Melatonin synchronizes protein synthesis rhythm in hepatocyte cultures as an agonist of intercellular calcium and protein kinases

Melatonin in nanomolar concentrations synchronizes protein synthesis in primary cultures of hepatocytes through calcium-dependent activation of protein kinases. The synchronizing effect of melatonin is blocked by the cytoplasmic calcium chelating agent BAPTA-AM (20 μM) as well as by the inhibitor of...

Full description

Saved in:
Bibliographic Details
Published inRussian journal of developmental biology Vol. 40; no. 3; pp. 183 - 187
Main Authors Brodsky, V. Ya, Golichenkov, V. A., Zvezdina, N. D., Fateeva, V. I., Mal’chenko, L. A.
Format Journal Article
LanguageEnglish
Published Dordrecht SP MAIK Nauka/Interperiodica 01.05.2009
Subjects
Animal Anatomy
Biomedical and Life Sciences
Cytology of Development
Developmental Biology
Histology
Life Sciences
Morphology
rhythm of protein synthesis
cell-cell communication
melatonin
melatonin receptors
cell self-organization
hepatocytes
Online AccessGet full text

Cover

More Information
Summary:Melatonin in nanomolar concentrations synchronizes protein synthesis in primary cultures of hepatocytes through calcium-dependent activation of protein kinases. The synchronizing effect of melatonin is blocked by the cytoplasmic calcium chelating agent BAPTA-AM (20 μM) as well as by the inhibitor of protein kinases 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine dihydrochloride (40 μM). Thus, protein phosphorylation is the key event in hepatocyte synchronization by melatonin, as we have demonstrated previously for gangliosides and biogenic amines. The antagonist of melatonin receptors luzindole (20 nM) blocks the synchronizing function of melatonin.
ISSN:1062-3604
1608-3326
DOI:10.1134/S1062360409030084