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Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen — derived free radicals

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Summary

In this study, we examined the effects of exposure of heart fatty acid-binding protein (h-FABP) to chemically generated O2 − or OH · with respect to its oleate binding and to its electrophoretic properties. Purified rat h-FABP at 40 μM scavenged as much as 30% O2 − and 85% OH ·. On the other hand, when 2 nmol (4 μM) FABP were exposed to free radicals, the maximum oleate binding capacity as measured by Scatchard analysis was reduced only by 14% and 27% for O2 − and OH ·, respectively. The electrophoretic pattern of free radical-exposed FABP was not markedly different when examined either by the non-denaturing or by denaturing PAGE, suggesting the absence of any degradation or aggregation of FABP by O2 − or OH ·. It is hypothesized that O2 − or OH · in physiological concentration may not alter the function of FABP markedly in the ischemic-reperfused myocardium.

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Abbreviations

h-FABP:

Heart Fatty Acid Binding Protein

NEFA:

Non-Esterified Fatty Acids

O2 − :

Superoxide anions

OH·:

hydroxyl radicals

OCI:

hypohalite radicals

H2O2 :

hydrogen peroxide

HPLC:

High Pressure Liquid Chromatography

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Authors and Affiliations

  1. Surgical Research Center, Department of Surgery, Cardiovascular Division, University of Connecticut School of Medicine, 06032, Farmington, Connecticut, USA

    Randall M. Jones, M. Renuka Prasad & Dipak K. Das

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  1. Randall M. Jones
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  2. M. Renuka Prasad
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  3. Dipak K. Das
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Jones, R.M., Renuka Prasad, M. & Das, D.K. Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen — derived free radicals. Mol Cell Biochem 98, 161–166 (1990). https://doi.org/10.1007/BF00231380

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