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. 2000 Apr 3;191(7):1197–1208. doi: 10.1084/jem.191.7.1197

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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LXs and peptides specifically compete for ³H-LXA₄ on HEK293 cells. ALXR-transfected HEK293 cells (5 × 10⁶/ml) were incubated with ³H-LXA₄ for 30 min at 4°C in the presence of an increasing concentration of unlabeled LXA₄ (▪) or (A) ATLa₁ (♦), ATLa₂ (•), 15-deoxy-LXA₄ (⋄), (B) MMK-1 (▵), MHC binding peptide (○), or SAA (♦). Bound and unbound radioligands were separated by filtration and specific binding was determined. Data represent the mean ± SEM from duplicates of n = 3.

LXs and peptides specifically compete for ³H-LXA₄ on HEK293 cells. ALXR-transfected HEK293 cells (5 × 10⁶/ml) were incubated with ³H-LXA₄ for 30 min at 4°C in the presence of an increasing concentration of unlabeled LXA₄ (▪) or (A) ATLa₁ (♦), ATLa₂ (•), 15-deoxy-LXA₄ (⋄), (B) MMK-1 (▵), MHC binding peptide (○), or SAA (♦). Bound and unbound radioligands were separated by filtration and specific binding was determined. Data represent the mean ± SEM from duplicates of n = 3.