A G-protein-coupled receptor for leukotriene B4 that mediates chemotaxis

Takehiko Yokomizo, Takashi Izumi, Kyungho Chang, Yoh Takuwa and Takao Shimizu ()
Additional contact information
Takehiko Yokomizo: Cardiovascular, Faculty of Medicine, The University of Tokyo
Takashi Izumi: Cardiovascular, Faculty of Medicine, The University of Tokyo
Kyungho Chang: The University of Tokyo
Yoh Takuwa: The University of Tokyo
Takao Shimizu: Cardiovascular, Faculty of Medicine, The University of Tokyo

Nature, 1997, vol. 387, issue 6633, 620-624

Abstract: Abstract Leukotriene B4(LTB4)1 is a potent chemoattractant that is primarily involved in inflammation, immune responses and host defence against infection2. LTB4 activates inflammatory cells by binding to its cell-surface receptor (BLTR)3. LTB4 can also bind and activate the intranuclear transcription factor PPARα, resulting in the activation of genes that terminate inflammatory processes4. Here we report the cloning of the complementary DNA encoding a cell-surface LTB4 receptor that is highly expressed in human leukocytes. Using a subtraction strategy, we isolated two cDNA clones (HL-1 and HL-5) from retinoic acid-differentiated HL-60 cells. These two clones contain identical open reading frames encoding a protein of 352 amino acids and predicted to contain seven membrane-spanning domains, but different 5′-untranslated regions. Membrane fractions of Cos-7 cells transfected with an expression construct containing the open reading frame of HL-5 showed specific LTB4 binding, with a Kd(0.154nM) comparable to that observed in retinoic acid-differentiated HL-60 cells. In CHO cells stably expressing this receptor, LTB4 induced increases in intracellular calcium, D-myo-inositol-1,4,5-triphosphate (InsP3) accumulation, and inhibition of adenylyl cyclase. Furthermore, CHO cells expressing exogenous BLTR showed marked chemotactic responses towards low concentrations of LTB4 in a pertussis-toxin-sensitive manner. Our findings, together with previous reports4,5, show that LTB4 is a unique lipid mediator that interacts with both cell-surface and nuclear receptors.

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/42506 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:387:y:1997:i:6633:d:10.1038_42506

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/42506

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().