Fatty acid-binding proteins function

Kaikans RM, Bass NM, Ockner RK Functions of fatty acid binding proteins. Experientia 1990 46 617. 

Coe, N.R. and Bernlohr, D.A. (1998) Physiological properties and functions of intracellular fatty acid-binding proteins. Biochimica et Biophysica Acta 1391, 287-306. 

Kennedy, M.W., Scott, J.C., Lo, S.J., Beauchamp, J. and McManus, D.P. (2000) The Sj-FABPc fatty acid binding protein of the human blood fluke Schistosoma japonicum structural and functional characterisation and unusual solvent exposure of a portal-proximal tryptophan. BiochemicalJournal 349, 377-384. 

Becker, M.M., Kalinna, B.H., Waine, G.J. and McManus, D.P. (1994) Gene cloning, overproduction and purification of a functionally active cytoplasmic fatty acid-binding protein (Sj-FABPc) from the human blood fluke Schistosoma japonicum. Gene 148, 321-325. 

Zimmerman, A. W. and Veerkamp, J. H., New insights into the structure and function of fatty acid-binding proteins. Cell Mol Life Sci, 2002, 59, 1096-1116. 

Veerkamp, I. H., et al., Structural and functional features of different types of cytoplasmic fatty acid-binding proteins. Biochim Biophys Acta, 1991,1081, 1-24. 

The ability of NOE matching to identify the correct pose from a collection of decoy poses was demonstrated on three test cases involving lead-like compounds bound to small proteins. One of these test cases involves muscle fatty acid-binding protein (mFABP) and the other two involve the leukocyte function-associated antigen 11-domain (LFA-1). As these results have been presented in detail elsewhere,1151 here we only summarize the results obtained when the BMRB average chemical shifts (diamagnetic protein statistics) were used for chemical shift predictions. The compounds used for these test cases are shown in Scheme 5.1 (compound 3 contains a proprietary core, which is represented by an ellipse). 

Bass NM (1988) The cellular fatty acid binding proteins aspects of structure, regulation, and function. Int Rev Cytol 111 143-84... 

The EFA metabolism is presented in several extensive reviews.9 16 17 Much of the information concerning EFA physiology and biochemistry has been derived from work in hepatocytes and may be of limited relevance to epidermis since a major role of the liver is to convert dietary lipids into energy stores. Meanwhile, keratinocytes are involved in the fatty acid metabolism required both for normal cellular processes and the specialized role in the permeability barrier. Unlike the liver, the epidermis does not possess the capacity to desaturate at the A5 or A6 position, and therefore the skin relies on a supply of AA, LA, and ALA from the bloodstream. There is evidence for a distinct fatty acid binding protein in keratinocyte plasma membranes that is involved in EFA uptake into the skin and also recycling of free fatty acids from the stratum corneum.18 The transport mechanism in epidermis differs from that in hepatocytes since there is preferential uptake of LA over OA, which may function to ensure adequate capture of LA for barrier lipid synthesis.18... 

Storch, J., Thumser, A.E.A. 2000. The fatty acid transport function of fatty acid-binding proteins. Biochim. Biophys. Acta 1486, 28-44. 

Long-chain fatty acids were previously believed to enter cells by diffusion, but evidence now implicates a family of protein-mediated transporters, the fatty acid transport protein (FATP) family. Internally, fatty acid-binding proteins (FABPs) constimte a family of low-molecular-weight proteins that function as intracellular transporters of fatty acids. 

Fatty acids C10 0 and longer have considerable detergent properties and are not found free within cells. Most cells contain small intracellular fatty acid-binding proteins (FABPs), which are thought to function in part to buffer the detergent effects of free fatty acids. In the commercial sense, soaps are the water-soluble sodium or potassium salts of fatty acids, which are made from fats and oils by treating them chemically with a strong base such as NaOH or KOH. 

S. Shaughnessy, E.R. Smith, S. Kodu-KULA, J. Storch, and S.K. Fried, Adipocyte metabolism in adipocyte fatty acid binding protein knockout (aP2—/—) mice after short-term high-fat feeding functional compensation by keratinocyte fatty acid binding protein. Diabetes, 2000, 49, 904-911. 

Simon, T. C., Cho, A., Tso, P., and Gordon, J. I. (1997) Suppressor and activator functions mediated by a repeated heptad sequence in the liver fatty acid-binding protein gene (Fabpl). Effects on renal, small intestinal, and colonic epithelial cell gene expression in transgenic mice. J. Biol. Chem. 272, 10652-10663. 

Hertzel, A.V., Bemlohr, D.A. 2000. The mammalian fatty acid-binding protein multigene family molecular and genetic insights into function. Trends Endocrinol. Metab. 11 175-180. 

Glatz, J. E, and van der Vusse, G. J. 1996. Cellular fatty acid binding proteins Their function and physiological significance. Progress in Lipid Research 3 243-282. 

---