NDLI: Chemical Probes That Differentially Modulate Peroxisome Proliferator-activated Receptor α and BLTR, Nuclear and Cell Surface Receptors for Leukotriene B4

Content Provider	Journal of Biological Chemistry (JBC)
Author	Devchand, Pallavi R. Hihi, Abdelmadjid K. Perroud, Mai Schleuning, Wolf-Dieter D. Spiegelman, Bruce M. Wahli, Walter
Abstract	Peroxisome proliferator-activated receptor α (PPARα)is a nuclear receptor for various fatty acids, eicosanoids, and hypolipidemic drugs. In the presence of ligand, this transcription factor increases expression of target genes that are primarily associated with lipid homeostasis. We have previously reported PPARα as a nuclear receptor of the inflammatory mediator leukotriene B4 (LTB4) and demonstrated an anti-inflammatory function for PPARα in vivo (Devchand, P. R., Keller, H., Peters, J. M., Vazquez, M., Gonzalez, F. J., and Wahli, W. (1996) Nature 384, 39–43). LTB4 also has a cell surface receptor (BLTR) that mediates proinflammatory events, such as chemotaxis and chemokinesis (Yokomizo, T., Izumi, T., Chang, K., Takuwa, Y., and Shimizu, T. (1997)Nature 387, 620–624). In this study, we report on chemical probes that differentially modulate activity of these two LTB4 receptors. The compounds selected were originally characterized as synthetic BLTR effectors, both agonists and antagonists. Here, we evaluate the compounds as effectors of the three PPAR isotypes (α, β, and γ) by transient transfection assays and also determine whether the compounds are ligands for these nuclear receptors by coactivator-dependent receptor ligand interaction assay, a semifunctional in vitro assay. Because the compounds are PPARα selective, we further analyze their potency in a biological assay for the PPARα-mediated activity of lipid accumulation. These chemical probes will prove invaluable in dissecting processes that involve nuclear and cell surface LTB4 receptors and also aid in drug discovery programs.
Related Links	http://www.jbc.org/content/274/33/23341.abstract
Ending Page	23348
Starting Page	23341
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	33
Volume Number	274
DOI	10.1074/jbc.274.33.23341
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1999-08-13
Access Restriction	Open
Subject Keyword	Peroxisome proliferator-activated receptor (PPAR) Leukotriene B4 (LTB4) BLTR agonist (BAg) BLTR antagonist (BAntag) 5-lipoxygenase (5-LO) Coactivator-dependent receptor ligand interaction assay (CARLA) Steroid receptor coactivator 1 (SRC-1) Ligand-induced complex (LIC) Glutathione S-transferase (GST) Ligand binding domain (LBD) Retinoid X acid receptor (RXR) Chloramphenicol acetyltransferase (CAT) CARBOHYDRATES, LIPIDS, AND OTHER NATURAL PRODUCTS
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Both Coactivator LXXLL Motif-dependent and -independent Interactions Are Required for Peroxisome Proliferator-activated Receptor γ (PPARγ) Function

Ligand type-specific Interactions of Peroxisome Proliferator-activated Receptor γ with Transcriptional Coactivators

PGC-1 Functions as a Transcriptional Coactivator for the Retinoid X Receptors

Identification of Nuclear Receptor Corepressor as a Peroxisome Proliferator-activated Receptor α Interacting Protein

p300 Interacts with the N- and C-terminal Part of PPARγ2 in a Ligand-independent and -dependent Manner, Respectively

Novel Peroxisome Proliferator-activated Receptor (PPAR) γ and PPARδ Ligands Produce Distinct Biological Effects

Mutations in Retinoid X Receptor That Impair Heterodimerization with Specific Nuclear Hormone Receptor

Ligand and Coactivator Identity Determines the Requirement of the Charge Clamp for Coactivation of the Peroxisome Proliferator-activated Receptor γ

Helix 12 stabilization contributes to basal transcriptional activity of PXR.

Chemical Probes That Differentially Modulate Peroxisome Proliferator-activated Receptor α and BLTR, Nuclear and Cell Surface Receptors for Leukotriene B4

Similar Documents

Both Coactivator LXXLL Motif-dependent and -independent Interactions Are Required for Peroxisome Proliferator-activated Receptor γ (PPARγ) Function

Ligand type-specific Interactions of Peroxisome Proliferator-activated Receptor γ with Transcriptional Coactivators

PGC-1 Functions as a Transcriptional Coactivator for the Retinoid X Receptors

Identification of Nuclear Receptor Corepressor as a Peroxisome Proliferator-activated Receptor α Interacting Protein

p300 Interacts with the N- and C-terminal Part of PPARγ2 in a Ligand-independent and -dependent Manner, Respectively

Novel Peroxisome Proliferator-activated Receptor (PPAR) γ and PPARδ Ligands Produce Distinct Biological Effects

Mutations in Retinoid X Receptor That Impair Heterodimerization with Specific Nuclear Hormone Receptor

Ligand and Coactivator Identity Determines the Requirement of the Charge Clamp for Coactivation of the Peroxisome Proliferator-activated Receptor γ

Helix 12 stabilization contributes to basal transcriptional activity of PXR.

Chemical Probes That Differentially Modulate Peroxisome Proliferator-activated Receptor α and BLTR, Nuclear and Cell Surface Receptors for Leukotriene B4