Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

Rfabg - Retinoid- and fatty acid-binding glycoprotein

Drosophila melanogaster

Synonyms: ApoL1, ApoL2, ApoLI, ApoLII, Apolipophorins, ...

Duncan, T. et al., Raval-Pandya, M. et al., Carlberg, C., Yao, T.P. et al., Kutty, R.K. et al., et al.

Bogerd, Babin, Kooiman, André, Ballagny, van Marrewijk, van der Horst,

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on RfaBp

We now demonstrate that ultraspiracle (usp), a Drosophila RXR homolog, can substitute for RXR in stimulating the DNA binding of receptors for retinoic acid, T3, vitamin D, and peroxisome proliferator activators [1].
The nuclear receptors for 1,25-dihydroxyvitamin D3 (VD) and 3,5,3'-triiodothyronine (T3), that is, VDRs and T3Rs respectively, control aspects of homeostasis, cell growth and differentiation [2].
The gene, localized to the chromosome 4 (102 F region), encodes a 3351-amino acid protein that could serve as the precursor for the approximately 70-kDa and >200-kDa polypeptides associated with RFABG [3].
To determine whether the weak response of the rat CaBP9k natural promoter to 1,25-(OH)2D3 could be enhanced by T3, CaBP9k promoter/reporter chloramphenicol acetyltransferase constructs were transfected in MCF-7 cells, and the cells were treated with the two hormones alone or in combination [4].
Heme added to a solution of purified RFABG bound in a saturable manner with an affinity of 3.8 x 10(-7) m.Thus, the current study clearly demonstrates that retinoid- and fatty acid-binding glycoprotein is a novel heme-binding protein, which may be involved in the transport and/or metabolism of heme in Drosophila [5].

Biological context of RfaBp

Molecular characterization and gene expression in the eye of the apolipophorin II/I precursor from Locusta migratoria [6].

Associations of RfaBp with chemical compounds

We previously have cloned and characterized a retinoid- and fatty acid-binding glycoprotein (RFABG) isolated from the heads of Drosophila melanogaster [5].
Again, no enhancement of the response to 1,25-(OH)2D3 was observed in the presence of T3 [4].
Hydrophobic ligands, like all-trans and 9-cis retinoic acid (RA), 3,5,3'-triiodothyronine (T3) and 1,25-dihydroxy-cholecalciferol (VD), mediate their biological response by binding to their respective nuclear receptors (RARs, RXRs, T3Rs and VDRs) which are members of the steroid receptor superfamily [7].

Analytical, diagnostic and therapeutic context of RfaBp

Hemin-agarose affinity chromatography of the native RFABG followed by Western blot analysis showed a single immunoreactive band at 70 kDa, indicating that the heme-binding domain resides in the 70 kDa subunit [5].

References

Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation. Yao, T.P., Segraves, W.A., Oro, A.E., McKeown, M., Evans, R.M. Cell (1992) [Pubmed]
Vitamin D3-thyroid hormone receptor heterodimer polarity directs ligand sensitivity of transactivation. Schräder, M., Müller, K.M., Nayeri, S., Kahlen, J.P., Carlberg, C. Nature (1994) [Pubmed]
Molecular characterization and developmental expression of a retinoid- and fatty acid-binding glycoprotein from Drosophila. A putative lipophorin. Kutty, R.K., Kutty, G., Kambadur, R., Duncan, T., Koonin, E.V., Rodriguez, I.R., Odenwald, W.F., Wiggert, B. J. Biol. Chem. (1996) [Pubmed]
Thyroid hormone receptor does not heterodimerize with the vitamin D receptor but represses vitamin D receptor-mediated transactivation. Raval-Pandya, M., Freedman, L.P., Li, H., Christakos, S. Mol. Endocrinol. (1998) [Pubmed]
Heme-binding by Drosophila retinoid- and fatty acid-binding glycoprotein (RFABG), a member of the proapolipophorin gene family. Duncan, T., Osawa, Y., Kutty, R.K., Kutty, G., Wiggert, B. J. Lipid Res. (1999) [Pubmed]
Molecular characterization and gene expression in the eye of the apolipophorin II/I precursor from Locusta migratoria. Bogerd, J., Babin, P.J., Kooiman, F.P., André, M., Ballagny, C., van Marrewijk, W.J., van der Horst, D.J. J. Comp. Neurol. (2000) [Pubmed]
RXR-independent action of the receptors for thyroid hormone, retinoid acid and vitamin D on inverted palindromes. Carlberg, C. Biochem. Biophys. Res. Commun. (1993) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.