Disease relevance of Fabp7

• BLBP was also detected in EGFR-positive cell lines derived from Nf1:p53 double mutant mice and human MPNST [1].
• To further define the role of MRG on mammary gland differentiation, a MRG transgenic mice model under the control of mouse mammary tumor virus promoter was established and the effect of MRG on mammary gland differentiation was investigated at histological and molecular levels [2].
• Overexpression of MRG in human breast cancer cells induced differentiation with changes in cellular morphology and a significant increase in the production of lipid droplets [3].

High impact information on Fabp7

• Brain lipid-binding protein is a direct target of Notch signaling in radial glial cells [4].
• Affinity-purified anti-BLBP antibodies block glial and neuronal differentiation in primary cell cultures, but have no effect on cell proliferation or adhesion [5].
• The expression of BLBP is spatially and temporally correlated with neuronal differentiation in many parts of the mouse CNS, including postnatal cerebellum, embryonic spinal cord, and cerebral cortex [5].
• In situ hybridization and immunocytochemistry show that BLBP is transiently expressed in radial glia in both the embryonic ventricular zone and the postnatal cerebellum [5].
• PAM14, a novel MRG- and Rb-associated protein, is not required for development and T-cell function in mice [6].

Chemical compound and disease context of Fabp7

• Treatment of human breast cancer cells with the omega-3 PUFA docosahexaenoic acid resulted in a differential growth inhibition proportional to their MRG expression [3].

Biological context of Fabp7

• Interestingly, knocking-down FABP7 function by electroporation of Fabp7 small interfering RNA severely curtailed cell proliferation but promoted neuronal differentiation [7].
• Role of Fabp7, a downstream gene of Pax6, in the maintenance of neuroepithelial cells during early embryonic development of the rat cortex [7].
• Brain lipid binding protein in axon-Schwann cell interactions and peripheral nerve tumorigenesis [1].
• BLBP expression was induced in normal Schwann cells following transfection with EGFR but not H-Ras12V [1].
• Among these is expression of the intermediate filament protein nestin and the brain fatty acid binding protein (B-FABP) [8].

Anatomical context of Fabp7

• We conclude that Fabp7 is a downstream gene of Pax6 transcription factor in the developing rat cortex and essential for maintenance of neuroepithelial cells during early cortical development [7].
• Conversely, reelin addition in vitro increased the Blbp content and process extension of radial glia from the cortex, but not the basal ganglia [9].
• In contrast, an enriched population of multipotential cells, neurosphere cultures derived from the adult or embryonic telencephalon, is immunoreactive for RC2, GLAST, and BLBP [10].
• Following injury, BLBP expression was induced in normal sciatic nerves when nonmyelinating Schwann cells remodeled their processes [1].
• Upon further development, B-FABP was confined to radial glial cells and immature astrocytes [11].

Associations of Fabp7 with chemical compounds

• The partially overlapping expression pattern with that of cellular retinoid binding proteins suggests that B-FABP is involved in the metabolism of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development [11].
• Between 3 h and 1 week after a single injection of permanent S-phase marker bromodeoxyuridine (BrdU), the number of BrdU-labeled BLBP-positive cells did not change, consistent with the idea that both markers here are associated with the maintained precursor cell pool [12].
• The identity of radial glial cells was proven by their immunoreactivity for antibodies against astrocyte-specific glutamate transporter, brain lipid-binding protein, and nestin [13].
• MRG-transfected cells or MRG protein treated cells were much more sensitive to docosahexaenoic acid-induced growth inhibition than MRG-negative or untreated control cells [3].
• Brain B-FABP bound NBD-stearic and cis-parinaric acid with K D values near 0.01 and 0.7 microM, respectively [14].

Regulatory relationships of Fabp7

• Overexpression of exogenous Pax6 mainly induced ectopic expression of Fabp7, rather than of Ngn2, in the early cortical primordium [7].
• A population of slow-dividing neural stem cells (NSCs) residing in the SVZa is identified by its slow cell cycle kinetics (cell cycle approx. 20 days); these cells, called 'S' cells, are negative for glial fibrillary acidic protein and occasionally express brain-lipid-binding protein, a molecular marker of radial glia [15].
• By Western blotting using affinity purified rabbit antibodies raised against the recombinant B-FABP it was demonstrated that in adult mice, B-FABP is predominantly expressed in the olfactory bulb [16].

Other interactions of Fabp7

• In contrast to vimentin, at later stages BLBP and GLAST were found in RG-like cell somata but not in their processes [17].
• B-FABP mRNA and protein were found in glial cells of the peripheral nervous system such as satellite cells of spinal and cranial ganglia and ensheathing cells of the olfactory nerve layer from as early as embryonic day 11 until adulthood [11].
• Although a novel brain-specific fatty acid-binding protein (B-FABP) was recently cloned, the identity of a second fatty acid-binding protein detected with antibodies to the heart (H-FABP) has not been clearly resolved [18].
• In infected brains, we found upregulated expression of genes encoding brain fatty acid binding protein (B-FABP), beta2-microglobulin (beta2m) and, as described previously, the chemokine IP-10 [19].
• Moreover, the colocalization of DPI and brain-type FABP (B-FABP) was observed in most of the non-neuronal supporting cells mentioned above, indicating that DBI and B-FABP are cooperatively involved in the energy metabolism of astrocytes and related cells, which are thought to support neuronal development and functions [20].

Analytical, diagnostic and therapeutic context of Fabp7

• Marked reduction of Fabp7 expression was confirmed by quantitative PCR [7].
• Subcellular localization studies by immunoelectron microscopy demonstrate that BLBP is present in the nucleus as well as the cytoplasm [5].
• Furthermore, we demonstrate that BLBP expression in primary cerebellar glial cells requires coculture with differentiating neurons, and that this induction is regulated by the radial glia-specific element [21].
• In situ hybridization histochemistry revealed B-FABP mRNA in various brain regions, with the highest levels in fiber tracts [22].
• Northern blot analysis using the B-FABP cDNA as a probe established the presence of an abundant mRNA approximately 0.8 kb long in rat brain and in the MOCH-1 oligodendrocyte cell line [22].

References