Structural and functional studies on different human FABP types

• Published in: Molecular and cellular biochemistry 1999-02, Vol.192 (1-2), p.137-142
• Main Authors: Veerkamp, J H, van Moerkerk, H T, Prinsen, C F, van Kuppevelt, T H
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Carrier Proteins - chemistry; Carrier Proteins - physiology; Chickens; Dose-Response Relationship, Drug; Epidermis - chemistry; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty acids; Heterogeneity; Humans; Mice; Molecular Sequence Data; Myelin P2 Protein - chemistry; Myelin P2 Protein - physiology; Neoplasm Proteins; Nerve Tissue Proteins; Nutrition; Protein Binding; Rabbits; Recombinant Proteins - metabolism; Rodents; Sequence Homology, Amino Acid; Tissue Distribution; Tretinoin - pharmacology; Tumor Suppressor Proteins; Vitamin A
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1023/a:1006866119264

Interaction of various ligands with recombinant proteins of 5 human FABP types was studied by radiochemical and fluorescence procedures. Liver, heart, intestinal and myelin FABP showed a higher affinity for oleic acid than adipocyte FABP. Intestinal and adipocyte FABP had a relatively high Kd value for arachidonic acid. Liver and intestinal FABP showed high affinity for DAUDA in contrast to the other FABP types. ANS was only well bound by liver and adipocyte FABP. Retinol was not bound by any FABP type, retinoic acid only by adipocyte FABP. Data indicate the importance of both electrostatic and hydrophobic interaction for the ligand-FABP binding. The immunological crossreactivity between six human FABP types including epidermal FABP and their respective antibodies raised in rabbit, chicken and mouse appeared to be low and may suggest heterogeneity of protein surface.