Caveolin proteins electrochemical oxidation and interaction with cholesterol
| Autor: | Isabel P.G. Fernandes, Ana Maria Oliveira-Brett |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Caveolin 3
Caveolin 2 Caveolin 1 Biophysics 02 engineering and technology Caveolae 01 natural sciences Electrochemistry Humans Physical and Theoretical Chemistry Tyrosine Lipid raft Chemistry 010401 analytical chemistry Reverse cholesterol transport Tryptophan General Medicine Electrochemical Techniques 021001 nanoscience & nanotechnology Recombinant Proteins 0104 chemical sciences Cholesterol cardiovascular system lipids (amino acids peptides and proteins) 0210 nano-technology Oxidation-Reduction |
| Zdroj: | Bioelectrochemistry (Amsterdam, Netherlands). 133 |
| ISSN: | 1878-562X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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