High-affinity binding sites for 12(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12(S)-HETE) in carcinoma cells. |
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Authors: | H Herbertsson S Hammarstr?m |
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Affiliation: | Department of Cell Biology, Faculty of Health Sciences, Link?ping University, Sweden. |
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Abstract: | 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. |
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