References: Lecithin
Biochim Biophys Acta. 1994 Dec 8;1215(3):307-13.
Interaction between apo A-I-containing lipoproteins and lecithin:cholesterol acyltransferase.
Ikeda Y, Ohta T, Matsuda I.
Department of Pediatrics, Kumamoto University School of Medicine, Kumamoto, Japan.
HDL2 and HDL3 subfractions of two species of apo A-I-containing lipoprotein, one containing only apo A-I (LpA-I) and the other containing both apo A-I and apo A-II (LpA-I/A-II), were tested for reactivity to lecithin:cholesterol acyltransferase (LCAT). These subfractions and their mixtures were incubated with lipoprotein-deficient plasma (LCAT source), and the rate of cholesterol esterification and kinetic parameters were determined. Apparent Vmax (appVmax) and apparent Km (appKm) for HDL2 subfractions of LpA-I and LpA-I/A-II were significantly lower than those of their HDL3 counterparts. Differences between subfractions were much more prominent in LpA-I than in LpA-I/A-II. appVmax of the HDL2 subfraction of LpA-I (LpA-IHDL2) was one-fifth, and appKm was one-third of those for the HDL3 subfraction (LpA-IHDL3). appVmax and appKm of LpA-IHDL2 were both lowest among the apo A-I-containing lipoprotein subfractions. When LpA-IHDL2 was added to other subfractions, the molar rate of cholesterol esterification was suppressed. Since LpA-IHDL2 consists of a particle 11.1 nm in diameter, our observations suggest that LpA-IHDL2 suppresses cholesterol esterification in apo A-I-containing lipoprotein, possibly by displacing LCAT from other subfractions with higher appKm and higher appVmax to 11.1 nm LpA-I particles with lower appKm and lower appVmax. All of these data suggest that the relative amount of 11.1 nm LpA-I particles in plasma regulates the reactivity of apo A-I-containing lipoprotein to LCAT and may play a key role on the production of cholesteryl esters in plasma.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7811716&dopt=Abstract lecithin
J Bioenerg Biomembr. 1992 Dec;24(6):625-34.
Differential scanning calorimetry study of glycogen phosphorylase b-detergent interactions.
Centeno F, Fernandez-Salguero P, Laynez JL, Gutierrez-Merino C.
Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
The overall thermal denaturation of glycogen phosphorylase b is irreversible and our results conform to the theoretical prediction of a reversible process followed by a slower irreversible process. The basic thermodynamic parameters of glycogen phosphorylase b denaturation have been worked out and found to be: critical temperature 57.0 +/- 0.5 degrees C, transition half-width 8 +/- 1 degrees C, and calorimetric enthalpy change and Van't Hoff enthalpy change of the denaturation process 450 +/- 50 and 105 +/- 15 kcal/mol of enzyme monomer, respectively, at pH 7.4. These parameters have been found to be largely altered by the detergents octylglucoside, cholate, and deoxycholate at or below their critical micelle concentration, but not by Triton X-100 nor by lecithin liposomes. Organic solvents, such as dimethyl sulfoxide and methanol, and the presence of sarcoplasmic reticulum membranes produces an alteration of the denaturation thermogram of glycogen phosphorylase b similar to that produced by the above-mentioned detergents. These results allow us to hypothesize that hydrophobic domains of glycogen phosphorylase b are involved in its association to sarcoplasmic reticulum membranes in the sarcoplasmic reticulum/glycogenolytic complex of mammalian skeletal muscle.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1459992&dopt=Abstract lecithin
Mutat Res. 1992 May 1;279(1):55-60.
Micronucleus induction and phagocytosis in mammalian cells treated with diesel emission particles.
Gu ZW, Zhong BZ, Nath B, Whong WZ, Wallace WE, Ong TM.
Division of Respiratory Disease Studies, National Institute for Occupational Safety and Health, Morgantown, WV 26505-2888.
Micronucleus induction and phagocytosis in V79 and CHO cells treated with diesel emission particles (DEP) were studied. After separation of the sample into supernatant and sediment fractions, the genotoxic activity of DEP was shown to reside in the supernatant fraction for the DMSO-extracted sample, and in the sedimented fraction for the dipalmitoyl lecithin (DPL), a primary component of pulmonary surfactant, dispersed sample. More particles from DMSO sediment samples were phagocytized than DPL sediment by both types of cells. This had no effect, however, on micronucleus induction. CHO cells phagocytized fewer particles, but gave a higher number of micronuclei than V79 cells. CHO cells seem to be more sensitive to DEP. Evidently, micronucleus induction is not the result of phagocytosis per se, but is due to the different response of the indicator cells to the DEP sample tested. These results further indicate that most, if not all, genotoxic compounds associated with DEP can be extracted by DMSO and that genotoxic activity associated with DEP inhaled into the lung may also be expressed by dispersion of particles in pulmonary surfactant.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1374533&dopt=Abstract lecithin
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