References: Lecithin
Indian J Exp Biol. 1995 Oct;33(10):749-51.
Effects of S-allyl cysteine sulfoxide isolated from Allium sativum Linn and gugulipid on some enzymes and fecal excretions of bile acids and sterols in cholesterol fed rats.
Sheela CG, Augusti KT.
Department of Bio-Chemistry, University of Kerala, Thiruvananthapuram, India.
S-allyl cysteine sulfoxide, isolated from garlic, A. sativum, is more or less as active as gugulipid in controlling hypercholestermia, obesity and derangement of enzyme activities in cholesterol diet fed rats. The beneficial effects of the drugs are partly due to their inhibitory effects on transaminases, alkaline phosphatase, lipogenic enzymes and HMG CoA reductase and partly due to their stimulatory effects on plasma lecithin-cholesterol acyl transferase lipolytic enzymes and fecal excretion of sterols and bile acids.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8575806&dopt=Abstract lecithin
Indian J Exp Biol. 1995 Oct;33(10):796-7.
Pulmonary phospholipid changes induced by butylated hydroxy toluene, an antioxidant, in rats.
Tamizhselvi R, Samikkannu T, Niranjali S.
Department of Biochemistry, University of Madras, India.
Butylated hydroxy toluene (BHT), 800 mg/kg body weight, dissolved in corn oil and administered (ip) in a single injection to male rats, damaged the lung as indicated by an increase in lavage ACE, protein and LDH and caused a significant increase in phospholipid, particularly, phosphatidyl choline (PC) in lung lavage and extracellular surfactant. The plasma lecithin cholesterol acyl transferase (LCAT) activity was inhibited leading to an increase in serum phospholipids and phosphatidyl choline. The results indicate that BHT-induced lung phospholipidosis may be attributed to an increase in surfactant phospholipids and/or due to the leakage of plasma phospholipids through damaged capillary membrane.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8575813&dopt=Abstract lecithin
Biochem J. 1993 May 1;291 ( Pt 3):697-700.
Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase.
Saari JC, Bredberg DL, Farrell DF.
Department of Ophthalmology, School of Medicine, University of Washington, Seattle 98195.
Esterification of all-trans-retinol is a key reaction of the vertebrate visual cycle, since it produces an insoluble, relatively non-toxic, form of the vitamin for storage and supplies substrate for the isomerization reaction. CoA-dependent and -independent pathways have been described for retinol esterification in retinal pigment epithelium (RPE). The CoA-independent reaction, catalysed by lecithin:retinol acyltransferase (LRAT) was examined in more detail in this study. Addition of retinol to RPE microsomes results in a burst of retinyl ester synthesis, followed by a rapid apparent cessation of the reaction. However, [3H]retinol, added when retinyl ester synthesis has apparently ceased, is rapidly incorporated into retinyl ester without a net increase in the amount of ester. The specific radioactivities of [3H]retinol and [3H]retinyl ester reach the same value. [14C]Palmitate from palmitoyl-CoA is incorporated into preexisting retinyl ester in the absence of net ester synthesis, too. These exchange reactions suggest that the reaction has reached equilibrium at the plateau of the progress curve and that only the accumulation of retinyl ester, and not its synthesis, has stopped during this phase of the reaction. Studies with geometrical isomers of retinol revealed that the rate of exchange of all-trans-retinol with all-trans-retinyl esters was about 6 times more rapid than exchange of 11-cis-retinol with 11-cis-retinyl ester. This is the first demonstration of the reversibility of LRAT and the first example of stereospecificity of retinyl ester synthesis in the visual system. Reversal of the LRAT reaction could contribute to the mobilization of 11-cis-retinol from 11-cis-retinyl ester pools.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8489497&dopt=Abstract lecithin [PubMe
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