References: Lecithin
Hepatology. 1997 Sep;26(3):527-36.
Effect of maternal cholestasis on biliary lipid and bile acid secretion in the infant rat.
El-Mir MY, Monte MJ, Morales AI, Arevalo M, Serrano MA, Marin JJ.
Department of Physiology and Pharmacology, University of Salamanca, Spain.
Partial and reversible impairment of bile formation has been reported to occur in the offspring of rats undergoing common bile duct ligation during the last third of pregnancy. This situation was defined as latent cholestasis of the neonate and was suggested to be related to the multilamellar bodies partially occupying the canalicular lumen. The current study was undertaken to investigate the presence of alterations in the secretion of biliary lipids in these infant rats. Using both high-performance liquid chromatography (HPLC) and gas chromatography-mass spectrometry (GC-MS) analyses, no changes caused by maternal cholestasis were found in either the conjugation pattern, or in the ratio of primary to secondary major bile acids in bile samples collected from 4-week-old and 8-week-old rats. However, a decrease in the proportion of cholate together with an increase in the amount of alpha- and omega-muricholate were found at 4 weeks of age. These changes were different from those observed in the pattern of maternal plasma bile acids, in which beta-, but not alpha-muricholate, concentrations were increased. Moreover, studies performed by labeling the bile acid pool of the cholestatic mother-fetus tandem with [14C]glycocholic acid (GC) at day 16 of pregnancy indicated that only a minor proportion (approximately 10%) of bile acids found in 4-week-old pups was of maternal origin. Changes in the bile acid pool composition were fully reversed by 8 weeks of age. Bile lecithin and cholesterol output were determined by enzymatic techniques, both under basal conditions and during stepwise taurocholate (TC) infusion. At the time when multilamellar bodies were found, i.e., 4 weeks after birth, no change in either nonstimulated or TC-induc
Appl Environ Microbiol. 1996 Apr;62(4):1252-6. ["Free in PMC","window.top.location='http://www.pubmedcentral.gov/articlerender.fcgi?tool=pubmed&pubmedid=8919785'","",""],
Influence of environmental parameters on phosphatidylcholine phospholipase C production in Listeria monocytogenes: a convenient method to differentiate L. monocytogenes from other Listeria species.
Coffey A, Rombouts FM, Abee T.
Department of Food Science, Wageningen Agricultural University, Netherlands.
The ability to produce phosphatidylcholine phospholipase C (lecithinase) is associated with virulence in pathogenic species of Listeria. Levels of production vary greatly among members of the genus, and this virulence factor is not readily detectable in many members of the pathogenic species on conventional agar media containing egg yolk, a common substrate for the enzyme. In this study, the influence of a variety of environmental parameters, including temperature, pH, and salt concentration, on the production of lecithinase by a number of strains was evaluated. Lecithinase production by Listeria monocytogenes LO28 in brain heart infusion medium was optimal at 1.75 to 2.0% NaCl; pH 7.0 to 7.3, and 37 to 40 degrees C, and the presence of oxygen had no effect. In a chemically defined medium, the optimal NaCl concentration and temperature were lower at 0.75 to 1.0% NaCl and 33.5 degrees C. As detection of virulence factors is useful to assist in the identification and differentiation of Listeria species, this report shows that lecithinase activity can conveniently be detected within 36 h on a relatively inexpensive medium. Under the conditions described, L. monocytogenes could be distinguished from other members of the genus as a result of distinct lecithin degradation which was not evident in L. innocua, L. seeligeri, L. ivanovii, L. welshimeri, or L. murrayi/grayi.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8919785&dopt=Abstract lecithin
J Biol Chem. 1997 Dec 12;272(50):31333-9.
The effect of apolipoprotein A-II on the structure and function of apolipoprotein A-I in a homogeneous reconstituted high density lipoprotein particle.
Durbin DM, Jonas A.
Department of Biochemistry, College of Medicine at Urbana-Champaign, University of Illinois, Urbana, Illinois 61801, USA.
In this study we examined the effects of apoA-II on the structure and function of apoA-I in homogeneous reconstituted HDL (rHDL). First, we measured the binding of apoA-II to apoA-I-rHDL, containing dipalmitoylphosphatidylcholine or palmitoyloleoylphosphatidylcholine, and the degree of apoA-I displacement at various ratios of apolipoproteins. Using fluorescence methods, we determined that apoA-II binding is rapid, irreversible, and associated with apoA-I displacement only when the molar ratio of apoA-II/apoA-I is greater than 1:2. Next, we used the stable apoA-II/apoA-I-rHDL complex at the apoA-II/apoA-I ratio of 1:2 to examine its physical properties, apoA-I structure, and reactivity with lecithin:cholesterol acyltransferase (LCAT). Using chemical cross-linking in conjunction with fluorescence and electrophoretic methods, we demonstrated that the conformation of apoA-I must be flexible to allow apoA-II binding to the apoA-I-rHDL particles and showed that the hybrid particles have an unchanged Stokes diameter. Fluorescence and circular dichroism measurements revealed little or no change in the secondary structure or in the N-terminal domain of apoA-I, but showed a marked destabilization of apoA-I to denaturation by guanidine hydrochloride. Limited tryptic digestion indicated that the central region of apoA-I becomes accessible to proteolysis in the hybrid particles. Together, these results suggest that amphipathic alpha-helices of apoA-II replace four central helices of one apoA-I molecule (residues approximately 99-187) in the complex and in the process destabilize apoA-I. Thus, apoA-II binding at physiologic ratios may not completely displace apoA-I from HDL, b
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