Polyunsaturated fatty acids modulate the properties of the sex steroid binding protein in goldfish

This study examines the effects of nonesterified fatty acids on the properties of the sex steroid binding protein (SSBP) in the plasma of goldfish (Carassius auratrus). Scatchard analysis revealed a single class of high affinity (K-d 1.89 +/- 0.20 nM), low capacity (B-max 302 +/- 17 nM) binding sites for [H-3]17 beta-estradiol in female goldfish plasma. The SSBP bound 17 beta-estradiol and testosterone with similar affinity but had much lower affinity for estriol, 17 alpha,20 beta-dihydroxy-4-pregnen-3-one and cholesterol. Nonesterified fatty acids inhibit the binding of [H-3]17 beta-estradiol to the SSBP as a function of dose, degree of unsaturation and fatty acid chain length. Polyunsaturated fatty acids (PUFAs) such as arachidonic acid (C20:4), eicosapentaenoic acid (C20:5) and docosahexaenoic acid (C22:6) strongly inhibit the binding of [H-3] 17 beta-estradiol to the SSBP By comparison, saturated fatty acids such as heptadecanoic acid (C17:0), palmitic acid (C16:0) and stearic acid (C18:0) were without effect. Scatchard analysis and Lineweaver-Burk; plots showed that PUFAs act through a competitive mechanism whereby they reduce the affinity but have no effect on the binding capacity of the SSBP. Collectively, these studies suggest that in addition to their roles as metabolic energy sources and as precursors to eicosanoids, PUFAs can be potent modulators of steroid hormone interactions with the SSBP in,goldfish plasma.