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  • Title: Calmodulin-dependent spectrin kinase activity in resealed human erythrocyte ghosts.
    Author: Nelson MJ, Daleke DL, Huestis WH.
    Journal: Biochim Biophys Acta; 1982 Apr 07; 686(2):182-8. PubMed ID: 6805511.
    Abstract:
    Membrane protein phosphorylation has been studied in resealed human erythrocyte ghosts by measuring the incorporation of 32P into spectrin and band 3. Norepinephrine- and Ca2+-stimulated phosphate incorporation was diminished in ghosts depleted of calmodulin. Ghosts prepared with endogenous calmodulin showed Ca2+- and norepinephrine-stimulated protein phosphorylation only when the ghosts had been resealed in the presence of (gamma-32P)ATP. Ghosts resealed with or without calmodulin in the presence of unlabeled ATP showed no net gain or loss of 32P when exposed to norepinephrine or a Ca2+-specific ionophore. These observations suggest that Ca2+ and norepinephrine stimulation of membrane protein phosphorylation is mediated by calmodulin-dependent spectrin kinase activity, and not by increased turnover of spectrin ATPase or by inhibition of phosphospectrin phosphatase.
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