Fatty acid-binding proteins difference

Hsu, K.-T. and Storch, J. (1996) Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. Journal of Biological Chemistry 271,13317—13323. 

P2 protein. PNS myelin contains a positively charged protein different from MBP that is referred to as P2 (Mr — 15,000). It is unrelated in sequence to MBP and is a member of a family of cytoplasmic fatty acid binding proteins (FABP) that are present in a variety of cell types [25]. The amount of P2 protein is variable among species, accounting for about 15% of total protein in bovine PNS myelin, 5% in humans and less than 1% in rodents. P2 protein is generally considered a PNS myelin protein but it is expressed in small amounts in CNS myelin sheaths of some species. P2 is an antigen for experimental allergic neuritis, the PNS counterpart of EAE (see Chs 36 and 38). P2 appears to be present in the major dense line of myelin sheaths, where it may play a structural role similar to MBP... 

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. 

Katongole, J.B.D. and March, B.E. (1980) Fat utilization in relation to intestinal fatty acid binding protein and bile salts in chicks of different ages and different genetic sources. Poultry Science 59,819-827. 

Hohmann AG, Suplita RL, Bolton NM, Neely MH, Fegley D, Mangieri R, Krey JF, Walker JM, Holmes PV, Crystal JD, Duranti A, Tontini A, Mor M, Tarzia G, Piomelli D (2005) An endocannabinoid mechanism for stress-induced analgesia. Nature 435(7045) 1108-12 Howlett AC, Qualy JM, Khachatrian LL (1986) Involvement of Gi in the inhibition of adenylate cyclase by cannabimimetic drugs. Mol Pharmacol 29(3) 307-13 Hsu K-T, Storch J (1996) Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J Biol Chem 271(23) 13317—23... 

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... 

The impact of different pharmacological compounds has been evaluated on hESC- or iPS-derived cardiomyocytes using Image Xpress Micro and FLIPR Tetra systems [111], impedance-based xCELLigence real-time cell analyzer Cardio system [112, 113], MEA [54, 114], and perforated patch clamp [38], The impact of cardiotoxic drugs on the release of biomarkers, such as troponin T and fatty acid-binding protein 3 from cardiomyocytes, has also been investigated to predict the cardiotoxicity [115]. 

Transport of fatty acids inside the parenchymal cells, that is, from the plas-malentma to the intracellular site of conversion, is most likely mediated by fatty acid-binding proteins (FABPs). At least seven different isoforms of this low molecular weight protein (15 kDa) have been described, among which there is the liver-type and muscle-type FABP (Glatz and Van der Vusse, 1990). FABPs facilitate intracellular transport of fatty acids by increasing their solubility in the aqueous environment. 

Thompson, J., A. Reese-Wagoner, and L. Banaszak. 1999. Liver fatty acid binding protein species variation and the accommodation of different ligands. Biochim. Biophys. Acta 1441(2-3) 117-130. 

Fatty-acid binding proteins (FABP) are involved in fatty acid metabolism and cellular lipid transport. Adipocyte FABP (aP2) is also expressed in macrophages bone marrow transplantation from Apo E -/-, aP2 -/-mice to Apo E-/- mice led to the development of smaller atherosclerotic lesions in recipient mice without differences in cholesterol, glucose, or insulin in plasma (514). 

Rickers et al, 1985). These experiments introduced a novel property of lipid transfer proteins from plants. It is of interest to note that, in animal cells, the properties of transferring and binding lipids are associated to two different types of proteins, the lipid transfer proteins and the fatty acid binding proteins (see Kader, 1985 Rickers et al. 1984). 

A number of studies over the past 10 years have described the kinetic properties and protease sensitivities of cellular fatty acid transfer systems. A general conclusion of these studies is that fatty acid transfer cannot be accounted for simply by a process of passive diffusion. " Moreover, at least three structurally different plasma membrane proteins that may mediate fatty acid transport have been identified by molecular cloning and expression in heterologous systems. These are the fatty acid transporter (FAT)," the fatty acid transport protein (FATP) and the plasma membrane fatty acid-binding protein (FABPp ,). ... 

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