Summary
In this study, we examined the effects of exposure of heart fatty acid-binding protein (h-FABP) to chemically generated O −2 or OH · with respect to its oléate binding and to its electrophoretic properties. Purified rat h-FABP at 40 µlM scavenged as much as 30% O −2 and 85% OH ·. On the other hand, when 2nmol (4µM) FABP were exposed to free radicals, the maximum oleate binding capacity as measured by Scatchard analysis was reduced only by 14% and 27% for O −2 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 O −2 or OH ·. It is hypothesized that O −2 or OH · in physiological concentration may not alter the function of FABP markedly in the ischemic-reperfused myocardium.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Abbreviations
- h-FABP:
-
Heart Fatty Acid Binding Protein
- NEFA:
-
Non-Esterified Fatty Acids
- O −2 :
-
Superoxide anions
- OH ·:
-
hydroxyl radicals
- OCI ·:
-
hypohalite radicals
- H2O2 :
-
hydrogen peroxide
- HPLC:
-
High Pressure Liquid Chromatography
References
Ockner RK, Manning JM, Poppenhausen RB, Ho WKL: A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues. Science 117: 56–58, 1972
Mishkin S, Stein L, Gatmaitan Z, Arias IM: The binding of fatty acids to cytoplasmic proteins: binding to Z protein in liver and other tissues of the rat. Biochem Biophys Res Commun 47: 997–1003, 1972
Glatz JFC, Van der Vusse GJ: Intracellular transport of lipids. Mol Cell Biochem 88: 37–44, 1989
Ockner RK, Manning JA, Kane JP: Fatty acid binding protein, isolation from rat liver, characterization, and immunochemical qualification. J Biochem 257: 7872–7878, 1982
Samanta A, Prasad MR, Engelman RM, Das DK: Possible physiological role of myocardial fatty acid binding protein in phospholipid biosynthesis. J Lipid Mediators 1:243–255, 1989
McCord JM: Oxygen-derived free radicals in post-ischemic tissue injury. N Engl J Med 312: 159–162, 1985
Horton AA, Fairhurst S: Lipid peroxidation and mechanism of toxicity. CRC Crit Rev Toxicol 18: 1–79, 1987
Kramer JH, Mak IT, Weglicki WB: Differential sensitivity of canine cardiac sarcolemmal and microsomal enzymes to inhibition by free radical-induced lipid peroxidation. Circ Res 55:120–124, 1984
Katz AM, Messineo FC: Lipid-membrane interactions and the pathogenesis of ischemic damage in the myocardium. Circ Res 48: 1–6, 1981
Samanta A, Das DK, Jones RM, George A, Prasad MR: Free radical scavenging by myocardial fatty acid binding protein. Free Radie Res Commun 7(2): 73–82, 1989
Glatz JFC, Baerwaldt CCF, Veerkamp JH, Kempen HJM: Diurnal variation of cytosolic fatty acid-binding protein content and of palmitate oxidation in rat liver and heart. J Biol Chem 259: 4295–4300, 1984
Offner GD, Troxler RF, Brecher P: Characterization of a fatty acid-binding protein from fat heart. J Biol Chem 261: 5584–5589, 1986
Kellog EW, Fridovich I: Superoxide and singlet oxygen in lipid peroxidation by a xanthine-oxidase system. J Biol Chem 250: 8812–8817, 1975
Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685, 1970
Davies KJA, Delsignore ME, Lin SW: Protein damage and degradation by oxygen radicals. J Biol Chem 262: 9902–9907, 1987
Davies KJA, Delsignore ME: Protein damage and degradation by oxygen radicals. J Biol Chem 262: 9908–9913, 1987
Katz AM, Messineo FC: Fatty acid effects on membranes; possible role in the pathogenesis of ischemic myocardial damage. J Mol Cell Cardiol (Suppl 3): 119–422, 1982
Turrens JG, Boveris A: Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191: 421–427, 1980
Glatz JFC, Van Bilsen M, Paulussen RJA, Veerkamp JH, Van der Vusse GJ, Reneman RS: Release of fatty acid-binding protein from isolated rat heart subjected to ischemia and reperfusion or to the calcium paradox. Biochim Biophys Acta 961: 148–152, 1988
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Jones, R.M., Prasad, M.R., Das, D.K. (1990). Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen — derived free radicals. In: Glatz, J.F.C., Van Der Vusse, G.J. (eds) Cellular Fatty Acid-binding Proteins. Developments in Molecular and Cellular Biochemistry, vol 6. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3936-0_20
Download citation
DOI: https://doi.org/10.1007/978-1-4615-3936-0_20
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6756-7
Online ISBN: 978-1-4615-3936-0
eBook Packages: Springer Book Archive