Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors

@article{Dreyer1992ControlOT,
  title={Control of the peroxisomal $\beta$-oxidation pathway by a novel family of nuclear hormone receptors},
  author={Christine Dreyer and Grigorios D. Krey and Hansj{\"o}rg Keller and Francoise Givel and Gerd Helftenbein and Walter Wahli},
  journal={Cell},
  year={1992},
  volume={68},
  pages={879-887}
}
Three novel members of the Xenopus nuclear hormone receptor superfamily have been cloned. They are related to each other and similar to the group of receptors that includes those for thyroid hormones, retinoids, and vitamin D3. Their transcriptional activity is regulated by agents causing peroxisome proliferation and carcinogenesis in rodent liver. All three Xenopus receptors activate the promoter of the acyl coenzyme A oxidase gene, which encodes the key enzyme of peroxisomal fatty acid beta… Expand
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References

SHOWING 1-10 OF 37 REFERENCES
Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
TLDR
A member of the steroid hormone receptor superfamily of ligand-activated transcription factors is cloned that is activated by a diverse class of rodent hepatocarcinogens that causes proliferation of peroxisomes. Expand
Nuclear receptors enhance our understanding of transcription regulation.
Abstract Receptors for retinoic acid, vitamin D3 and the steroid and thyroid hormones belong to a family of ligand-activated enhancer-binding factors which are composed of a number of functionalExpand
Two cis-acting regulatory sequences in the peroxisome proliferator-responsive enhancer region of rat acyl-CoA oxidase gene.
TLDR
The mechanism of transcriptional induction of the rat liver acyl-CoA oxidase gene by hypolipidemic agents is clarified, and it is found that the sequence between -639 and -472 acts as a peroxisome proliferator-responsive, tissue-specific enhancer. Expand
The steroid and thyroid hormone receptor superfamily.
TLDR
A superfamily of regulatory proteins that include receptors for thyroid hormone and the vertebrate morphogen retinoic acid is identified, suggesting mechanisms underlying morphogenesis and homeostasis may be more ubiquitous than previously expected. Expand
Differential induction and regulation of peroxisomal enzymes: predictive value of peroxisome proliferation in identifying certain nonmutagenic carcinogens.
TLDR
The morphological phenomenon of peroxisome proliferation should serve as a simple, sensitive, and valuable biological indicator for the identification of nongenotoxic or nonmutagenic chemicals that may be carcinogenic. Expand
A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR
TLDR
Evidence is provided that expression of the gene for cellular retinol-binding protein type II (CRBPII), a key protein in the intestinal absorption of vitamin A, is dramatically up-regulated by retinoic acid in the presence of RXR but not RAR, suggesting that an RXR-mediated pathway exists for modulating vitamin A metabolism. Expand
Pathophysiology of peroxisomal beta-oxidation.
TLDR
Combination of specific isolation procedures, enzyme assays and morphological analysis have resulted in the current knowledge of peroxisomal physiology, which has greatly benefited from the study of inborn errors of metabolism and the contribution of molecular biology. Expand
The steroid receptor superfamily: more excitement predicted for the future.
TLDR
This superfamily of regulatory molecules was shown to include also the receptors for thyroid hormone (T3) vitamin D3 and retinoic acid and perhaps more surprising was the inclusion of oncogenes such as v-erb A in this family. Expand
Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model.
TLDR
This "regulatory zipper model" may explain the mechanism by which ligand activates nuclear hormone receptors and suggest a novel model that structurally and functionally links these events. Expand
Superfamily of steroid nuclear receptors: positive and negative regulators of gene expression
  • W. Wahli, Ernest Martinez
  • Biology, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1991
TLDR
The similarity between all these hormone response enhancer elements, as well as between the receptors themselves, indicates a conserved general strategy for the hormonal control of transcription by steroids. Expand
...
1
2
3
4
...