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Transferrin and ferritin modulate the activity of brain calcium-calmodulin-dependent phosphodiesterase.

Authors
  • Yefimova, M G
  • Shcherbakova, I S
  • Shushakova, N D
Type
Published Article
Journal
Biochemistry. Biokhimii︠a︡
Publication Date
Feb 01, 1997
Volume
62
Issue
2
Pages
165–170
Identifiers
PMID: 9159870
Source
Medline
License
Unknown

Abstract

The effect of the key iron homeostasis proteins transferrin and ferritin on the activity of partially purified brain calcium-calmodulin-dependent phosphodiesterase (CaM-PDE, EC 3.4.1.17) were studied. Transferrin and ferritin were found to be potent natural activators of CaM-PDE. The key factor determining the degree of activation by these proteins is their saturation with iron: apotransferrin activated CaM-PDE 6-7-fold; iron-poor brain ferritin and liver apoferritin (taken for comparison) activated the enzyme 4-5- and 2-fold, respectively. Diferric transferrin and iron-rich liver ferritin had no effects on the enzyme activity. Transferrin and ferritin (both in apo- and iron-saturated forms) did not change the activity of calmodulin-phosphodiesterase complex. The data suggest that apotransferrin and iron-poor transferrin are involved in the regulation of cyclic nucleotide content in nervous tissue.

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