Fatty acid-binding protein 1 (FABP1) (FABP1)

Fatty acid-binding protein 1 (FABP1), commonly known as Liver-type FABP (L-FABP), is a low-molecular-weight cytosolic protein primarily expressed in the liver, but also found in the kidneys and intestines [1, 5]. It belongs to a family of intracellular lipid chaperones that facilitate the uptake, transport, and metabolism of long-chain fatty acids and other hydrophobic ligands, such as heme and bilirubin [3, 6]. FABP1 plays a critical role in systemic lipid homeostasis by shuttling ligands to the nucleus, where they activate peroxisome proliferator-activated receptors (PPARs) to regulate gene expression [4, 13]. In disease states, FABP1 is implicated in the pathogenesis of metabolic dysfunction-associated steatohepatitis (MASH), nonalcoholic fatty liver disease (NAFLD), and chronic kidney disease [7, 11, 20]. It also serves as a clinically significant biomarker; for instance, urinary L-FABP levels are used to monitor acute kidney injury and the progression of renal disease [6, 11]. Pharmacologically, FABP1 interacts with hypolipidemic drugs like fibrates and is being actively investigated as a therapeutic target for metabolic and inflammatory disorders [1, 4, 8]. Inhibition of FABP1 has shown potential in reducing hepatic steatosis, inflammation, and fibrosis in preclinical models [7].

Other names

Liver-type fatty acid-binding proteinL-FABPFABPL

FABP1 acts as an intracellular lipid chaperone that binds and transports long-chain fatty acids, heme, and other lipophilic ligands to specific cellular compartments, including the nucleus where it directly interacts with and activates peroxisome proliferator-activated receptors (PPARs) to modulate lipid metabolism and inflammatory gene expression [1, 4, 13].