Fatty acid-binding proteins of nervous tissue
- PMID: 11478368
- DOI: 10.1385/JMN:16:2-3:133
Fatty acid-binding proteins of nervous tissue
Abstract
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.
Similar articles
-
Fatty acid binding proteins from different tissues show distinct patterns of fatty acid interactions.Biochemistry. 2000 Jun 20;39(24):7197-204. doi: 10.1021/bi000314z. Biochemistry. 2000. PMID: 10852718
-
Effect of fatty acid-binding proteins on intermembrane fatty acid transport studies on different types and mutant proteins.Eur J Biochem. 2000 Oct;267(19):5959-66. doi: 10.1046/j.1432-1327.2000.01665.x. Eur J Biochem. 2000. PMID: 10998056
-
Collision-mediated transfer of long-chain fatty acids by neural tissue fatty acid-binding proteins (FABP): studies with fluorescent analogs.J Mol Neurosci. 2001 Apr-Jun;16(2-3):143-50; discussion 151-7. doi: 10.1385/JMN:16:2-3:143. J Mol Neurosci. 2001. PMID: 11478369
-
Cytoplasmic fatty acid-binding protein facilitates fatty acid utilization by skeletal muscle.Acta Physiol Scand. 2003 Aug;178(4):367-71. doi: 10.1046/j.1365-201X.2003.01166.x. Acta Physiol Scand. 2003. PMID: 12864741 Review.
-
New insights into the structure and function of fatty acid-binding proteins.Cell Mol Life Sci. 2002 Jul;59(7):1096-116. doi: 10.1007/s00018-002-8490-y. Cell Mol Life Sci. 2002. PMID: 12222958 Free PMC article. Review.
Cited by
-
Modeling of pathological traits in Alzheimer's disease based on systemic extracellular signaling proteome.Mol Cell Proteomics. 2011 Oct;10(10):M111.008862. doi: 10.1074/mcp.M111.008862. Epub 2011 Jul 8. Mol Cell Proteomics. 2011. PMID: 21742799 Free PMC article.
-
Fatty acid binding proteins are novel modulators of synaptic epoxyeicosatrienoic acid signaling in the brain.Sci Rep. 2023 Sep 14;13(1):15234. doi: 10.1038/s41598-023-42504-4. Sci Rep. 2023. PMID: 37709856 Free PMC article.
-
FABP3, FABP4, and heart rate variability among patients with chronic schizophrenia.Front Endocrinol (Lausanne). 2023 May 15;14:1165621. doi: 10.3389/fendo.2023.1165621. eCollection 2023. Front Endocrinol (Lausanne). 2023. PMID: 37255976 Free PMC article.
-
Salivary and Lacrimal Gland Alterations of the Epidermal Fatty Acid-Binding Protein (E-FABP) in Non-Obese Diabetic Mice.Int J Mol Sci. 2022 Mar 23;23(7):3491. doi: 10.3390/ijms23073491. Int J Mol Sci. 2022. PMID: 35408851 Free PMC article.
-
cDNA microarray analysis of changes in gene expression induced by neuronal hypoxia in vitro.Neurochem Res. 2002 Oct;27(10):1105-12. doi: 10.1023/a:1020913123054. Neurochem Res. 2002. PMID: 12462408
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous