Fatty acid-binding protein (FABP)

Fatty acid-binding proteins (FABPs) are a family of small (∼15 kDa), highly conserved, cytosolic transport proteins that bind long-chain fatty acids and a variety of other hydrophobic molecules (eicosanoids, retinoids, bile salts, peroxisome proliferators). FABPs operate as intracellular chaperones for fatty acids, facilitating their solubilization, uptake, trafficking, compartmentalization (e.g., mitochondria, endoplasmic reticulum, nucleus), and ultimately participation in metabolic or signaling pathways. There are ten characterized mammalian FABPs, each with distinct tissue specificity, and their diverse roles range from lipid absorption, storage, and oxidation to regulation of gene expression and cell differentiation. Specific FABPs are increasingly recognized as critical modulators in metabolic diseases, inflammation, cardiovascular disorders, cancer, infection, and neurobiology, and are being explored as both disease biomarkers and therapeutic targets, though no FABP inhibitors are currently approved.

Other names

FABPFatty acid-binding protein familyIntracellular lipid-binding proteinFor specific members: FABP1 (liver)FABP2 (intestinal)FABP3 (heart-type)FABP4 (adipocyte)FABP5 (epidermal, also "fatty acid transporter")FABP7 (brain)etc.

Inhibition of fatty acid binding and transport within cells; Modulation of lipid-mediated signaling pathways; Disruption of gene expression mediated by lipid/FABP complexes; Alteration of metabolic and inflammatory pathway activation.