Fatty acid-binding proteins of nervous tissue

• Published in: Journal of molecular neuroscience 2001-04, Vol.16 (2-3), p.133-142
• Main Authors: Veerkamp, J H, Zimmerman, A W
• Format: Article
• Language: English
• Subjects: Adult; Animals; Antibody Specificity; Biological Transport; Brain - embryology; Brain - metabolism; Carrier Proteins - classification; Carrier Proteins - genetics; Carrier Proteins - immunology; Carrier Proteins - physiology; Cell Membrane - metabolism; Chylomicrons - metabolism; Cross Reactions; Energy Metabolism; Epitopes - immunology; Fatty Acid Binding Protein 3; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids - metabolism; Fatty Acids, Unsaturated; Fetal Proteins - metabolism; Gene Expression Regulation, Developmental; Humans; Lipoproteins, VLDL - metabolism; Liposomes - metabolism; Mice; Mitochondria - metabolism; Models, Biological; Multigene Family; Myelin Sheath - metabolism; Neoplasm Proteins; Nerve Crush; Nerve Regeneration; Nerve Tissue Proteins - classification; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - immunology; Nerve Tissue Proteins - physiology; Neuroglia - metabolism; Peripheral Nerves - metabolism; Peroxisomes - metabolism; Protein Binding; Protein Isoforms - genetics; Protein Isoforms - metabolism; Proteins; Rats; Recombinant Proteins - metabolism; RNA, Messenger - biosynthesis; Sciatic Nerve - physiology; Structure-Activity Relationship; Substrate Specificity; Tumor Suppressor Proteins
• ISSN: 0895-8696; 0895-8696; 1559-1166
• DOI: 10.1385/jmn:16:2-3:133

Fatty acid-binding proteins (FABPs) are cytosolic 14-15 kDa proteins, which are supposed to be involved in fatty acid (FA) uptake, transport, and targeting. They may modulate FA concentration and in this way influence function of enzymes, membranes, ion channels and receptors, and gene expression and cellular growth and differentiation. Nine FABP types can be discerned with a specific tissue distribution. In spite of 30-70% amino acid sequence identity, they have a similar tertiary, beta-clam structure in which the FA is bound. Nervous tissue contains four FABP types with a distinct spatio-temporal distribution. Myelin (M)-FABP is only present in the peripheral nerves, brain (B)-FABP and epidermal (E)-FABP mainly in glial cells and neurons, respectively of pre- and perinatal brain, and heart (H)-FABP in adult brain. Possible functions of FABPs in the nervous system are discussed. Binding studies with a range of physiological FA showed no large differences between recombinant proteins of the four human FABP types in binding specificity and affinity, also not for polyunsaturated FA (PUFA). The transfer of FA from fixed liposomes to mitochondria was similarly promoted by the four types. A marked difference in conformational stability was observed with H-FABP > B-FABP > M-FABP > E-FABP. Surface epitopes of H-FABP showed reaction with anti-B-FABP antibodies, but no other cross-reactivity of FABP type and heterologous antibodies was observed. The functional significance of the distinct spatio-temporal pattern of the four FABP types remains to be elucidated.