References: Lecithin
Free Radic Biol Med. 1989;7(3):237-42.
Selective sensitization of chemiluminescence resulted from lipid and oxygen radical reactions.
Sharov VS, Kazamanov VA, Vladimirov YA.
Institute of Radioengineering and Electronics, Academy of Sciences, Moscow, U.S.S.R.
Eu3+-tetracycline complex (EuT) increased the chemiluminescence (CL) intensity of linolenic acid micells (UFA-somes) oxidized with lipoxygenase and CL of the lecithin liposomes peroxidized with Fe2+ ions by 3 orders of magnitude. In the systems producing oxygen radicals (xanthine + xanthine oxidase and Fenton's reagent) EuT was ineffective. Luminol increased CL intensity up to 4 orders of magnitude in Fenton's reagent and by 2 orders of magnitude in xanthine oxidase reaction. The sensitization of CL in Fe2+-induced lipid peroxidation (LPO) of liposomes was by a factor 40, while in lipoxygenase reaction very low sensitization was observed. By means of cut-off light filter OS-12 (Soviet) having short wave-length transmittance limit at 560 nm it was possible to measure separately in the same sample the luminol-sensitized CL (maximal emission near 480 nm) and EuT-sensitized CL (maximum at 620 nm); these two CL components reflect, correspondingly, the production rate of oxygen- and lipid-free radicals. Mannitol, the OH radical scavenger, inhibited luminol-dependent component of CL in peroxidized liposomes and did not inhibited EuT sensitized CL in the same system. Apparently, hydroxyl radicals are produced in LPO reactions and responsible for the effect of CL sensitization by luminol, but are not involved in the chain LPO process.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2570736&dopt=Abstract lecithin
Braz J Med Biol Res. 2003 Dec;36(12):1613-20. Epub 2003 Nov 17.
Neuroprotection by flavonoids.
Dajas F, Rivera-Megret F, Blasina F, Arredondo F, Abin-Carriquiry JA, Costa G, Echeverry C, Lafon L, Heizen H, Ferreira M, Morquio A.
Departamento de Neuroquimica, Instituto de Investigaciones Biol gicas Clemente Estable, Universidade da Republica, Montevideo, Uruguay.
The high morbidity, high socioeconomic costs and lack of specific treatments are key factors that define the relevance of brain pathology for human health and the importance of research on neuronal protective agents. Epidemiological studies have shown beneficial effects of flavonoids on arteriosclerosis-related pathology in general and neurodegeneration in particular. Flavonoids can protect the brain by their ability to modulate intracellular signals promoting cellular survival. Quercetin and structurally related flavonoids (myricetin, fisetin, luteolin) showed a marked cytoprotective capacity in in vitro experimental conditions in models of predominantly apoptotic death such as that induced by medium concentrations (200 M) of H2O2 added to PC12 cells in culture. Nevertheless, quercetin did not protect substantia nigra neurons in vivo from an oxidative insult (6-hydroxydopamine), probably due to difficulties in crossing the blood-brain barrier. On the other hand, treatment of permanent focal ischemia with a lecithin/quercetin preparation decreased lesion volume, showing that preparations that help to cross the blood-brain barrier may be critical for the expression of the effects of flavonoids on the brain. The hypothesis is advanced that a group of quercetin-related flavonoids could become lead molecules for the development of neuroprotective compounds with multitarget anti-ischemic effects.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14666245&dopt=Abstract lecithin [PubMed - in process]
Comp Biochem Physiol B. 1989;94(2):389-94.
Studies on the structure of lecithin:cholesterol acyltransferase (LACT)--comparisons of the active site region and secondary structure of the human and the porcine enzymes.
Yuksel KU, Park YB, Jung JH, Gracy RW, Lacko AG.
Department of Biochemistry, Texas College of Osteopathic Medicine, Fort Worth.
1. Chemical modification of essential serine, histidine and cysteine residues of porcine LCAT were accompanied by loss of enzymatic activity. 2. Modification of cysteine with DTNB inactivated the enzyme which could not be reactivated by KCN suggesting direct involvement of the cysteine residue(s) in catalysis. 3. About half of the primary structure of the porcine enzyme was determined. 4. Respective regions of the human and porcine LCAT are highly homologous; especially, the amino-terminus and the region surrounding the DFP-labeled serine residues. 5. The observed primary structure differences represent amino acid substitutions that are projected to induce significant changes in secondary structure.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2591200&dopt=Abstract lecithin
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