High-affinity binding sites for 12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12(S)-HETE) in carcinoma cells.
12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12(S)-HETE) enhances tumor cell adhesion to endothelial cells [Honn et al. (1988) Proc. Soc. Exp. Biol. Med. 189, 130-135]. The effect is correlated to surface expression of an integrin receptor, GpIIb/IIIa. Here, we describe evidence for high-affinity binding of 12(S)-HETE to Lewis lung carcinoma cells. Scatchard plot analyses indicated a single class of sites with apparent Kd and Bmax values of 0.44 nM and 66,000 sites per cell, respectively. Competition experiments with unlabeled compounds shod d that the binding was reversible and saturable as well as stereo- and regiospecific. The 12(S)-HETE binding, demonstrated here, might be an important step in a series of events controlling surface expression of integrin receptors.
Herbertsson
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H
Department of Cell Biology, Faculty of Health Sciences, Linköping University, Sweden.
Hammarström
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S
D019377:12-Hydroxy-5,8,10,14-eicosatetraenoic Acid; D001665:Binding Sites; D001667:Binding, Competitive; D006893:Hydroxyeicosatetraenoic Acids / Q000378:metabolism*; D007700:Kinetics; D008084:Lipoxygenase / Q000378:metabolism; D008175:Lung Neoplasms / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D006893:Hydroxyeicosatetraenoic Acids; D019377:12-Hydroxy-5,8,10,14-eicosatetraenoic Acid; D008084:Lipoxygenase