PMID: 6162913Mar 1, 1981Paper

Ca2+- or Mg2+-stimulated ATPase activity in bullfrog spinal nerve: relation to Ca2+ requirements for fast axonal transport

Journal of Neurochemistry
R Hammerschlag, J A Bobinski

Abstract

Adenosine triphosphatase (ATPase) activity stimulated by Ca2+ or Mg2+ was characterized in spinal nerve and spinal sensory ganglion of bullfrog. Enzyme activity of homogenates from both sources reached a maximum at a 1-2 mM concentration of either cation, although the level of maximal activity in nerve trunks was approximately twice that in ganglia. Enzyme activation was not observed with 2 mM-Sr2+ or Ba2+. Co2+ or Mn2+, at 2 mM, depressed Ca2+ activation of the enzyme by 50-60% in nerve but had no inhibitory effect on ganglia activity. In intact spinal ganglion/spinal nerve preparations, incubated for 20 h in medium containing 0.2 mM-Co2+, no effect was detected on Ca2+/Mg2+ ATPase activity in ganglia or nerve trunks whereas fast axonal transport was inhibited by 80%. Incubation in medium containing 0.02 mM-Hg2+ depressed enzyme activity in ganglia by 64% and in nerve trunks by 44%, whereas fast transport was again inhibited by 80%. When only nerve trunks were exposed to these ions, Hg2+ but not Co2+ was observed to slow the rate of fast axonal transport. The divalent cation specificity of the Ca2+/Mg2+ ATPase activity is distinct from the ion specificities, determined in previous work, of the Ca2+ requirement during initiatio...Continue Reading

References

Mar 14, 1975·Brain Research·A Edström, H Mattsson
Apr 18, 1975·Science·R HammerschlagA Y Chiu
Dec 3, 1976·Brain Research·M WakabayashiY Takahashi
Dec 13, 1974·Brain Research·M A Khan, S Ochs
Apr 1, 1967·Archives of Biochemistry and Biophysics·Y NakamaruK Konishi
Apr 1, 1959·Biochimica Et Biophysica Acta·B B MARSH

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Citations

Mar 1, 1982·Journal of Neurochemistry·G Shecket, R J Lasek
Sep 1, 1982·Journal of Neurochemistry·L Larivière, P A Lavoie

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