Lipid carrier

The phospholipids thus obtained are transported by lipid-carrier cytoplasmic proteins to the membranes (cellular or intracellular) to replace the used or impaired phospholipid molecules. 

Tablets fast dissolving, lipid-carrier based, slow releasing, disintegrate without water, float in the stomach (gastric retentive), buccal... 

Larabi M, et al. Reduction of NO synthase expression and TNF alpha production of macrophages by amphotericin B lipid carriers. Antimicrob Agents Chemother 2001 45 553. 

Spagnou S, Miller AD, Keller M. Lipidic carriers of siRNA differences in the formulation, cellular uptake, and delivery with plasmid DNA. Biochemistry 2004 43(42) 13348-13356. 

Nomura T, et al. Effect of particle size and charge on the disposition of lipid carriers after intratumoral injection into tissue-isolated tumors. Pharm Res 1998 15 128. 

NADH is oxidized by NADH dehydrogenase (complex I), delivering its electrons into the chain and returning as NAD to enzymes that require it. The electrons are passed along a series of protein and lipid carriers that serve as the wire. These include, in order ... 

Muller, R. H., Radtke, M. and Wissing, S. A., Solid lipid nanoparticles (SLN) and nanostructured lipid carriers (NLC) in cosmetic and dermatological preparations. Adv. Drug Deliv. Rev., 54 (Snppl. 1), S131-55, 2002. 

Both the heat-stable SCP protein of Ritter and Dempsey (R2) and the heat-labile SCP protein of Scallen et al. (S2) bind other lipids (e.g., phospholipids and fatty acids) in addition to water-insoluble cholesterol and its precursors (R2, R3, R5, S2). In view of this apparent lack of specificity, Ritter and Dempsey (R5) have suggested that the carrier protein may be more generally called lipid carrier protein (LCP), although its binding to squalene and sterol carrier protein may more directly refiect its functional role in cholesterol biosynthesis. Obviously, more work is needed to clearly define both structural role and functional properties of this protein or proteins. 

M2. Mc nathy, W. J., Magnani, H. N., Alaupovic, P., Torsvik, H., and Berg, K., Identification of plasma lipid carriers in familial lecithin cholesterol acyltrans-ferase deficiency. CiraikUion 46, Suppl. II, 247 (1972). 

Bacitracin inhibits the dephosphorylation of this lipid carrier, a step essential to the carrier molecule s ability to accept cell wall constituents for transport. 

Human-leukemic antigen (HLA-DR) has been found in remarkably low proportions on the plasma membrane of human, lymphoblastoid cells. In the presence of tunicamycin, both subunits of this cell-surface antigen showed lower apparent molecular weights. One of them completely lost its [3H]-labelled 2-acetamido-2-deoxy-D-glucose portion, implying that HLA-DR antigens possess oligosaccharides whose synthesis is lipid carrier-dependent.555... 

Assembly of this repeating unit begins with the transfer of a phosphogaladosyl unit from UDP-Gal to the phospho group of the lipid carrier undecaprenol phosphate. 

Figure 21-1 Movement of triacylglycerols from liver and intestine to body cells and lipid carriers of blood. VLDL very low density lipoprotein which contains triacylglycerols, phospholipids, cholesterol, and apolipoproteins B, and C. IDL intermediate density lipoproteins found in human plasma. LDL low density lipoproteins which have lost most of their triacylglycerols. ApoB-100, etc., are apolipoproteins listed in Table 21-2. LCAT, lecithin cholesterol acyltransferase CETP, cholesteryl ester transfer protein (see Chapter 22).

A third group of lipid-binding proteins have a four-helix bundle structure. They include the insect lipophorins, which transport diacylglycerols in the hemolymph (see main text), and nonspecific lipid carriers of green plants.q An 87-residue four-helix protein with a more open structure binds acyl-coenzyme A molecules in liver.r... 

Many larger lipid carrier proteins are known. The 476-residue plasma cholesteryl ester transfer protein is discussed briefly in Chapter 22. Plasma phospholipid transfer proteins are of similar size.t/U A 456-residue human phospholipid-binding protein interacts with the lipopolysaccharide of the surfaces of gram-negative bacteria (Fig. 8-30) and participates in the immune response to the bacteria. It has an elongated boomerang shape with two cavities, both of which bind a molecule of phosphatidylcholine. Other plasma lipid transfer proteins may have similar structures/... 

Another possible regulatory mechanism has been pointed out by Elbein for plant systems. His results implied either that the carrier lipid for different sugars are different polyprenyl phosphates, or that the glycosyltransferases have their own pools of lipid carriers, which do not mix.16 The results, compared to those for other plant and animal systems, suggested that the polyprenyl phosphates are the same for different sugars in each system, thus ruling out the first hypothesis, and reinforcing the concept of different pools.30... 

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