Abstract
Adipocyte fatty acid-binding protein (A-FABP), which is also known as ap2 or FABP4, is a fatty acid chaperone that has been further defined as a fat-derived hormone. It regulates lipid homeostasis and is a key mediator of inflammation. Circulating levels of A-FABP are closely associated with metabolic syndrome and cardiometabolic diseases with imminent diagnostic and prognostic significance. Numerous animal studies have elucidated the potential underlying mechanisms involving A-FABP in these diseases. Recent studies demonstrated its physiological role in the regulation of adaptive thermogenesis and its pathological roles in ischemic stroke and liver fibrosis. Due to its implication in various diseases, A-FABP has become a promising target for the development of small molecule inhibitors and neutralizing antibodies for disease treatment. This review summarizes the clinical and animal findings of A-FABP in the pathogenesis of cardio-metabolic diseases in recent years. The underlying mechanism and its therapeutic implications are also highlighted.
Highlights
Serum Adipocyte fatty acid-binding protein (A-Fatty acid-binding proteins (FABPs)) levels were significantly correlated with glycated hemoglobin 1c (HbA1c)
Serum A-FABP levels were positively correlated with carotid intima-media thickness (CIMT) in both sexes, but an independent association was only observed in women
A-FABP levels are independently associated with carotid atherosclerosis in women
Summary
Fatty acid-binding proteins (FABPs) belong to the lipocalin family and are a group of. 14–15 kDa proteins involved in intracellular lipid homeostasis as well as metabolic and inflammatory pathways [1,2]. They are ubiquitously expressed in body organs/tissues, including the liver, intestine, heart, adipose tissue, epidermis, ileum, brain, myelin, and testis [2]. Despite the considerable variation in protein sequences, FABPs share similar tertiary structures: a beta-barrel domain and an internal water-filled cavity, where hydrophobic ligands, such as long-chain fatty acid and eicosanoids, are bound to with high affinity [3,4]. FABPs function as lipid chaperones to transport lipids to specific organelles, such as the endoplasmic reticulum (ER) and mitochondria, within the cell [1]
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