References: Lecithin
J Biol Chem. 1996 Feb 9;271(6):3039-45.
Structural studies of a peptide activator of human lecithin-cholesterol acyltransferase.
Buchko GW, Treleaven WD, Dunne SJ, Tracey AS, Cushley RJ.
Department of Chemistry and Institute of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6.
The synthetic lipid-associating peptide, LAP-20 (VSSLLSSLKEYWSSLKESFS), activates lecithin-cholesterol acyltransferase (LCAT) despite its lack of sequence homology to apolipoprotein A-I, the primary in vivo activator of LCAT. Using SDS and dodecylphosphocholine (DPC) to model the lipoprotein environment, the structural features responsible for LAP-20's ability to activate LCAT were studied by optical and two-dimensional 1H NMR spectroscopy. A large blue shift in the intrinsic fluorescence of LAP-20 with the addition of detergent suggested that the peptide formed a complex with the micelles. Analysis of the CD data shows that LAP-20 lacks well defined structure in aqueous solution but adopts helical, ordered conformations upon the addition of SDS or DPC. The helical nature of the peptides in the presence of both lipids was confirmed by upfield H alpha NMR secondary shifts relative to random coil values. Average structures for both peptides in aqueous solutions containing SDS and DPC were generated using distance geometry methods from 329 (SDS) and 309 (DPC) nuclear Overhauser effect-based distance restraints. The backbone (N, Calpha, C=O) RMSD from the average structure of an ensemble of 17 out of 20 calculated structures was 0.41 +/- 0.15 Angstrom for LAP-20 in SDS and 0.41 +/- 0.12 A for an ensemble of 20 out of 20 calculated structures for LAP-20 in DPC. In the presence of SDS, the distance geometry and simulated annealing calculations show that LAP-20 adopts a well defined class A amphipathic helix with distinct hydrophobic and hydrophilic faces. A similar structure was obtained for LAP-20 in the presence of DPC, suggesting that both detergents may be used inter
Zentralbl Bakteriol Mikrobiol Hyg [A]. 1988 Nov;269(3):377-86.
Synergism of Candida albicans and delta toxin producing Staphylococcus aureus on mouse mortality and morbidity: protection by indomethacin.
Carlson EC.
Michigan Technological University, Houghton 49931.
Twelve Staphylococcus aureus strains, six positive and six negative for delta-toxin production, were studied for synergistic effects on mouse mortality and morbidity when combined with Candida albicans and inoculated intraperitoneally (i.p.). S. aureus strains producing delta-toxin were found to exhibit a relatively great synergistic decrease (between near 10(3)-10(5)-fold) in LD50 (dose necessary to kill 50% of exposed animals in five days) when combined with a nonlethal dose of C. albicans and injected i.p. S. aureus strains which did not produce delta showed less of a synergistic effect with C. albicans (10-10(2)-fold drop in LD50). A synergistic effect on mortality could also be produced when animals were dually injected with C. albicans and sterile growth filtrates from the delta-toxin producing strains or the purified delta-toxin. The lethal agent in the culture filtrate was, like delta-toxin, sensitive to lecithin and insensitive to heat. Indomethacin protected animals from the C. albicans-filtrate induced death. Blood measurements made following i.p. injection of delta-toxin and C. albicans revealed chemistry changes indicative of shock, kidney and liver damage; delta-toxin alone caused no significant chemistry changes whereas C. albicans alone caused some blood chemistry changes but liver and kidney damage was not indicated. No synergism on mortality was found between C. albicans and purified alpha-toxin or toxic shock syndrome toxin-1.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3064497&dopt=Abstract lecithin
J Clin Invest. 1996 Apr 15;97(8):1844-51.
Hyperalphalipoproteinemia in human lecithin cholesterol acyltransferase transgenic rabbits. In vivo apolipoprotein A-I catabolism is delayed in a gene dose-dependent manner.
Brousseau ME, Santamarina-Fojo S, Zech LA, Berard AM, Vaisman BL, Meyn SM, Powell D, Brewer HB Jr, Hoeg JM.
Molecular Disease Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Lecithin cholesterol acyltransferase (LCAT) is an enzyme involved in the intravascular metabolism of high density lipoproteins (HDLs). Overexpression of human LCAT (hLCAT) in transgenic rabbits leads to gene dose-dependent increases of total and HDL cholesterol concentrations. To elucidate the mechanisms responsible for this effect, 131I-HDL apoA-I kinetics were assessed in age- and sex-matched groups of rabbits (n=3 each) with high, low, or no hLCAT expression. Mean total and HDL cholesterol concentrations (mg/dl), respectively, were 162+/-18 and 121+/-12 for high expressors (HE), 55+/-6 and 55+/-10 for low expressors (LE), and 29+/-2 and 28+/-4 for controls. Fast protein liquid chromatography analysis of plasma revealed that the HDL of both HE and LE were cholesteryl ester and phospholipid enriched, as compared with controls, with the greatest differences noted between HE and controls. These compositional changes resulted in an incremental shift in apparent HDL particle size which correlated directly with the level of hLCAT expression, such that HE had the largest HDL particles and controls the smallest. In vivo kinetic experiments demonstrated that the fractional catabolic rate(FCR, d(-1)) of apoA-I was slowest in HE (0.328+/-0.03) followed by LE (0.408+/-0.01) and, lastly, by controls (0.528+/-0.04). ApoA-I FCR was inversely associated with HDL cholesterol level (r=-0.851,P<0.01) and hLCAT activity (r=-0.816, P<0.01). These data indicate that fractional catabolic rate is the predominant mechanism by which hLCAT overexpression differenti
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