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Gene Review

Fabp4  -  fatty acid binding protein 4, adipocyte

Mus musculus

Synonyms: 3T3-L1 lipid-binding protein, 422/aP2, A-FABP, AFABP, ALBP, ...
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Disease relevance of Fabp4

  • Apoe-/- mice with Ap2+/+ adipocytes and Ap2-/- macrophages generated by bone-marrow transplantation showed a comparable reduction in atherosclerotic lesions to those with total aP2 deficiency, indicating an independent role for macrophage aP2 in atherogenesis [1].
  • We conclude KFABP can functionally compensate for the absence of AFABP, resulting in no major alterations in adipocyte metabolism or fat accumulation in response to short-term feeding of high-fat diets that result in moderate hyperinsulinemia [2].
  • RESULTS: TNFalpha mRNA was increased in the retinas of experimental animals on P13 and P15, during the early stages of retinal neovascularization [3].
  • By screening a random cyclic peptide phage display library, we have identified a novel peptide, P15, that abrogated CK2 phosphorylation by blocking the substrate in vitro [4].
  • The recombinant ALBP was soluble in E. coli extracts and resistant to bacterial proteolysis [5].

High impact information on Fabp4


Biological context of Fabp4


Anatomical context of Fabp4


Associations of Fabp4 with chemical compounds

  • However, in the presence of 10 microm oleate, A-FABP and E-FABP each bound to HSL with high affinity (Kd of 0.5 and 3 nM, respectively) in a approximately 1:1 molar stoichiometry, whereas liver FABP and intestinal FABP did not exhibit any association [16].
  • The glycerol release from isproterenol-stimulated ALBP/aP2 null fat cells was similarly reduced by approximately 35% [11].
  • The significant decrease in both basal and isoproterenol-stimulated lipolysis in adipose tissue of ALBP/aP2 null mice supports the model whereby intracellular lipid-binding proteins function as lipid chaperones, facilitating the movement of fatty acids out of the fat cell [11].
  • ALBP/aP2 and KLBP exhibit similar binding affinities for most long-chain fatty acids; however, ALBP/aP2 exhibits a two to three-fold increased affinity for myristic, palmitic, oleic and linoleic acids, the predominant fatty acids of adipocytes [17].
  • As measured by guanidinium hydrochloride denaturation, the stability of ALBP/aP2 is nearly 3 kcal/mol greater than that of KLBP [17].

Physical interactions of Fabp4


Regulatory relationships of Fabp4

  • In 3T3-L1 preadipocytes, simultaneous administration of a PPARdelta-selective ligand and MIX significantly enhanced the early expression of PPARgamma and ALBP/aP2, but only modestly promoted terminal differentiation as determined by lipid accumulation [24].

Other interactions of Fabp4

  • The activation by A-FABP was dependent upon its fatty acid binding properties because a non-fatty acid binding mutant, R126Q, failed to activate HSL [16].
  • In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus [25].
  • Treating differentiating 3T3-L1 preadipocytes with t10c12 CLA and conjugated nonadecadienoic acid (CNA, a 19-carbon CLA cognate) resulted in decreased intracellular triglyceride accumulation and mRNA levels of the adipogenic gene fatty acid synthase and adipocyte lipid binding protein [26].
  • At the molecular level, activation of PPARdelta by fatty acids induced transcription of the genes encoding fatty acid transporter, adipocyte lipid-binding protein, and PPARgamma [27].
  • It was further found that AFABP, but not acetylated AFABP, prevented cytochrome c, a well characterized peripheral membrane protein, from binding to membranes [28].

Analytical, diagnostic and therapeutic context of Fabp4


  1. Lack of macrophage fatty-acid-binding protein aP2 protects mice deficient in apolipoprotein E against atherosclerosis. Makowski, L., Boord, J.B., Maeda, K., Babaev, V.R., Uysal, K.T., Morgan, M.A., Parker, R.A., Suttles, J., Fazio, S., Hotamisligil, G.S., Linton, M.F. Nat. Med. (2001) [Pubmed]
  2. Adipocyte metabolism in adipocyte fatty acid binding protein knockout mice (aP2-/-) after short-term high-fat feeding: functional compensation by the keratinocyte [correction of keritinocyte] fatty acid binding protein. Shaughnessy, S., Smith, E.R., Kodukula, S., Storch, J., Fried, S.K. Diabetes (2000) [Pubmed]
  3. Regulation of matrix metalloproteinase expression by tumor necrosis factor in a murine model of retinal neovascularization. Majka, S., McGuire, P.G., Das, A. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  4. Antitumor effect of a novel proapoptotic peptide that impairs the phosphorylation by the protein kinase 2 (casein kinase 2). Perea, S.E., Reyes, O., Puchades, Y., Mendoza, O., Vispo, N.S., Torrens, I., Santos, A., Silva, R., Acevedo, B., López, E., Falcón, V., Alonso, D.F. Cancer Res. (2004) [Pubmed]
  5. Cloning of murine adipocyte lipid binding protein in Escherichia coli. Its purification, ligand binding properties, and phosphorylation by the adipocyte insulin receptor. Chinander, L.L., Bernlohr, D.A. J. Biol. Chem. (1989) [Pubmed]
  6. Transcriptional regulation of gene expression during adipocyte differentiation. MacDougald, O.A., Lane, M.D. Annu. Rev. Biochem. (1995) [Pubmed]
  7. A eukaryotic transcriptional repressor with carboxypeptidase activity. He, G.P., Muise, A., Li, A.W., Ro, H.S. Nature (1995) [Pubmed]
  8. CCAAT/enhancer binding protein alpha is sufficient to initiate the 3T3-L1 adipocyte differentiation program. Lin, F.T., Lane, M.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  9. Cell-free transcription directed by the 422 adipose P2 gene promoter: activation by the CCAAT/enhancer binding protein. Cheneval, D., Christy, R.J., Geiman, D., Cornelius, P., Lane, M.D. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  10. Expression of the differentiation-induced gene for fatty acid-binding protein is activated by glucocorticoid and cAMP. Cook, J.S., Lucas, J.J., Sibley, E., Bolanowski, M.A., Christy, R.J., Kelly, T.J., Lane, M.D. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  11. Targeted disruption of the adipocyte lipid-binding protein (aP2 protein) gene impairs fat cell lipolysis and increases cellular fatty acid levels. Coe, N.R., Simpson, M.A., Bernlohr, D.A. J. Lipid Res. (1999) [Pubmed]
  12. Expression of specific mRNAs during adipose differentiation: identification of an mRNA encoding a homologue of myelin P2 protein. Bernlohr, D.A., Angus, C.W., Lane, M.D., Bolanowski, M.A., Kelly, T.J. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  13. Mammary derived growth inhibitor is not a distinct protein but a mix of heart-type and adipocyte-type fatty acid-binding protein. Specht, B., Bartetzko, N., Hohoff, C., Kuhl, H., Franke, R., Börchers, T., Spener, F. J. Biol. Chem. (1996) [Pubmed]
  14. Peroxisome proliferator-activated receptor gamma-mediated differentiation: a mutation in colon cancer cells reveals divergent and cell type-specific mechanisms. Gupta, R.A., Sarraf, P., Mueller, E., Brockman, J.A., Prusakiewicz, J.J., Eng, C., Willson, T.M., DuBois, R.N. J. Biol. Chem. (2003) [Pubmed]
  15. Regulation of gene expression in adipose cells by polyunsaturated fatty acids. Bernlohr, D.A., Coe, N.R., Simpson, M.A., Hertzel, A.V. Adv. Exp. Med. Biol. (1997) [Pubmed]
  16. Fatty acid-binding protein-hormone-sensitive lipase interaction. Fatty acid dependence on binding. Jenkins-Kruchten, A.E., Bennaars-Eiden, A., Ross, J.R., Shen, W.J., Kraemer, F.B., Bernlohr, D.A. J. Biol. Chem. (2003) [Pubmed]
  17. Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes. Simpson, M.A., LiCata, V.J., Ribarik Coe, N., Bernlohr, D.A. Mol. Cell. Biochem. (1999) [Pubmed]
  18. Characterization of the mouse carbonic anhydrase II gene promoter. Marino, L.R. J. Biol. Chem. (1993) [Pubmed]
  19. Dietary trans-10,cis-12 conjugated linoleic acid induces hyperinsulinemia and fatty liver in the mouse. Clément, L., Poirier, H., Niot, I., Bocher, V., Guerre-Millo, M., Krief, S., Staels, B., Besnard, P. J. Lipid Res. (2002) [Pubmed]
  20. Essential role of citrate export from mitochondria at early differentiation stage of 3T3-L1 cells for their effective differentiation into fat cells, as revealed by studies using specific inhibitors of mitochondrial di- and tricarboxylate carriers. Kajimoto, K., Terada, H., Baba, Y., Shinohara, Y. Mol. Genet. Metab. (2005) [Pubmed]
  21. Adipose tissue lipolysis as a metabolic pathway to define pharmacological strategies against obesity and the metabolic syndrome. Langin, D. Pharmacol. Res. (2006) [Pubmed]
  22. Crystal structure of recombinant murine adipocyte lipid-binding protein. Xu, Z., Bernlohr, D.A., Banaszak, L.J. Biochemistry (1992) [Pubmed]
  23. Interaction of adipocyte fatty acid-binding protein (AFABP) and JAK2: AFABP/aP2 as a regulator of JAK2 signaling. Thompson, B.R., Mazurkiewicz-Muñoz, A.M., Suttles, J., Carter-Su, C., Bernlohr, D.A. J. Biol. Chem. (2009) [Pubmed]
  24. Peroxisome proliferator-activated receptor delta (PPARdelta )-mediated regulation of preadipocyte proliferation and gene expression is dependent on cAMP signaling. Hansen, J.B., Zhang, H., Rasmussen, T.H., Petersen, R.K., Flindt, E.N., Kristiansen, K. J. Biol. Chem. (2001) [Pubmed]
  25. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. Helledie, T., Antonius, M., Sorensen, R.V., Hertzel, A.V., Bernlohr, D.A., Kølvraa, S., Kristiansen, K., Mandrup, S. J. Lipid Res. (2000) [Pubmed]
  26. trans-10,cis-12 CLA inhibits differentiation of 3T3-L1 adipocytes and decreases PPAR gamma expression. Kang, K., Liu, W., Albright, K.J., Park, Y., Pariza, M.W. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  27. Expression of peroxisome proliferator-activated receptor PPARdelta promotes induction of PPARgamma and adipocyte differentiation in 3T3C2 fibroblasts. Bastie, C., Holst, D., Gaillard, D., Jehl-Pietri, C., Grimaldi, P.A. J. Biol. Chem. (1999) [Pubmed]
  28. The adipocyte fatty acid-binding protein binds to membranes by electrostatic interactions. Smith, E.R., Storch, J. J. Biol. Chem. (1999) [Pubmed]
  29. Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein. Ory, J., Kane, C.D., Simpson, M.A., Banaszak, L.J., Bernlohr, D.A. J. Biol. Chem. (1997) [Pubmed]
  30. Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies. LaLonde, J.M., Levenson, M.A., Roe, J.J., Bernlohr, D.A., Banaszak, L.J. J. Biol. Chem. (1994) [Pubmed]
  31. Expression, purification, and crystallization of the adipocyte lipid binding protein. Xu, Z.H., Buelt, M.K., Banaszak, L.J., Bernlohr, D.A. J. Biol. Chem. (1991) [Pubmed]
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