FABP1 Human

Fatty Acid Binding Protein-1 (FABP1), also known as liver-type fatty acid-binding protein (L-FABP), is a member of the fatty acid-binding protein family. These proteins are small, highly conserved cytoplasmic proteins that play a crucial role in the binding, transport, and metabolism of long-chain fatty acids (LCFAs) and other hydrophobic molecules .

The fatty acid-binding proteins were first discovered in 1972 during experiments aimed at identifying a soluble fatty acid carrier in the enterocyte responsible for intestinal absorption of LCFAs . The human FABP1 gene is located on the short (p) arm of chromosome 2, from base pair 88,122,982 to base pair 88,128,131 .

FABP1 has a unique structure compared to other members of the FABP family. It consists of ten antiparallel beta strands that form a barrel with a larger binding pocket, allowing it to accommodate multiple ligands simultaneously . This structure enables FABP1 to bind a wider range of hydrophobic ligands, including bilirubin, monoglycerides, bile acids, and fatty acyl CoA .

FABP1 is primarily expressed in the liver, where it accounts for 7-11% of the total cytosolic protein . It is also found in the intestine, kidney, pancreas, stomach, and lung . The protein plays a significant role in the binding, transport, and metabolism of LCFAs, endocannabinoids, phytocannabinoids, and other hydrophobic molecules . FABP1 is unique in its ability to bind a diverse range of ligands, which helps prevent cytotoxicity by binding potentially toxic molecules such as heme and fatty acids .

Altered expression of FABP1 has been linked to various metabolic conditions, including obesity and non-alcoholic fatty liver disease (NAFLD) . The human FABP1 T94A variant, a single nucleotide polymorphism, is associated with altered body mass index (BMI), clinical dyslipidemias, atherothrombotic cerebral infarction, and NAFLD . Understanding the role of FABP1 and its variants in these conditions is crucial for developing targeted therapies.