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A spin-label study on human high density lipoprotein.

M Kanashiro, R Miura, T Yamano

    Journal of Biochemistry
    |March 1, 1985
    PubMed
    Summary
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    Spin labeling of high density lipoproteins (HDL) with NEM-TEMPO revealed distinct immobilization patterns. Covalent binding to apolipoprotein A-I showed reversible temperature changes, while noncovalent binding demonstrated irreversible changes above 25°C.

    Area of Science:

    • Biochemistry
    • Lipid Metabolism
    • Spectroscopy

    Background:

    • High density lipoproteins (HDL) are crucial for reverse cholesterol transport.
    • Understanding HDL structure and protein interactions is vital for cardiovascular health.
    • Spin labeling offers a method to probe molecular dynamics and binding sites.

    Purpose of the Study:

    • To investigate the binding characteristics and dynamics of N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)maleimide (NEM-TEMPO) with human plasma HDL.
    • To differentiate between covalent and noncovalent binding of NEM-TEMPO to HDL components.
    • To characterize the temperature-dependent behavior and activation energy of NEM-TEMPO binding to HDL.

    Main Methods:

    • Human plasma HDL was labeled with NEM-TEMPO.

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  • Electron spin resonance (ESR) spectroscopy was used to analyze spin-labeled HDL.
  • Temperature-dependent changes in ESR spectra were monitored.
  • The effect of 2,4,6-trinitrobenzene sulfonic acid (TNBS) on binding was assessed.
  • Ascorbate reduction was used to evaluate bound spin labels.

    • Main Results:

    • ESR spectra showed both strongly and weakly immobilized NEM-TEMPO components.
    • Strongly immobilized component (covalent, apolipoprotein A-I) exhibited reversible temperature changes.
    • Weakly immobilized component (noncovalent) showed irreversible changes above 25°C with an activation energy of 26 kcal/mol.
    • NEM-TEMPO binding to strong sites was suppressed by TNBS, suggesting lysine residue involvement.
    • Both components were reduced by ascorbate at a rate of 0.048 min⁻¹.

    Conclusions:

    • NEM-TEMPO binding to HDL involves distinct covalent and noncovalent interactions.
    • Apolipoprotein A-I contains specific sites for covalent NEM-TEMPO modification.
    • Temperature sensitivity differs between covalent and noncovalent NEM-TEMPO binding.
    • TNBS pretreatment indicates lysine residues are likely targets for covalent binding.