Caveolin proteins electrochemical oxidation and interaction with cholesterol

Bioelectrochemistry. 2020 Jun:133:107451. doi: 10.1016/j.bioelechem.2019.107451. Epub 2020 Jan 29.

Abstract

Caveolae consist in lipid raft domains composed of caveolin proteins, cholesterol, glycosphingolipids, and GPI-anchored proteins. Caveolin proteins present three different types, caveolin 1 (CAV-1), caveolin 2 (CAV-2) and caveolin 3 (CAV-3), with a very similar structure and amino acid composition. The native caveolin proteins oxidation mechanism was investigated for the first time, at a glassy carbon electrode, using cyclic, square wave and differential pulse voltammetry. The three native caveolin proteins oxidation mechanism presented only one tyrosine and tryptophan amino acid residues oxidation peak. Denatured caveolin proteins presented also the tyrosine, tryptophan and cysteine amino acid residues oxidation peaks. The reverse cholesterol transport is related to caveolae and caveolin proteins, and CAV-1 is directly connected to cholesterol transport. The influence of cholesterol on the three caveolin proteins electrochemical behaviour was evaluated. In the absence and in the presence of cholesterol, significant differences in the CAV-1 oxidation peak current were observed.

Keywords: Caveolae; Caveolin proteins; Cholesterol; Denaturing agents; Differential pulse voltammetry; Glassy carbon electrode.

MeSH terms

  • Caveolae / metabolism
  • Caveolin 1 / chemistry
  • Caveolin 1 / metabolism*
  • Caveolin 2 / chemistry
  • Caveolin 2 / metabolism*
  • Caveolin 3 / chemistry
  • Caveolin 3 / metabolism*
  • Cholesterol / metabolism*
  • Electrochemical Techniques
  • Humans
  • Oxidation-Reduction
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • CAV1 protein, human
  • CAV2 protein, human
  • CAV3 protein, human
  • Caveolin 1
  • Caveolin 2
  • Caveolin 3
  • Recombinant Proteins
  • Cholesterol