References: Lecithin
Vision Res. 2003 Dec;43(28):3037-44.
Visual cycle retinoid processing proteins are present in HEK293S cells.
Chen Y, Moiseyev G, Wu BX, Ma JX, Crouch RK.
Department of Ophthalmology, Medical University of South Carolina, 167 Ashley Avenue, 29425, Charleston, SC, USA
In HEK293S cells expressing opsin, rhodopsin regenerates on addition of all-trans retinol. This study was to determine if key proteins in the retinal pigment epithelium (RPE) are present in these cells. Cellular retinoid binding protein, cellular retinoic-acid binding protein, RPE65, caveolin-1-alpha- and -beta-isoforms, interphotoreceptor retinoid binding protein, and 11-cis retinol dehydrogenase, but not lecithin:retinol acyltransferase (LRAT), were identified by Western blot analysis. LRAT transcripts were found by RT-PCR and Southern blot analysis. Small interference RNA specific to LRAT reduced ester formation, confirming that the enzyme is present. Therefore, HEK293S cells contain the functional components of the retinoid cycle found in the RPE.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14611939&dopt=Abstract lecithin
J Biomed Mater Res. 2003 Dec 1;67A(3):813-27.
Preparation, degradation, and calcification of biodegradable polyurethane foams for bone graft substitutes.
Gorna K, Gogolewski S.
Polymer Research, AO/ASIF Research Institute, Clavadelerstrasse, CH-7270 Davos, Switzerland.
Autogenous cancellous bone graft is used to heal critical-size segmental long bone defects and defects in the maxillofacial skeleton. Harvesting of bone graft is traumatic, causes morbidity of the donor site, and often results in complications. Thus, there is a need for new biologically functional bone graft substitutes that, instead of autogenous bone graft, could be used to facilitate bone regeneration in critical-size defects. Porous biodegradable elastomeric polyurethane scaffolds combined with the patient's own bone marrow could potentially be such bone substitutes. The elastomeric bone substitute prevents shear forces at the interface between bone and rigid, e.g., ceramic bone substitutes and establishes an intimate contact with the native bone ends, thus facilitating the proliferation of osteogenic cells and bone regeneration. Crosslinked 3D biodegradable polyurethane scaffolds (foams) with controlled hydrophilicity for bone graft substitutes were synthesized from biocompatible reactants. The scaffolds had hydrophilic-to-hydrophobic content ratios of 70:30, 50:50, and 30:70. The reactants used were hexamethylene diisocyanate, poly(ethylene oxide) diol (MW = 600) (hydrophilic component), and poly(epsilon-caprolactone) diol (M(w) = 2000), amine-based polyol (M(w) = 515) or sucrose-based polyol (M(w) = 445) (hydrophobic component), water as the chain extender and foaming agent, and stannous octoate, dibutyltin dilaurate, ferric acetylacetonate, and zinc octoate as catalysts. Citric acid was used as a calcium complexing agent, calcium carbonate, glycerol phosphate calcium salt, and hydroxyapatite were used as inorganic fillers, and lecithin or solutions of vitamin D(3) were used as surfactants. The scaffolds had an open-pore str
Protein Sci. 1995 Apr;4(4):791-803. ["Protein","window.top.location='Laxative online source: www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?db=PubMed&cmd=Display&dopt=pubmed_protein&from_uid=7613477'","",""],
Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
Schindler PA, Settineri CA, Collet X, Fielding CJ, Burlingame AL.
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143, USA.
Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS). A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation. In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides. Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS. All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures. The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78. These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides. Previous studies of LCAT indicated that removal o
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