Cellular Retinol and Retinoic Acid-Binding Proteins

2015 ◽  
pp. 27-30
Author(s):  
Frank Chytil
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Retinoic Acid Binding Proteins

scholarly journals Novel Fluorescence Competition Assay for Retinoic Acid Binding Proteins

2018 ◽  
Vol 9 (12) ◽  
pp. 1297-1300 ◽  
Author(s):  
Charles W. E. Tomlinson ◽  
David R. Chisholm ◽  
Roy Valentine ◽  
Andrew Whiting ◽  
Ehmke Pohl
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Competition Assay ◽  
Retinoic Acid Binding Proteins

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 Nuclear Detection of Cellular Retinoic Acid Binding Proteins I and II with New Antibodies

1998 ◽  
Vol 46 (10) ◽  
pp. 1103-1111 ◽  
Author(s):  
Marie-Pierre Gaub ◽  
Yves Lutz ◽  
Norbert B. Ghyselinck ◽  
Isabelle Scheuer ◽  
Véronique Pfister ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Polyclonal Antibodies ◽  
Amino Acid Sequences ◽  
Mouse Embryos ◽  
Low Molecular Weight ◽  
E Coli ◽  
Nuclear Receptor Family ◽  
Retinoic Acid Binding Proteins ◽  
Receptor Family

Apart from the retinoic acid nuclear receptor family, there are two low molecular weight (15 kD) cellular retinoic acid binding proteins, named CRABPI and II. Mouse monoclonal and rabbit polyclonal antibodies were raised against these proteins by using as antigens either synthetic peptides corresponding to amino acid sequences unique to CRABPI or CRABPII, or purified CRABP proteins expressed in E. coli. Antibodies specific for mouse and/or human CRABPI and CRABPII were obtained and characterized by immunocytochemistry and immunoblotting. They allowed the detection not only of CRABPI but also of CRABPII in both nuclear and cytosolic extracts from transfected COS-1 cells, mouse embryos, and various cell lines.

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