scholarly journals Retinoic acid induction of human cellular retinoic acid-binding protein-II gene transcription is mediated by retinoic acid receptor-retinoid X receptor heterodimers bound to one far upstream retinoic acid-responsive element with 5-base pair spacing.

1994 ◽  
Vol 269 (35) ◽  
pp. 22334-22339 ◽  
Author(s):  
A. Aström ◽  
U. Pettersson ◽  
P. Chambon ◽  
J.J. Voorhees
Keyword(s):  
Retinoic Acid ◽  
Gene Transcription ◽  
Base Pair ◽  
Retinoic Acid Receptor ◽  
Binding Protein ◽  
Retinoid X Receptor ◽  
Acid Receptor ◽  
Acid Binding Protein ◽  
Responsive Element

Retinoic Acid Receptor, Cytosolic Retinol-Binding and Retinoic Acid-Binding Protein mRNA Transcripts and Proteins in Rat Insulin-Secreting Cells

Diabetes ◽  
1993 ◽  
Vol 42 (8) ◽  
pp. 1109-1114 ◽  
Author(s):  
B. S. Chertow ◽  
W. S. Blaner ◽  
N. Rajan ◽  
D. A. Primerano ◽  
P. Meda ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Binding Protein ◽  
Acid Receptor ◽  
Acid Binding Protein ◽  
Mrna Transcripts ◽  
Insulin Secreting Cells

scholarly journals Direct Channeling of Retinoic Acid between Cellular Retinoic Acid-Binding Protein II and Retinoic Acid Receptor Sensitizes Mammary Carcinoma Cells to Retinoic Acid-Induced Growth Arrest

2002 ◽  
Vol 22 (8) ◽  
pp. 2632-2641 ◽  
Author(s):  
Anuradha S. Budhu ◽  
Noa Noy
Keyword(s):  
Retinoic Acid ◽  
Mammary Carcinoma ◽  
Transcriptional Activity ◽  
Retinoic Acid Receptor ◽  
Binding Protein ◽  
Carcinoma Cells ◽  
Acid Receptor ◽  
Acid Binding Protein ◽  
Mammary Carcinoma Cells ◽  
Crabp Ii

ABSTRACT Cellular retinoic acid-binding protein II (CRABP-II) is an intracellular lipid-binding protein that associates with retinoic acid with a subnanomolar affinity. We previously showed that CRABP-II enhances the transcriptional activity of the nuclear receptor with which it shares a common ligand, namely, the retinoic acid receptor (RAR), and we suggested that it may act by delivering retinoic acid to this receptor. Here, the mechanisms underlying the effects of CRABP-II on the transcriptional activity of RAR and the functional consequences of these effects were studied. We show that CRABP-II, a predominantly cytosolic protein, massively undergoes nuclear localization upon binding of retinoic acid; that it interacts with RAR in a ligand-dependent fashion; and that, in the presence of retinoic acid, the CRABP-II-RAR complex is a short-lived intermediate. The data establish that potentiation of the transcriptional activity of RAR stems directly from the ability of CRABP-II to channel retinoic acid to the receptor. We demonstrate further that overexpression of CRABP-II in MCF-7 mammary carcinoma cells dramatically enhances their sensitivity to retinoic acid-induced growth inhibition. Conversely, diminished expression of CRABP-II renders these cells retinoic acid resistant. Taken together, the data unequivocally establish the function of CRABP-II in modulating the RAR-mediated biological activities of retinoic acid.

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