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Related Experiment Videos

Calreticulin-melatonin. An unexpected relationship.

Manuel Macías1, Germaine Escames, Josefa Leon

  • 1Departamento de Fisiología and Instituto de Biotecnología, Universidad de Granada, Avenida de Madrid 11, E-18012 Granada, Spain.

European Journal of Biochemistry
|February 27, 2003
PubMed
Summary

Researchers identified specific nuclear melatonin binding sites in rat liver cells. They discovered that calreticulin is a novel, high-affinity melatonin receptor involved in genomic regulation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Endocrinology

Background:

  • Melatonin is known to affect cellular functions at the nuclear level.
  • Specific melatonin binding sites have been previously identified in the rat liver cell nucleus.

Purpose of the Study:

  • To identify and characterize nuclear melatonin binding sites in rat hepatocytes.
  • To determine the molecular identity of proteins that bind melatonin within the cell nucleus.

Main Methods:

  • Nuclear extracts from rat hepatocytes were purified using ammonium sulfate precipitation and affinity chromatography.
  • Ligand blot analysis was used to identify melatonin-binding polypeptides.
  • N-Terminal sequencing, Western blot analysis, and binding kinetics with recombinant calreticulin were performed.

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Main Results:

  • Two melatonin-binding polypeptides of approximately 60 kDa and 74 kDa were identified.
  • The 60 kDa protein showed high homology to rat calreticulin.
  • Calreticulin demonstrated high-affinity melatonin binding (Kd = 1.08 +/- 0.2 nm).

Conclusions:

  • Calreticulin represents a novel class of high-affinity melatonin binding sites.
  • These findings suggest calreticulin's role in melatonin's genomic regulatory functions.
  • The study provides evidence for melatonin's direct action at the nuclear level via calreticulin.