The action of stress hormones on the structure and function of erythrocyte membrane

Gen Physiol Biophys. 2015 Jul;34(3):311-21. doi: 10.4149/gpb_2014041. Epub 2015 Mar 2.

Abstract

The action of a mixture of hormones (cortisol and adrenaline) on erythrocyte membrane during their binding was investigated. Changes in the membrane structure were elucidated by atomic force microscopy; microviscosity of the lipid bilayer and changes in the activity of Na(+),K(+)-ATPase at different concentrations of the hormones in erythrocyte suspension were estimated by the fluorescence method. Cortisol and adrenaline were shown to compete for the binding sites. A hormone that managed to bind nonspecifically to the membrane hindered the binding of another hormone. In a mixture of these hormones, cortisol won a competition for the binding sites; therewith, microviscosity of the membranes increased by 25%, which corresponds to a change in microviscosity produced by the action of cortisol alone. The competitive relationships affected also the Na(+),K(+)-ATPase activity, which was indicated by appearance of the second maximum of enzyme activity. It is assumed that an increase in microviscosity of erythrocyte membrane first raises the Na(+),K(+)-ATPase activity due to a growth of the maximum energy of membrane phonons, and then decreases the activity due to hindering of conformational transitions in the enzyme molecule.

MeSH terms

  • Animals
  • Cells, Cultured
  • Drug Combinations
  • Epinephrine / administration & dosage*
  • Erythrocyte Membrane / drug effects
  • Erythrocyte Membrane / metabolism*
  • Erythrocyte Membrane / ultrastructure*
  • Hydrocortisone / administration & dosage*
  • Male
  • Membrane Fluidity / drug effects
  • Membrane Fluidity / physiology*
  • Rats
  • Rats, Wistar
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Structure-Activity Relationship
  • Viscosity

Substances

  • Drug Combinations
  • Sodium-Potassium-Exchanging ATPase
  • Hydrocortisone
  • Epinephrine