Loading…

Molecular cloning and characterization of two novel human RXRα splice variants

Two novel cDNAs encoding RXRα splice variants (RXRα2 and RXRα3) were identified among human full-length cDNA libraries. RXRα2 and RXRα3 cDNAs possess open reading frames, leading to production of proteins lacking the N-terminal 27 and 97 amino acid residues of the RXRα1 product, respectively. RXRα2...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of steroid biochemistry and molecular biology 2004-09, Vol.92 (1), p.19-28
Main Authors: Kojo, Hitoshi, Tajima, Kaoru, Fukagawa, Masao, Isogai, Takao, Nishimura, Shintaro
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Two novel cDNAs encoding RXRα splice variants (RXRα2 and RXRα3) were identified among human full-length cDNA libraries. RXRα2 and RXRα3 cDNAs possess open reading frames, leading to production of proteins lacking the N-terminal 27 and 97 amino acid residues of the RXRα1 product, respectively. RXRα2 and RXRα3 genes have respective 5′-terminal exons. RXRα3 is expressed in brain, spleen and prostate whereas the expression of RXRα2 was below the detectable level. Both RXRα2 and RXRα3 showed a level of transcriptional activity and a dose response curve against the agonist LG100268 similar to RXRα1 in reporter assay for the RXRα homodimer or that for the heterodimer with PPARγ2. However, clear differences were observed among the splice variants when dose response curves were compared by the assay in the presence of coactivators such as SRC-1 and PGC-1. These results suggest specific physiological roles of two novel human RXRα splice variants.
ISSN:0960-0760
1879-1220
DOI:10.1016/j.jsbmb.2004.07.001