Changes in function and kinetics of macrophages and lymphocytes caused by retinoic acid

1987 ◽  
Vol 103 (6) ◽  
pp. 802-804 ◽  
Author(s):  
V. I. Nozdrin ◽  
V. G. Kvachev ◽  
T. I. Galenko
Keyword(s):  
Retinoic Acid ◽  
Kinetics Of

Kinetics of Plasma and Tissue Distribution of 9-cis-Retinoic Acid in Rat

2000 ◽  
Vol 13 (1) ◽  
pp. 9-16 ◽  
Author(s):  
B. Disdier ◽  
M.N. Marchetti ◽  
H. Bun ◽  
M. Placidi ◽  
A. Durand
Keyword(s):  
Retinoic Acid ◽  
Tissue Distribution ◽  
Kinetics Of

Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids

1999 ◽  
Vol 55 (11) ◽  
pp. 1850-1857 ◽  
Author(s):  
Barnali Neel Chaudhuri ◽  
Gerard J. Kleywegt ◽  
Isabelle Broutin-L'Hermite ◽  
Terese Bergfors ◽  
Hans Senn ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Specific Protein ◽  
Binding Affinities ◽  
Cellular Processes ◽  
Crabp I ◽  
Retinoid Binding Proteins ◽  
Retinoic Acid Binding Proteins ◽  
Crabp Ii ◽  
Kinetics Of

Retinoids play important roles in diverse cellular processes including growth, cell differentiation and vision. Many natural and synthetic retinoids are used as drugs in dermatology and oncology. A large amount of data has been accumulated on the cellular activity of different synthetic retinoids. They are stabilized and transported inside the cell cytoplasm by binding and transport proteins, such as cellular retinol-binding proteins and cellular retinoic acid binding proteins (CRABPs). The structures of human CRABP II in complex with two different synthetic retinoids, Ro13-6307 and Ro12-7310 (at 2.1 and 2.0 Å resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic acid, Am80 (at 2.8 Å resolution) are described. The binding affinities of human CRABP I and II for the retinoids studied here have been determined. All these compounds have comparable binding affinities (nanomolar range) for both CRABPs. Apart from the particular interactions of the carboxylate group of the retinoids with specific protein groups, each structure reveals characteristic interactions. Studying the atomic details of the interaction of retinoids with retinoid-binding proteins facilitates the understanding of the kinetics of retinoid trafficking inside the cytoplasm.

scholarly journals A dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and retinoic acid receptor:retinoid X receptor heterodimers regulates Oct-3/4 expression in embryonal carcinoma cells.

1995 ◽  
Vol 15 (2) ◽  
pp. 1034-1048 ◽  
Author(s):  
E Ben-Shushan ◽  
H Sharir ◽  
E Pikarsky ◽  
Y Bergman
Keyword(s):  
Transcription Factors ◽  
Retinoic Acid ◽  
Binding Site ◽  
Transcriptional Repression ◽  
Embryonal Carcinoma ◽  
Dependent Manner ◽  
Orphan Receptors ◽  
Positive Regulators ◽  
Ec Cells ◽  
Kinetics Of

The Oct-3/4 transcription factor is a member of the POU family of transcription factors and, as such, probably plays a crucial role in mammalian embryogenesis and differentiation. It is expressed in the earliest stages of embryogenesis and repressed in subsequent stages. Similarly, Oct-3/4 is expressed in embryonal carcinoma (EC) cells and is repressed in retinoic acid (RA)-differentiated EC cells. Previously we have shown that the Oct-3/4 promoter harbors an RA-responsive element, RAREoct, which functions in EC cells as a binding site for positive regulators of transcription and in RA-differentiated EC cells as a binding site for positive regulators of transcription and in RA-differentiated EC cells as a binding site for negative regulators. Our present results demonstrate that in P19 and RA-treated P19 cells, the orphan receptors ARP-1/COUP-TFII and EAR-3/COUP-TFI repress Oct-3/4 promoter activity through the RAREoct site in a dose-dependent manner. While the N-terminal region of the ARP-1/COUP-TFII receptor is dispensable for this repression, the C-terminal domain harbors the silencing region. Interestingly, three different RA receptor:retinoid X receptor (RAR:RXR) heterodimers, RAR alpha:RXR alpha, RAR beta:RXR alpha, and RAR beta:RXR beta, specifically bind and activate Oct-3/4 promoter through the RAREoct site in a ligand-dependent manner. We have shown that antagonism between ARP-1/COUP-TFII or EAR-3/COUP-TFI and the RAR:RXR heterodimers and their intracellular balance modulate Oct-3/4 expression. Oct-3/4 transcriptional repression by the orphan receptors can be overcome by increasing amounts of RAR:RXR heterodimers. Conversely, activation of Oct-3/4 promoter by RAR:RXR heterodimers was completely abolished by EAR-3/COUP-TFI and by ARP-1/COUP-TFII. The orphan receptors bind the RAREoct site with a much higher affinity than the RAR:RXR heterodimers. This high binding affinity provides ARP-1/COUP-TFII and EAR-3/COUP-TFI with the ability to compete with and even displace RAR:RXR from the RAREoct site and subsequently to actively silence the Oct-3/4 promoter. We have shown that RA treatment of EC cells results in up-regulation of ARP-1/COUP-TFII and EAR-3/COUP-TFI expression. Most interestingly, in RA-treated EC cells, the kinetics of Oct-3/4 repression inversely correlates with the kinetics of ARP-1/COUP-TFII and EAR-3/COUP-TFI activation. These findings are in accordance with the suggestion that these orphan receptors participate in controlling a network of transcription factors, among which Oct-3/4 is included, which may establish the pattern of normal gene expression during development.

Fluorescence spectra and kinetics of isomers and dimers of retinoic acid

1990 ◽  
Vol 53 (6) ◽  
pp. 1271-1275 ◽  
Author(s):  
M. V. Bel'kov ◽  
S. L. Bondarev
Keyword(s):  
Retinoic Acid ◽  
Fluorescence Spectra ◽  
Kinetics Of

Dose-dependent kinetics of all-trams-retinoic acid in rats

1981 ◽  
Vol 30 (2) ◽  
pp. 107-113 ◽  
Author(s):  
Brian N. Swanson ◽  
Charles A. Frolik ◽  
Daniel W. Zaharevitz ◽  
Peter P. Roller ◽  
Michael B. Sporn
Keyword(s):  
Retinoic Acid ◽  
Kinetics Of ◽  
Dose Dependent Kinetics ◽  
Dose Dependent

scholarly journals Scavenging of Retinoid Cation Radicals by Urate, Trolox, and α-, β-, γ-, and δ-Tocopherols

2019 ◽  
Vol 20 (11) ◽  
pp. 2799 ◽  
Author(s):  
Malgorzata Rozanowska ◽  
Ruth Edge ◽  
Edward J. Land ◽  
Suppiah Navaratnam ◽  
Tadeusz Sarna ◽  
...  
Keyword(s):  
Amino Acids ◽  
Retinoic Acid ◽  
Rate Constants ◽  
Cation Radical ◽  
Age Related Macular Degeneration ◽  
Cation Radicals ◽  
Age Related ◽  
Increased Risk ◽  
Kinetics Of ◽  
Skin Photosensitivity

Retinoids are present in human tissues exposed to light and under increased risk of oxidative stress, such as the retina and skin. Retinoid cation radicals can be formed as a result of the interaction between retinoids and other radicals or photoexcitation with light. It has been shown that such semi-oxidized retinoids can oxidize certain amino acids and proteins, and that α-tocopherol can scavenge the cation radicals of retinol and retinoic acid. The aim of this study was to determine (i) whether β-, γ-, and δ-tocopherols can also scavenge these radicals, and (ii) whether tocopherols can scavenge the cation radicals of another form of vitamin A—retinal. The retinoid cation radicals were generated by the pulse radiolysis of benzene or aqueous solution in the presence of a selected retinoid under oxidizing conditions, and the kinetics of retinoid cation radical decays were measured in the absence and presence of different tocopherols, Trolox or urate. The bimolecular rate constants are the highest for the scavenging of cation radicals of retinal, (7 to 8) × 109 M−1·s−1, followed by retinoic acid, (0.03 to 5.6) × 109 M−1·s−1, and retinol, (0.08 to 1.6) × 108 M−1·s−1. Delta-tocopherol is the least effective scavenger of semi-oxidized retinol and retinoic acid. The hydrophilic analogue of α-tocopherol, Trolox, is substantially less efficient at scavenging retinoid cation radicals than α-tocopherol and urate, but it is more efficient at scavenging the cation radicals of retinoic acid and retinol than δ-tocopherol. The scavenging rate constants indicate that tocopherols can effectively compete with amino acids and proteins for retinoid cation radicals, thereby protecting these important biomolecules from oxidation. Our results provide another mechanism by which tocopherols can diminish the oxidative damage to the skin and retina and thereby protect from skin photosensitivity and the development and/or progression of changes in blinding retinal diseases such as Stargardt’s disease and age-related macular degeneration (AMD).

Sign in / Sign up

Export Citation Format

Share Document