Validation of the Binding Site Structure of the Cellular Retinol-Binding Protein (CRBP) by Ligand NMR Chemical Shift Perturbations

2005 ◽  
Vol 127 (15) ◽  
pp. 5310-5311 ◽  
Author(s):  
Bing Wang ◽  
Kenneth M. Merz
Keyword(s):  
Chemical Shift ◽  
Binding Site ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Nmr Chemical Shift ◽  
Site Structure ◽  
Cellular Retinol Binding Protein

scholarly journals Retinol bound to cellular retinol-binding protein is a substrate for cytosolic retinoic acid synthesis.

1993 ◽  
Vol 268 (36) ◽  
pp. 27133-27142
Author(s):  
S Ottonello ◽  
G Scita ◽  
G Mantovani ◽  
D Cavazzini ◽  
G L Rossi
Keyword(s):  
Retinoic Acid ◽  
Binding Protein ◽  
Acid Synthesis ◽  
Retinol Binding Protein ◽  
Cellular Retinol Binding Protein

scholarly journals Molecular basis for the interaction of cellular retinol binding protein 2 (CRBP2) with nonretinoid ligands

2021 ◽  
Vol 62 ◽  
pp. 100054
Author(s):  
Josie A. Silvaroli ◽  
Jacqueline Plau ◽  
Charlie H. Adams ◽  
Surajit Banerjee ◽  
Made Airanthi K. Widjaja-Adhi ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Cellular Retinol Binding Protein

Fluorescence studies of rat cellular retinol binding protein II produced in Escherichia coli: an analysis of four tryptophan substitution mutants

Biochemistry ◽  
1992 ◽  
Vol 31 (8) ◽  
pp. 2376-2383 ◽  
Author(s):  
Bruce C. Locke ◽  
Jean M. MacInnis ◽  
Shi Jun Qian ◽  
Jeffrey I. Gordon ◽  
Ellen Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Fluorescence Studies ◽  
Cellular Retinol Binding Protein

scholarly journals Teq I RFLP in the human cellular retinol-binding protein (CRBP) gene

1988 ◽  
Vol 16 (15) ◽  
pp. 7758-7758
Author(s):  
A. Pellegrino ◽  
S. Garofalo ◽  
S. Cocozza ◽  
A. Monticelli ◽  
R. Faraonio ◽  
...  
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Cellular Retinol Binding Protein

Cellular Retinol-binding Protein in Mucosa, in Benign and Malignant Non-squamous Cell Tumours of the Head and Neck

1989 ◽  
Vol 107 (3-4) ◽  
pp. 313-320 ◽  
Author(s):  
Peter Wahlberg ◽  
Göran Fex ◽  
Johan Wennerberg ◽  
Roger Willén
Keyword(s):  
Head And Neck ◽  
Squamous Cell ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Cellular Retinol Binding Protein

scholarly journals Cellular retinol-binding protein type III is a PPARγ target gene and plays a role in lipid metabolism

2008 ◽  
Vol 295 (6) ◽  
pp. E1358-E1368 ◽  
Author(s):  
Cynthia F. Zizola ◽  
Gary J. Schwartz ◽  
Silke Vogel
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Lipid Metabolism ◽  
Free Fatty Acid ◽  
Target Gene ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Wild Type ◽  
Type Iii ◽  
Cellular Retinol Binding Protein

Cellular retinol-binding protein (CRBP) type III (CRBP-III) belongs to the family of intracellular lipid-binding proteins, which includes the adipocyte-binding protein aP2. In the cytosol, CRBP-III binds retinol, the precursor of retinyl ester and the active metabolite retinoic acid. The goal of the present work is to understand the regulation of CRBP-III expression and its role in lipid metabolism. Using EMSAs, luciferase reporter assays, and chromatin immunoprecipitation assays, we found that CRBP-III is a direct target of peroxisome proliferator-activated receptor-γ (PPARγ). Moreover, CRBP-III expression was induced in adipose tissue of mice after treatment with the PPARγ agonist rosiglitazone. To examine a potential role of CRBP-III in regulating lipid metabolism in vivo, CRBP-III-deficient (C-III-KO) mice were maintained on a high-fat diet (HFD). Hepatic steatosis was decreased in HFD-fed C-III-KO compared with HFD-fed wild-type mice. These differences were partly explained by decreased serum free fatty acid levels and decreased free fatty acid efflux from adipose tissue of C-III-KO mice. In addition, the lack of CRBP-III was associated with reduced food intake, increased respiratory energy ratio, and altered body composition, with decreased adiposity and increased lean body mass. Furthermore, expression of genes involved in mitochondrial fatty acid oxidation in brown adipose tissue was increased in C-III-KO mice, and C-III-KO mice were more cold tolerant than wild-type mice fed an HFD. In summary, we demonstrate that CRBP-III is a PPARγ target gene and plays a role in lipid and whole body energy metabolism.

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