title: Recent insights into the biological functions of liver fatty acid binding protein 1.
abstract: Over four decades have passed since liver fatty acid binding protein (FABP)1 was first isolated. There are few protein families for which most of the complete tertiary structures, binding properties, and tissue occurrences are described in such detail and yet new functions are being uncovered for this protein. FABP1 is known to be critical for fatty acid uptake and intracellular transport and also has an important role in regulating lipid metabolism and cellular signaling pathways. FABP1 is an important endogenous cytoprotectant, minimizing hepatocyte oxidative damage and interfering with ischemia-reperfusion and other hepatic injuries. The protein may be targeted for metabolic activation through the cross-talk among many transcriptional factors and their activating ligands. Deficiency or malfunction of FABP1 has been reported in several diseases. FABP1 also influences cell proliferation during liver regeneration and may be considered as a prognostic factor for hepatic surgery. FABP1 binds and modulates the action of many molecules such as fatty acids, heme, and other metalloporphyrins. The ability to bind heme is another cytoprotective property and one that deserves closer investigation. The role of FABP1 in substrate availability and in protection from oxidative stress suggests that FABP1 plays a pivotal role during intracellular bacterial/viral infections by reducing inflammation and the adverse effects of starvation (energy deficiency).
authors.affiliation: Jiangxi Normal University, Nanchang, Jiangxi, People's Republic of China Department of Biology, University of North Carolina at Charlotte, Charlotte, NC Carolinas HealthCare System, Charlotte, NC burczyn@cc.umanitoba.ca guqiwang@yahoo.com.
authors.forename: GuQi
authors.initials: G
authors.lastname: Wang
authors.affiliation: Department of Biology, University of North Carolina at Charlotte, Charlotte, NC Carolinas HealthCare System, Charlotte, NC Wake Forest Baptist Medical Center, Winston-Salem, NC.
authors.forename: Herbert L
authors.initials: HL
authors.lastname: Bonkovsky
authors.affiliation: Carolinas HealthCare System, Charlotte, NC Wake Forest Baptist Medical Center, Winston-Salem, NC.
authors.forename: Andrew
authors.initials: A
authors.lastname: de Lemos
authors.affiliation: Faculty of Pharmacy, University of Manitoba, Winnipeg, Manitoba, Canada burczyn@cc.umanitoba.ca guqiwang@yahoo.com.
authors.forename: Frank J
authors.initials: FJ
authors.lastname: Burczynski
mesh_terms: D000818:Animals; D050556:Fatty Acid-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D050356:Lipid Metabolism / Q000235:genetics / Q000502:physiology; D008099:Liver / Q000378:metabolism*; D018384:Oxidative Stress / Q000235:genetics / Q000502:physiology
chemical_list: D050556:Fatty Acid-Binding Proteins
keywords: fatty liver; heme; infection; inflammation; liver regeneration; metalloporphyrins; nonalcoholic fatty liver disease; oxidative stress; steatosis