References: Lecithin
Exp Cell Res. 1993 Nov;209(1):33-7.
Regulation of vitamin A transport into cultured stellate cells of rat liver: studies by anchored cell analysis and sorting system.
Matsuura T, Nagamori S, Hasumura S, Sujino H, Niiya M, Shimizu K.
Department of Internal Medicine I, Jikei University School of Medicine, Tokyo, Japan.
Stellate cells (SC) in the liver store the most retinoid in the body, but the mechanisms of specific retinoid transport into SC remain to be elucidated. In this study, to analyze the retinoid content of cultured SC, we employed an anchored cell analysis and sorting system (ACAS), which provides fluorescence analysis of single cultured cells under the phase-contrast microscope by utilizing a laser. First, we examined the effect of retinol binding protein (RBP) on retinol transport into cultured SC of rat liver. Rat holo-RBP added to the medium inhibited retinol uptake into SC. We also prepared RBP-free human serum by affinity chromatography using conjugated anti-human RBP IgG and compared retinoid fluorescence of SC cultured in human serum with or without RBP. No significant difference in retinoid fluorescence intensity was observed between SC cultured with and without holo-RBP. Second, the removal of cellular retinol by esterification may be important for the continued uptake of retinol. Retinyl esters are stored in lipid droplets of SC. Therefore we examined the relationship between the lipid droplet number and the retinoid fluorescence intensity in SC which were cultured in medium containing retinol for 1-3 days. The increases in lipid droplet number and in retinoid fluorescence in SC were almost parallel. Progesterone, previously shown to increase the esterification of retinol by lecithin:retinol acyltransferase (LRAT) in vitro, was added to the SC medium; progesterone facilitated retinol uptake in cultured SC. In conclusion, RBP did not facilitate specific retinol transport into SC. However, the specific transport of retinol is likely to be dependent on the intracellula
Indian J Lepr. 1988 Oct;60(4):593-9.
Use of non-conventional antigen: M. habana in detecting M. leprae antibodies from leprosy patients and contacts in FLA-ABS test.
Rana NS, Gupta HP, Singh NB.
Division of Microbiology, Central Drug Research Institute, Lucknow.
An indirect immunofluorescent (FLA-ABS) test has been developed to detect M. leprae specific antibodies in the active and subclinical cases of leprosy. An antigenically related mycobacterium, M. habana, was used as an antigen to detect M. leprae specific antibodies in the sera samples of leprosy patients. A comparison was made with M. leprae antigen using same set of sera samples. M. habana is capable of detecting anti-M. leprae antibodies in the serum samples of leprosy patients, previously absorbed with various mycobacterial antigens, cardiolipin and lecithin, almost to the same percentage as M. leprae. Possible use of M. habana antigen as an alternative to M. leprae, in the serodiagnosis of leprosy, has been discussed.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3075637&dopt=Abstract lecithin
Biochemistry. 1992 Nov 17;31(45):11112-7.
Regulation of the concentration of pre beta high-density lipoprotein in normal plasma by cell membranes and lecithin-cholesterol acyltransferase activity.
Miida T, Kawano M, Fielding CJ, Fielding PE.
Cardiovascular Research Institute, University of California, San Francisco 94143.
A minor fraction of plasma high-density lipoprotein (pre beta-1 HDL) has been shown to promote cholesterol efflux from peripheral cell membranes [Castro, G. R., & Fielding, C. J. (1988) Biochemistry 27, 25-29]. When isolated native plasma is incubated at 37 degrees C, this fraction is specifically decreased. On the other hand, the level of plasma pre beta-1 HDL is fully protected in the presence of even very low levels of fibroblasts, vascular smooth muscle cells, or macrophages. Blood cells were completely inactive in maintaining plasma pre beta-1 HDL levels in the absence of peripheral cells, even at the relatively high levels present in whole blood. The loss of pre beta-1 observed in isolated plasma was dependent upon lecithin-cholesterol acyltransferase (LCAT) activity. These data suggest that reverse cholesterol transport catalyzed by pre beta-1 HDL, and subsequent LCAT-mediated cholesterol esterification, is directly dependent upon the interaction between this HDL species and competent peripheral cells.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1445850&dopt=Abstract lecithin
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