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

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.

scholarly journals Investigation on the Binding and Conformational Change of All-trans-Retinoic Acid with Peptidyl Prolyl cis/trans Isomerase Pin1 Using Spectroscopic and Computational Techniques

2021 ◽  
Vol 2021 ◽  
pp. 1-13
Author(s):  
GuoFei Zhu ◽  
ShaoLi Lyu ◽  
Yang Liu ◽  
Chao Ma ◽  
Wang Wang
Keyword(s):  
Retinoic Acid ◽  
Conformational Change ◽  
Conformational Changes ◽  
Fluorescence Spectra ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Principal Component ◽  
Computational Techniques ◽  
Trans Retinoic Acid ◽  
All Trans Retinoic Acid

Binding and conformational change of all-trans-retinoic acid (ATRA) with peptidyl prolyl cis/trans isomerase Pin1 were investigated systematically by spectroscopic and computational techniques under experimentally optimized physiological conditions. The intrinsic fluorescence of Pin1 was quenched through a static quenching mechanism in the presence of ATRA with binding constants on the order of 105 mol/L. Thermodynamic parameters (ΔH = 15.76 kJ/mol and ΔS = 158.36 J/mol·K at 293 K) and computational results illustrated that the hydrophobic interactions played a significant role in the binding process of ATRA to Pin1, but electrostatic forces, weak van der Waals, and hydrogen bonds cannot be ignored. Circular dichroism, fluorescence spectra, and computational simulations revealed that ATRA interacted with residues Lys63 and Arg69 of Pin1 to affect its conformational changes. Molecular dynamic simulation, principal component analysis, and free energy landscape monitored the dynamical conformational characteristics of ATRA binding to Pin1. All in all, the present research might provide a reference for the development and design of retinoic acid drugs that inhibit the activity of Pin1.

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

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

Photochromism, Kinetics and Fluorescence of 1-(2-methyl-3-benzofuranyl)-2-[2-methyl-5-(4-cyanophenyl)-3-thienyl]perfluorocyclopentene

2014 ◽  
Vol 886 ◽  
pp. 175-178
Author(s):  
Dan Dan Xue ◽  
Zhi Yuan Sun ◽  
Shou Zhi Pu
Keyword(s):  
Fluorescence Intensity ◽  
Fluorescence Spectra ◽  
Uv Light ◽  
Photochromic Properties ◽  
Strong Fluorescence ◽  
Open Ring ◽  
Kinetics Of ◽  
Hexane Solution

An unsymmetrical photochromic diarylethene compound, 1-(2-methyl-3-benzofuranyl)-2-[2-methyl-5-(4-cyanophenyl)-3-thienyperfluorocyclopentene was synthesized, and its photochromic properties, kinetics of the photochromic cyclization/cycloreversion and fluorescence were investigated in detail. The compound exhibited good photochromism, changing from colorless to red after irradiation with 297 nm UV light, in which absorption maxima were observed at 530 nm in hexane solution. Simultaneously, cyclization/cycloreversion kinetics of this diarylethene was researched. The open-ring isomer of the diarylethene exhibited relatively strong fluorescence at 377 nm in hexane solution (2 × 10-5 mol L-1), when excited at 327 nm. The fluorescence intensity decreased along with the photochromism upon irradiation with 297 nm light. The fluorescence spectra of the diarylethene are depended on the concentration.

Kinetics of camptothecin hydrolysis determined by PCA and FA analysis of fluorescence spectra

2003 ◽  
Author(s):  
Stefan Kruszewski ◽  
Ryszard Siuda ◽  
Blanka Ziomkowska ◽  
Michal Cyrankiewicz
Keyword(s):  
Fluorescence Spectra ◽  
Kinetics Of
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