We have updated our privacy policy. If you have any question, contact us at privacy@scicrunch.org. Dismiss and don't show again

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2.

The peroxisome proliferator-activated receptor alpha (PPARalpha) is a ligand-inducible transcription factor, which belongs to the nuclear receptor superfamily. PPARalpha mediates the carcinogenic effects of peroxisome proliferators in rodents. In humans, PPARalpha plays a fundamental role in regulating energy homeostasis via control of lipid metabolism. To study the possible role of chaperone proteins in the regulation of PPARalpha activity, a monoclonal antibody (mAb) was made against PPARalpha and designated as 3B6/PPAR. The specificity of mAb 3B6/PPAR in recognizing PPARalpha was tested in immunoprecipitations using in vitro translated PPAR subtypes. The mAb 3B6/PPAR recognized PPARalpha, failed to bind to PPARbeta or PPARgamma, and is efficient in both immunoprecipitating and visualizing the receptor on protein blots. The immunoprecipitation of PPARalpha in mouse liver cytosol using mAb 3B6/PPAR has resulted in the detection of two co-immunoprecipitated proteins, which are heat shock protein 90 (hsp90) and the hepatitis B virus X-associated protein 2 (XAP2). The concomitant depletion of PPARalpha in hsp90-depleted mouse liver cytosol was also detected. Complex formation between XAP2 and PPARalpha/FLAG was also demonstrated in an in vitro translation binding assay. hsp90 interacts with PPARalpha in a mammalian two-hybrid assay and binds to the E/F domain. Transient expression of XAP2 co-expressed with PPARalpha resulted in down-regulation of a peroxisome proliferator response element-driven reporter gene activity. Taken together, these results indicate that PPARalpha is in a complex with hsp90 and XAP2, and XAP2 appears to function as a repressor. This is the first demonstration that PPARalpha is stably associated with other proteins in tissue extracts and the first nuclear receptor shown to functionally interact with XAP2.

Pubmed ID: 12482853 RIS Download

Mesh terms: Animals | Antibodies, Monoclonal | COS Cells | HSP90 Heat-Shock Proteins | Intracellular Signaling Peptides and Proteins | Liver | Mice | Nuclear Proteins | Precipitin Tests | Protein Binding | Proteins | Receptors, Cytoplasmic and Nuclear | Repressor Proteins | Transcription Factors

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIEHS NIH HHS, Id: ES07799

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.