The expression pattern of a novel gene encoding brain-fatty acid binding protein correlates with neuronal and glial cell development

Abstract

Fatty acid binding proteins (FABPs) are a multigene family of small intracellular proteins that bind hydrophobic ligands. In this report we describe the cloning and expression pattern of a novel member of this gene family that is specifically expressed in the developing and adult nervous system and thus was designated brain (B)-FABP. B-FABP is closely related to heart (H)-FABP with 67% amino acid identity. B-FABP expression was first detected at mouse embryonic day 10 in neuroepithelial cells and its pattern correlates with early neuronal differentiation. Upon further development, B-FABP was confined to radial glial cells and immature astrocytes. 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. In the adult mouse brain, B-FABP was found in the glia limitans, in radial glial cells of the hippocampal dentate gyrus and Bergman glial cells. These findings suggest a function of B-FABP during neurogenesis or neuronal migration in the developing nervous system. 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.

Isoforms of Rat Liver Fatty Acid Binding Protein Differ in Structure and Affinity for Fatty Acids and Fatty Acyl CoAs

“…Liver fatty acid binding protein (L-FABP) is one of nearly twenty 14-15 kDa fatty acid binding proteins [reviewed in Veerkamp and Maatman (1995), Banaszak et al (1994), Borchers and Spener (1994), and Matarese et al (1989)]. Many of these FABPs have been identified as distinct types in a variety of tissues including liver, heart, intestine [reviewed in Borchers and Spener (1994), and Paulussen and Veerkamp (1990)], adipose tissue (Dutta-Roy et al, 1993;Matarese et al, 1989), and brain (Myers-Payne et al, 1996;Kurtz et al, 1994;Feng et al, 1994). Despite the absence of conclusive evidence for the physiological role of FABPs, much information has been reported over the last 30 years suggesting potential FABP functions [reviewed in Clarke and Armstrong (1989), Bass (1988), Glatz et al (1993), Ockner et al (1992), Veerkamp et al (1993), Issemann et al (1992), Veerkamp (1995), Borchers and Spener (1994), and Paulussen and Veerkamp (1990)].…”

Expression, Purification, and Ligand-Binding Analysis of Recombinant Keratinocyte Lipid-Binding Protein (MAL-1), an Intracellular Lipid-Binding Protein Found Overexpressed in Neoplastic Skin Cells

“…Recently, differential screening of a murine skin squamous cell carcinoma library resulted in the isolation of a cDNA that is predicted to encode a new member of the iLBP family termed keratinocyte lipid-binding protein, KLBP (previously called Mal-1) (Krieg et al, 1993). The predicted sequence of the KLBP exhibits between 50%-60% identity and 60%-70% similarity with the amino acid sequence of several iLBPs, including the adipocyte LBP (Matarese & Bernlohr, 1988), myelin P2 (Narayanan et al, 1988) ( Schmitt et al, 1994), brain FABP (Kurtz et al, 1994), heart FABP (Claffey et al, 1987), psoriasis-activated FABP (Madsen et al, 1992), cutaneous FABP (Watanabe et al, 1994), and epidermal FABP (Siegenthaler et al, 1994). In addition, KLBP has significant sequence similarity (∼35% identity, 40%-45% similarity) with cellular retinoic acid binding proteins I and II (Krieg et al, 1993).…”

A multi-omics approach to visualize early neuronal differentiation in 4D

“…For R14, consisting of 27 Day 0 cells, we used KPNA2 , a gene associated with the localization of OCT4 (Li et al, 2008). For R15, a pool of 90 cells from Days 7, 13 and 20, we used FABP7 , which is expressed in NSCs during development (Kurtz et al, 1994).…”