Description
Fatty acid binding protein 1 (FABP1) is one of nine known cytosolic fatty acid binding proteins ranging in size from 14-
15 kDa containing 127-
132 amino acids. Members of this protein family exhibit high affinity for small lipophilic ligands and were named according to the tissue from which they were initially isolated. Studies suggest that FABPs are involved in the uptake and metabolism of fatty acids, in the maintenance of cellular membrane fatty acid levels, in intracellular trafficking of these substrates, in the modulation of specific enzymes of lipid metabolic pathways, and in the modulation of cell growth and differentiation. FABP family members have highly conserved three dimensional structures and 22-
73% amino acid sequence similarity. FABP1 is composed of ten antiparallel β strands that form a barrel and have a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acids into its binding pocket. Expression of FABP1 is decreased in hepatoblastoma and hepatocellular carcinoma making the protein a potential tumor marker. Moreover, studies have suggested FABP1 as a potential biomarker for both liver and kidney injury.
Background
Human Fatty Epidermal Acid Binding Protein FABP also called FABP-5 is a 15 kD member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds ( bile acids or retinoids). In an internal cavity. The fatty acid binding proteins aP2 (fatty acid binding protein [FABP]-4) and mal1 (EFABP) are closely related and both are expressed in adipocytes.
References
[1] AMY REESE-WAGONER Leonard B James Thompson. Structural properties of the adipocyte lipid binding protein[J]. Biochimica et biophysica acta. Molecular and cell biology of lipids, 1999, 1441 2: Pages 106-116. DOI:
10.1016/s1388-1981(99)00154-7[2] CHERYL A. BAXA. Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA[J]. Biochemistry Biochemistry, 1989, 28 22: 8683-8690. DOI:
10.1021/bi00448a003[3] MARK A. PERRELLA. Absence of adipocyte fatty acid binding protein prevents the development of accelerated atherosclerosis in hypercholesterolemic mice[J]. FASEB Journal, 2001, 15 10: 1774-1776. DOI:
10.1096/fj.01-0017fje[4] K. UYSAL. Improved glucose and lipid metabolism in genetically obese mice lacking aP2.[J]. Endocrinology, 2000, 27 1: 3388-3396. DOI:
10.1210/en.141.9.3388[5] GKHAN S. HOTAMISLIGIL. Uncoupling of Obesity from Insulin Resistance Through a Targeted Mutation in aP2, the Adipocyte Fatty Acid Binding Protein[J]. Science, 1996, 274 5291. DOI:
10.1126/science.274.5291.1377[6] DONG GUO. FABP4 secreted by M1-polarized macrophages promotes synovitis and angiogenesis to exacerbate rheumatoid arthritis.[J]. Bone Research, 2022, 10 1: 45. DOI:
10.1038/s41413-022-00211-2[7] C BASTIE. Expression of peroxisome proliferator-activated receptor PPARdelta promotes induction of PPARgamma and adipocyte differentiation in 3T3C2 fibroblasts.[J]. The Journal of Biological Chemistry, 1999, 274 31: 21920-21925. DOI:
10.1074/jbc.274.31.21920[8] G P LIM. Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer’s disease.[J]. Journal of Neuroscience, 2000, 20 15: 5709-5714.
[9] YAQIN ZHANG. High expression of FABP4 and FABP6 in patients with colorectal cancer[J]. World Journal of Surgical Oncology, 2019. DOI:
10.1186/s12957-019-1714-5