Proc Natl Acad Sci U S A
May 1997
Steroidogenic factor 1 (SF-1), an orphan member of the intracellular receptor superfamily, plays an essential role in the development and function of multiple endocrine organs. It is expressed in all steroidogenic tissues where it regulates the P450 steroidogenic genes to generate physiologically active steroids. Although many of the functions of SF-1 in vivo have been defined, an unresolved question is whether a ligand modulates its transcriptional activity.
View Article and Find Full Text PDFT-cell hybridomas, thymocytes, and T cells can be induced to undergo apoptotic cell death by activation through the T-cell receptor. This process requires macromolecular synthesis and thus gene expression, and it has been shown to be influenced by factors regulating transcription. Recently, activation, T-cell hybridomas rapidly express the Fas/CD95 receptor and its ligand, Fas ligand (FasL), which interact to transduce the death signal in the activated cell.
View Article and Find Full Text PDFA metabolite of all-trans retinoic acid produced by insect cells was discovered to activate the intracellular retinoic acid X receptor. The compound, beta-glucopyranosyl 9-cis-retinoate [1], was purified and its structure was determined by analysis of spectroscopic data.
View Article and Find Full Text PDFThe binding affinities of 9-cis-retinoic acid (9-cis-RA) and all-trans-retinoic acid (t-RA) for retinoic acid receptors (RAR) alpha, beta, and gamma and for retinoid X receptors (RXR) alpha, beta, and gamma were determined using the recombinant receptor proteins and were compared with each hormone's ability to activate transcription through the receptors in mammalian and yeast cell systems. 9-cis-RA bound to both the RXRs (Kd values = 1.4-2.
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