Document Detail


Ligand specificity and conformational stability of human fatty acid-binding proteins.
MedLine Citation:
PMID:  11461829     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fatty acid binding proteins (FABPs) are small cytosolic proteins with virtually identical backbone structures that facilitate the solubility and intracellular transport of fatty acids. At least eight different types of FABP occur, each with a specific tissue distribution and possibly with a distinct function. To define the functional characteristics of all eight human FABPs, viz. heart (H), brain (B), myelin (M), adipocyte (A), epidermal (E), intestinal (I), liver (L) and ileal lipid-binding protein (I-LBP), we studied their ligand specificity, their conformational stability and their immunological crossreactivity. Additionally, binding of bile acids to I-LBP was studied. The FABP types showed differences in fatty acid binding affinity. Generally, the affinity for palmitic acid was lower than for oleic and arachidonic acid. All FABP types, except E-FABP, I-FABP and I-LBP interacted with 1-anilinonaphtalene-8-sulphonic acid (ANS). Only L-FABP, I-FABP and M-FABP showed binding of 11-((5-dimethylaminonaphtalene-1-sulfonyl)amino)undecanoic acid (DAUDA). I-LBP showed increasing binding of bile acids in the order taurine-conjugated>glycine-conjugated>unconjugated bile acids. A hydroxylgroup of bile acids at position 7 decreased and at position 12 increased the binding affinity to I-LBP. The fatty acid-binding affinity and the conformation of FABP types were differentially affected in the presence of urea. Our results demonstrate significant differences in ligand binding, conformational stability and surface properties between different FABP types which may point to a specific function in certain cells and tissues. The preference of I-LBP (but not L-FABP) for conjugated bile acids is in accordance with a specific role in bile acid reabsorption in the ileum.
Authors:
A W Zimmerman; H T van Moerkerk; J H Veerkamp
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The international journal of biochemistry & cell biology     Volume:  33     ISSN:  1357-2725     ISO Abbreviation:  Int. J. Biochem. Cell Biol.     Publication Date:  2001 Sep 
Date Detail:
Created Date:  2001-07-19     Completed Date:  2001-12-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9508482     Medline TA:  Int J Biochem Cell Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  865-76     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University Medical Center Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. a.zimmerman@bioch.kun.nl
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MeSH Terms
Descriptor/Qualifier:
Bile Acids and Salts / metabolism
Carrier Proteins / chemistry*,  metabolism*
Fatty Acid-Binding Proteins
Fatty Acids / metabolism*
Humans
Kinetics
Ligands
Neoplasm Proteins*
Organ Specificity
Protein Conformation
Protein Denaturation
Recombinant Proteins / chemistry,  metabolism
Substrate Specificity
Tumor Suppressor Proteins*
Chemical
Reg. No./Substance:
0/Bile Acids and Salts; 0/Carrier Proteins; 0/FABP1 protein, human; 0/FABP5 protein, human; 0/FABP7 protein, human; 0/Fabp1 protein, mouse; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids; 0/Ligands; 0/Neoplasm Proteins; 0/Recombinant Proteins; 0/Tumor Suppressor Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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