H. Bielarczyk
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  4. J. Kabata
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  5. W. Lysiak
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Szutowicz, A., Stcepień, M., Bielarczyk, H. et al. ATP citrate lyase in cholinergic nerve endings. Neurochem Res 7, 799–810 (1982). https://doi.org/10.1007/BF00965673

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