Modification of neuroblastoma X glioma hybrid NG108-15 adenylate cyclase by vanadium ions

David Lichtstein*, Debra Mullikin-Kilpatrick, Arthur J. Blume

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Vanadium ions activate as well as inhibit the activity of the NG108-15 adenylate cyclase in vitro in the absence of any hormone. Below 5mM ion, ortho- and metavanadate activate; the maximal increase in activity is 2-fold. Vanadyl sulfate, at 0.1-0.1mM, activates to a similar magnitude as does vanadate over these concentrations; above 0.1mM, it inhibits. Activation of the enzyme by vanadate is not additive to that induced by PGE1 or NaF. Vanadium ions do not alter the Ka for PGE1-activation, nor the Ki for Dala met amide-inhibition, nor diminish the efficacy of opiate, muscarinic and alpha adrenergic regulation of the enzyme. However, the mechanisms by which NaF and vanadium ions activate must differ. Vanadium, unlike NaF, does not attenuate the ability of hormone receptors to direct inhibition of adenylate cyclase.

Original languageEnglish
Pages (from-to)1157-1165
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume105
Issue number3
DOIs
StatePublished - 14 Apr 1982

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