scholarly journals Validation of Recombinant Chicken Liver Bile Acid Binding Protein as a Tool for Cholic Acid Hosting

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 645
Author(s):  
Giusy Tassone ◽  
Maurizio Orlandini ◽  
Massimo Olivucci ◽  
Cecilia Pozzi
Keyword(s):  
Bile Acid ◽  
High Resolution ◽  
Affinity Chromatography ◽  
Bile Acids ◽  
Drug Carriers ◽  
Chicken Liver ◽  
Purification Procedure ◽  
Acid Binding Protein ◽  
Bile Acid Binding ◽  
Exogenous Substances

Bile acids (BAs) are hydroxylated steroids derived from cholesterol that act at the intestinal level to facilitate the absorption of several nutrients and also play a role as signaling molecules. In the liver of various vertebrates, the trafficking of BAs is mediated by bile acid-binding proteins (L-BABPs). The ability to host hydrophobic or amphipathic molecules makes BABPs suitable for the distribution of a variety of physiological and exogenous substances. Thus, BABPs have been proposed as drug carriers, and more recently, they have also been employed to develop innovative nanotechnology and biotechnology systems. Here, we report an efficient protocol for the production, purification, and crystallization of chicken liver BABP (cL-BABP). By means of target expression as His6-tag cL-BABP, we obtained a large amount of pure and homogeneous proteins through a simple purification procedure relying on affinity chromatography. The recombinant cL-BABP showed a raised propensity to crystallize, allowing us to obtain its structure at high resolution and, in turn, assess the structural conservation of the recombinant cL-BABP with respect to the liver-extracted protein. The results support the use of recombinant cL-BABP for the development of drug carriers, nanotechnologies, and innovative synthetic photoswitch systems.

Conformational and dynamics changes induced by bile acids binding to chicken liver bile acid binding protein

2008 ◽  
Vol 71 (4) ◽  
pp. 1889-1898 ◽  
Author(s):  
Ivano Eberini ◽  
Alessandro Guerini Rocco ◽  
Anna Rita Ientile ◽  
António M. Baptista ◽  
Elisabetta Gianazza ◽  
...  
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Binding Protein ◽  
Chicken Liver ◽  
Acid Binding Protein ◽  
Bile Acid Binding

scholarly journals NMR-based modeling and binding studies of a ternary complex between chicken liver bile acid binding protein and bile acids

2007 ◽  
Vol 69 (1) ◽  
pp. 177-191 ◽  
Author(s):  
Simona Tomaselli ◽  
Laura Ragona ◽  
Lucia Zetta ◽  
Michael Assfalg ◽  
Pasquale Ferranti ◽  
...  
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Ternary Complex ◽  
Binding Protein ◽  
Chicken Liver ◽  
Binding Studies ◽  
Acid Binding Protein ◽  
Bile Acid Binding

Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein

2008 ◽  
Vol 21 (5) ◽  
pp. 348-354 ◽  
Author(s):  
Piero Ricchiuto ◽  
Alessandro Guerini Rocco ◽  
Elisabetta Gianazza ◽  
Dario Corrada ◽  
Tiziana Beringhelli ◽  
...  
Keyword(s):  
Bile Acid ◽  
Molecular Recognition ◽  
Binding Protein ◽  
Chicken Liver ◽  
Water Molecules ◽  
Acid Binding Protein ◽  
Bile Acid Binding

Bile acids regulate the ontogenic expression of ileal bile acid binding protein in the rat via the farnesoid X receptor

2002 ◽  
Vol 122 (5) ◽  
pp. 1483-1492 ◽  
Author(s):  
Sandy T. Hwang ◽  
Nancy L. Urizar ◽  
David D. Moore ◽  
Susan J. Henning
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Binding Protein ◽  
Farnesoid X Receptor ◽  
Acid Binding Protein ◽  
Bile Acid Binding ◽  
Ontogenic Expression

scholarly journals NMR Dynamic Studies Suggest that Allosteric Activation Regulates Ligand Binding in Chicken Liver Bile Acid-binding Protein

2006 ◽  
Vol 281 (14) ◽  
pp. 9697-9709 ◽  
Author(s):  
Laura Ragona ◽  
Maddalena Catalano ◽  
Marianna Luppi ◽  
Daniel Cicero ◽  
Tommaso Eliseo ◽  
...  
Keyword(s):  
Bile Acid ◽  
Ligand Binding ◽  
Binding Protein ◽  
Chicken Liver ◽  
Allosteric Activation ◽  
Acid Binding Protein ◽  
Dynamic Studies ◽  
Bile Acid Binding

Chicken Liver Bile Acid-Binding Protein Is in a Compact Partly Folded State at Acidic pH. Its Relevance to the Interaction with Lipid Membranes†

Biochemistry ◽  
2005 ◽  
Vol 44 (23) ◽  
pp. 8486-8493 ◽  
Author(s):  
Verónica Nolan ◽  
Massimiliano Perduca ◽  
Hugo L. Monaco ◽  
Guillermo G. Montich
Keyword(s):  
Bile Acid ◽  
Lipid Membranes ◽  
Binding Protein ◽  
Chicken Liver ◽  
Acidic Ph ◽  
Acid Binding Protein ◽  
Bile Acid Binding

Structural and Dynamic Determinants of Ligand Binding in the Ternary Complex of Chicken Liver Bile Acid Binding Protein with Two Bile Salts Revealed by NMR†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (44) ◽  
pp. 12557-12567 ◽  
Author(s):  
Tommaso Eliseo ◽  
Laura Ragona ◽  
Maddalena Catalano ◽  
Michael Assfalg ◽  
Maurizio Paci ◽  
...  
Keyword(s):  
Bile Acid ◽  
Ligand Binding ◽  
Bile Salts ◽  
Ternary Complex ◽  
Binding Protein ◽  
Chicken Liver ◽  
Acid Binding Protein ◽  
Bile Acid Binding

scholarly journals Regulation of expression of human intestinal bile acid-binding protein in Caco-2 cells

1998 ◽  
Vol 330 (1) ◽  
pp. 261-265 ◽  
Author(s):  
Tatsuo KANDA ◽  
Laurent FOUCAND ◽  
Yuichi NAKAMURA ◽  
Isabelle NIOT ◽  
Philippe BESNARD ◽  
...  
Keyword(s):  
Gene Expression ◽  
Bile Acid ◽  
Western Blot ◽  
Bile Acids ◽  
Transport System ◽  
Binding Protein ◽  
Dependent Manner ◽  
Acid Binding Protein ◽  
Bile Acid Binding ◽  
Active Transport System

Molecular mechanisms of the bile acid active transport system in the ileal enterocytes remain unknown. We examined whether bile acids affect human enterocyte gene expression of intestinal bile acid-binding protein (I-BABP), a component of this transport system. Differentiated Caco-2 cells were incubated in the presence of human bile, bile acids or other lipids. The level of I-BABP expression was evaluated by Northern and Western blot analyses. A 24 h incubation of Caco-2 cells in a medium containing either bile or bile acids resulted in a remarkable 7.5-fold increase in the I-BABP mRNA level over the control level. Neither cholesterol, palmitic acid, phosphatidylcholine nor cholestyramine treated bile showed any difference in I-BABP mRNA expression from the control. Bile acid treatment increased the level of I-BABP mRNA in Caco-2 cells in a time- and dose-dependent manner. Western blot analysis showed that this induction led to increase in cytosolic I-BABP. Chenodeoxycholic acid and deoxycholic acid showed greater induction effects than other hydrophilic bile acids, including their own glycine conjugates. Pretreatment by actinomycin D or cycloheximide completely inhibited the up-regulation of I-BABP expression by bile acid. Bile acids, especially lipophilic bile acids, increase the I-BABP expression in Caco-2-cells, suggesting that luminal bile acids play an important role in regulating the I-BABP gene expression.

Sign in / Sign up

Export Citation Format

Share Document