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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The flight muscle of adult desert locusts, Schistocerca gregaria, contains a fatty acid binding protein (FABP) that is homologous to mammalian M-FABP (cardiac FABP. In spite of the evolutionary distance between invertebrates and vertebrates, locust muscle FABP is similar to cardiac FABP in its amino acid sequence, structure, and binding behavior. While cardiac FABP is present already in the prenatal period, locust FABP is an adult specific protein; its expression is directly linked to metamorphosis. A correlation seems to exist between fatty acid oxidative capacity and FABP content in both locust and mammals. To accomplish the higher metabolic rate encountered during migratory flight, locust flight muscle cytosol contains more than three times as much FABP as that in mammalian heart. Increased fatty acid utilization by exercise or endurance training apparently induces FABP expression. Similarities and differences between vertebrate and invertebrate M-FABP are discussed in light of the proposed functions of muscle FABP as fatty acid transporter and cytoprotectant.
Comp Biochem Physiol B Biochem Mol Biol
PMID:Fatty acid binding protein in locust and mammalian muscle. Comparison of structure, function and regulation. 755 41

M-FABP from flight muscle of the locust, Schistocerca gregaria, is similar to mammalian H-FABP in its physical characteristics and amino acid sequence. We have studied developmental changes using ELISA, Northern Blotting, and EM/immuno-gold techniques. M-FABP is found in cytoplasm and nuclei, but not in mitochondria. It is the most abundant soluble muscle protein in fully developed adult locusts, comprising 18% of the total cytosolic protein. However, no FABP is detectable at the beginning of the adult stage. Its concentration rises dramatically during the next 10 days, after which it reaches its maximal value. Expression apparently is turned on after ecdysis and continues for 10 days; thereafter, FABP mRNA diminishes and reaches a constant, but low level, probably needed to maintain the current FABP level. From a series of experiments employing metamorphosis-controlling hormones and antihormones it is evident that the induction of FABP expression is directly linked to metamorphosis.
Mol Cell Biochem
PMID:Developmental changes of FABP concentration, expression, and intracellular distribution in locust flight muscle. 823 58

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.
J Mol Neurosci
PMID:Fatty acid-binding proteins of nervous tissue. 1147 68

The protein component of the myelin layer is essential for all aspects of peripheral nerves, and its deficiency can lead to structural and functional impairment. The presence of peripheral myelin protein 2 (P2, PMP2, FABP8, M-FABP) in Schwann cells has been known for decades and shown recently to be involved in the lipid homeostasis in the peripheral neural system. However, its precise role during de- and remyelination has yet to be elucidated. To this end, we assessed remyelination after sciatic nerve crush injury in vivo, and in an experimental de/remyelination ex vivo myelinating culture model in P2-deficient (P2 -/- ) and wild-type (WT) animals. In vivo, the nerve crush paradigm revealed temporal structural and functional changes in P2 -/- mice as compared to WT animals. Concomitantly, P2 -/- DRG cultures demonstrated the presence of shorter internodes and enlarged nodes after ex vivo de/remyelination. Together, these data indicate that P2 may play a role in remyelination of the injured peripheral nervous system, presumably by affecting the nodal and internodal configuration.
Cell Mol Neurobiol 2018 Mar
PMID:The Role of Peripheral Myelin Protein 2 in Remyelination. 2844 47