Lipid transfer

HMG-CoA-Reductase-Inhibitors Lipoprotein Metabolism Lipid Transfer Proteins... 

Plasma lipid transfer proteins, which include the cholesteryl-ester-transfer-protein (CETP previously known as lipid transfer protein I, LTP-I) and the phospholipid-transfer-protein (PLTP previously known as lipid transfer protein II, LTP-II) mediate the transfer of lipids (cholesteryl esters, triglycerides and phospholipids) between lipoproteins present in human plasma. These proteins significantly affect plasma lipoprotein concentration and composition. 

In humans, CETP and PLTP are directly involved in the transfer of lipids between different lipoprotein classes. Through their action, these lipid transfer proteins have major effects on the concentration and composition of HDL. This section further describes the physiological function of CETP and PLTP in humans. 

Tall A (1995) Plasma lipid transfer proteins. Annu Rev Biochem 64 235-257... 

Jiang XC, Zhou HW (2006) Plasma lipid transfer proteins. Curr Opin Lipidol 17 302—308... 

Lipid Transfer Proteins Lipidation Lipopolysaccharide Lipoprotein Lipase... 

Biodegradable films made from edible biopolymers from renewable sources could become an important factor in reducing the environmental impact of plastic waste. Proteins, lipids, and polysaccharides are the main biopolymers employed to make edible films and coatings. Which of these components are present in different proportions and determine the properties of the material, as a barrier to water vapor, oxygen, carbon dioxide, and lipid transfer in food systems (Gomez-Guillen et al. 2002 and 2009). 

Schad SG. Trcka J, Vieth S. Scheurer S. Conti A. Brbcker EB. Trautmann A Wine anaphylaxis in a German patient IgE-mediated allergy against a lipid transfer protein of grapes. Int Arch Allergy Immunol 2005 136 159-164. 

Webb, NR, Connell, PM, Graf, GA, Smart, EJ, de Villiers, WJ, de Beer, FC, and van der Westhuyzen, DR, 1998. SR-BII, an isoform of the scavenger receptor BI containing an alternate cytoplasmic tail, mediates lipid transfer between high density lipoprotein and cells. J Biol Chem 273, 15241-15248. 

CBP is predicted by PSORT analysis to be a cytoplasmic protein (Horton et al. 2007) and to contain a steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain of 200 amino acids at its C-terminus (Figure 24.2a). 

Lipophorin acts as a reusable shuttle between the membrane-bound lipophorin receptors in tissues (Tsuchida and Wells 1990, Gopalapillai et al. 2006) and is not generally endocytosed in the cells (Law and Wells 1989, Arrese et al. 2001, Canavoso et al. 2001). Thus, the intracellular CBP alone seems not to be able to pick up carotenoid from the lipophorin that resides outside of the cell. Cell surface components are thought to be necessary to allow intracellular delivery of carotenoids (Figure 24.6, magnification) (Arrese et al. 2001). The lipid transfer particle (LTP) (Blacklock and Ryan 1994, Tsuchida et al. 1997) on the outer surface of membranes and unknown membrane-spanning factors that specifically transfer carotenoids might be candidates. 

Alpy, F. and Tomasetto, C. 2005. Give lipids a START The StAR-related lipid transfer (START) domain in mammals. J. Cell Sci., 118(Pt 13) 2791-2801. 

Romanowski, M. J., Soccio, R. E., Breslow, J. L., and Burley, S. K. 2002. Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Proc. Natl. Acad. Sci. U.S.A., 99(10) 6949-6954. 

Soccio, R. E. and Breslow, J. L. 2003. StAR-related lipid transfer (START) proteins Mediators of intracellular lipid metabolism. J. Biol. Chem., 278(25) 22183-22186. 

Tsuchida, K., Soulages, J. L., Moribayashi, A., Suzuki, K., Maekawa, H., and Wells, M. A. 1997. Purification and properties of a lipid transfer particle from Bombyx mori Comparison to the lipid transfer particle from Manduca sexta. Biochim. Biophys. Acta, 1337(l) 57-65. 

Tsuchida, K., Arai, M., Tanaka, Y. et al. 1998. Lipid transfer particle catalyzes transfer of carotenoids between lipophorins of Bombyx mori. Insect Biochem. Mol. Biol., 28(12) 927-934. 

Lerche, M.H. and Poulsen, F.M. (1998) Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins. Protein Science 7, 2490-2498. 

MTP is responsible for the transfer of TGs and cholesteryl esters from the endoplasmic reticulum (ER) to lipoprotein particles (VLDL in hepatocytes in the liver and chylomicrons in endocytes in the intestine) for secretion [52]. It is a heterodimer consisting of a unique large subunit essential for lipid transfer encoded by the mttp gene and a smaller subunit, the ubiquitous ER enzyme protein disulfide isomerase [53]. 

In this case, a loss of FRET is observed when the transferable lipid moves to an acceptor membrane. The most common FRET pair used for these studies is the NBD/rhodamine pair [160, 161], Some other FRET pairs have been used for the study of membrane sideness conservation [162] and intermembrane lipid transfer [163], Distinguishably, a study of membrane activation by molecular selective recognition was performed using FRET [97],... 

Nichols, J. W. and Pagano, R. E. (1983). Resonance energy-transfer assay of protein-mediated lipid transfer between vesicles. J. Biol. Chem. 258, 5368-5371. 

Nielsen KK, Nielsen JE, Madrid S, Mikkelsen JD. New antifungal proteins from sugar beet Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. Plant Mol Biol 1996 31 539-552. 

Lipid transfer peptides and proteins occur in eukaryotic and prokaryotic cells. In vitro they possess the ability to transfer phospholipids between lipid membranes. Plant lipid transfer peptides are unspecific in their substrate selectivity. They bind phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, and glycolipids. Some of these peptides have shown antifungal activity in vitro The sequences of lipid transfer proteins and peptides contain 91-95 amino acids, are basic, and have eight cysteine residues forming four disulfide bonds. They do not contain tryptophan residues. About 40% of the sequence adopts a helical structure with helices linked via disulfide bonds. The tertiary structure comprises four a-helices. The three-dimensional structure of a lipid transfer peptide from H. vulgare in complex with palmitate has been solved by NMR. In this structure the fatty acid is caged in a hydrophobic cavity formed by the helices. 

Pastorello, E.A., et al. (2000). The maize major allergen, which is responsible food-induced allergic reactions, is a lipid transfer protein, J. Allergy Clin. Immunol., 106, 4, 744-751. 

Pastorello, E.A., et al. (2001). Lipid transfer proteins and 2S albumins as allergens. 

LIPID PHASE TRANSITION KINETICS LIPID PHASE TRANSITION KINETICS LIPID TRACER KINETICS Lipid transfer across membrane bilayers, PHOSPHOLIPID FLIP-FLOP Lipoamide,... 

For quantification of phospholipids identify the spots with iodine vapor or Soln. D. Mark the spots with a pencil, and cut the spots as well as a part of the plate with the same size but free of lipids. Transfer the material into a test tube and determine the amount of phosphate as described in Protocol 1.3.3. 

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