Journal of Experimental Medicine, Vol 157, 628-641, Copyright © 1983 by Rockefeller University Press

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Specific binding of leukotriene B4 to a receptor on human polymorphonuclear leukocytes

RA Kreisle and CW Parker

In this paper we have described the binding of nanomoler concentrations of [3H]leukotriene B4 (LTB4) to human polymorphonuclear leukocytes. Because up to 80% of the total [3H]LTB4 binding was blocked by excess (greater than 100 times) [14C]LTB4, the majority of binding is specific. Stereospecificity of the LTB4 binding is demonstrated by the diminished relative abilities of the 6-trans-and 12-epi-6-trans- isomers of LTB4 to block [3H]LTB4 binding. With these two isomers 3-10- fold higher than [14C]LTB4 concentrations were needed for equivalent inhibition of [3H]LTB4 binding. This difference is quantitatively less dramatic than the differences between these isomers in many in vitro functional assays such as chemokinesis, chemotaxis, and degranulation. Binding of [3H]FMLP is not blocked at greater than 100-fold excess of LTB4. The binding of [3H]LTB4 to cells appears to be essentially irreversible at 4 degrees C, but not at 37 degrees C where initially bound LTB4 is rapidly converted to metabolites which then enter the medium. These results suggest the presence of a saturable, stereospecific site for LTB4 on PMN. The association of LTB4 binding and the initiation of pharmacological responses to LTB4 will require further studies.
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• OSTERUD, B., BJORKLID, E. (2003). Role of Monocytes in Atherogenesis. Physiol. Rev. 83: 1069-1112 [Abstract] [Full Text]  
• DAHLEN, S.-E. (2000). Pharmacological Characterization of Leukotriene Receptors. Am. J. Respir. Crit. Care Med. 161: S41-45 [Full Text]  

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