| For medical practitioners and the general public - Cholesterol Journal Article Catalog. |
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| Interaction of sialosyl cholesterol with the cell surface of rat astrocytes and its biological activities Ito, J., T. Kato, et al. (1992), Neurochem Int 20(4): 493-9. Abstract: The interaction between sialosyl cholesterol (alpha- or beta-D-N-acetyl neuraminyl cholesterol, alpha- or beta-SC) and the plasma membrane of astrocytes was investigated by the use of 14C-labeled alpha- or beta-SC. Both alpha- and beta-SC were dose-dependently and time-dependently bound to rat astrocytes. The Scatchard plot analyses showed that rat astrocytes bound apparently 9.69 x 10(9) molecules of both alpha-SC/cell (apparent Kd = 2.29 x 10(-5) M) and beta-SC/cell (apparent Kd = 5.39 x 10(-5) M) at 37 degrees C. Both the binding of alpha-SC to astrocytes and the subsequent inhibition of DNA synthesis were decreased at the low temperature (4 degrees C), and also suppressed by serum proteins including albumin. One molecule of bovine serum albumin (BSA) bound 2.3 molecules of alpha-SC with the slightly lower Kd-value (8.03 x 10(-6) M) than that for the binding site on astrocytes. BSA not only suppressed the alpha-SC-binding to astrocytes but also increased its release from the cells to the culture media. Gangliosides such as GM1 and GM3 unaffected the alpha-SC-binding, promoted the small release of alpha-SC from the cell surface, and inhibited the morphological changes of astrocytes induced by alpha-SC. The mechanism of alpha-SC-binding to cultured astrocytes with reference to the effects of serum or gangliosides is discussed. |
| Interaction of the cholesteryl ester transfer protein I405V polymorphism with alcohol consumption in smoking and non-smoking healthy men, and the effect on plasma HDL cholesterol and apoAI concentration Gudnason, V., K. Thormar, et al. (1997), Clin Genet 51(1): 15-21. Abstract: Three hundred and sixteen healthy Icelandic men and women were examined for the effect of the cholesteryl ester transfer protein (CETP) I405V polymorphism on plasma triglycerides, HDL cholesterol (HDLC) and apoAI concentration. Genotyping was performed using an allele specific oligomelting assay and the frequency of the V allele was 0.31 (95 CI for men 0.23-0.33 and for women 0.29-0.39). In women no significant difference was associated with the V405 genotype for any plasma lipid trait. However, men who were homozygous for the V405 allele had 9% higher apoAI and 14% higher HDLC levels (p < 0.05) than those homozygous for the common I405 allele. The genotype effect was seen only in the non-smokers (p = 0.07 and < 0.05, respectively), and in those consuming alcohol (p < 0.05 for both). Analysis of interaction between the environmental, life-style factors and genotype in men for the traits of HDLC and apoAI showed statistically significant interaction of the genotype only with alcohol consumption. The non-smoking men who reported alcohol consumption and who were homozygous for the CETP V405 allele had 16% higher plasma apoAI concentration than those who carried the I405 allele, and up to 20% higher apoAI level than smokers. On the basis of prospective studies carried out on the Icelandic population, non-smoking, alcohol-consuming men who are homozygous for the V405 allele could have from 32% to 40% lower risk of having a heart attack. |
| Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study Harris, J. R., S. Bhakdi, et al. (2002), J Struct Biol 139(2): 122-35. Abstract: The Vibrio cholerae cytolysin (VCC) 63-kDa monomer has been shown to interact in aqueous suspension with cholesterol microcystals to produce a ring/pore-like heptameric oligomer approximately 8 nm in outer diameter. Transmission electron microscopy data were produced from cholesterol samples adsorbed to carbon support films, spread across the holes of holey carbon films, and negatively stained with ammonium molybdate. The VCC oligomers initially attach to the edge of the stacked cholesterol bilayers and with increasing time cover the two planar surfaces. VCC oligomers are also released into solution, with some tendency to cluster, possibly via the hydrophobic membrane-spanning domain. At the air/water interface, the VCC oligomers are likely to be selectively oriented with the hydrophobic domain facing the air. Despite some molecular disorder/plasticity within the oligomers, multivariate statistical analysis and rotational self-correlation using IMAGIC-5 strongly suggest the presence of sevenfold rotational symmetry. To correlate the electron microscopy data with on-going biochemical and permeability studies using liposomes of varying lipid composition, the direct interaction of VCC with several cholesterol derivatives and other steroids has been examined. 19-Hydroxycholesterol and 7 beta-hydroxycholesterol both induce VCC oligomerization. beta-Estradiol, which does not possess an aliphatic side chain, also efficiently induces VCC oligomer formation, as does cholesteryl acetate. Cholesteryl stearate and oleate and the C22 (2-trifluoroacetyl)naphthyloxy analogue of cholesterol fail to induce VCC oligomerization, but binding of the monomer to the surface of these steroids does occur. Stigmasterol has little tendency to induce oligomer formation, and oligomers are largely confined to the edge of the bilayers; ergosterol has even less oligomerization ability. Attempts to solubilize and stabilize the VCC oligomers from cholesterol suspensions have been pursued using the neutral surfactant octylglucoside. Although individual solubilized oligomers have been defined which exhibit a characteristic cytolysin channel conformation in the side-on orientation, a tendency remains for the oligomers to cluster via their hydrophobic domains. |
| Interactions between cholesterol and lipids in bilayer membranes. Role of lipid headgroup and hydrocarbon chain-backbone linkage Bhattacharya, S. and S. Haldar (2000), Biochim Biophys Acta 1467(1): 39-53. Abstract: We have employed four lipids in the present study, of which two are cationic and two bear phosphatidylcholine (PC) headgroups. Unlike dipalmitoylphosphatidylcholine, the other lipids employed herein do not have any ester linkage between the hydrocarbon chains and the respective lipid backbones. Small unilamellar vesicles formed from each of the PC and cationic lipids with or without varying amounts of cholesterol have been examined using the steady-state fluorescence anisotropy method as a function of temperature. The anisotropy data clearly indicate that the order in the lipid bilayer packing is strongly affected upon inclusion of cholesterol. This effect is similar irrespective of the electrostatic character of the lipid employed. The influence of cholesterol inclusion on multi-lamellar lipid dispersions has also been examined by 1H-nuclear magnetic resonance spectroscopy above the phase transition temperatures. With all the lipids, the line widths of (CH2)n protons of hydrocarbon chains in the NMR spectra respond to the addition of cholesterol to membranes. The influence on the bilayer widths of various lipids upon inclusion of cholesterol was determined from X-ray diffraction studies of the cast films of the lipid-cholesterol coaggregates in water. The effect of cholesterol on the efflux rates of entrapped carboxyfluorescein (CF) from the phospholipid vesicles was determined. Upon incremental incorporation of cholesterol into the phospholipid vesicles, the CF leakage rates were progressively reduced. Independent experiments measuring transmembrane OH- ion permeation rates from cholesterol-doped cationic lipid vesicles using entrapped dye riboflavin also demonstrated that the addition of cholesterol into the cationic lipid vesicles reduced the leakage rates irrespective of lipid molecular structure. It was found that the cholesterol induced changes on the membrane properties such as lipid order, linewidth broadening, efflux rates, bilayer widths, etc., did not depend on the ability of the lipids to participate in the hydrogen bonding interactions with the 3beta-OH of cholesterol. These findings emphasize the importance of hydrophobic interaction between lipid and cholesterol and demonstrate that it is not necessary to explain the observed cholesterol induced effects on the basis of the presence of hydrogen bonding between the 3beta-OH of cholesterol and the lipid chain-backbone linkage region or headgroup region. |
| Interactions between common genetic polymorphisms in ABCG5/G8 and CYP7A1 on LDL cholesterol-lowering response to atorvastatin Kajinami, K., M. E. Brousseau, et al. (2004), Atherosclerosis 175(2): 287-93. Abstract: Cholesterol excretion by ATP binding cassette transporters G5 and G8 (ABCG5/G8) and bile acid biosynthesis by cholesterol 7alpha-hydroxylase (CYP7A1) are major pathways for the removal of cholesterol into bile. To investigate the interactions between common polymorphisms in ABCG5/G8 and CYP7A1 and statin response, we examined the relationships between five non-synonymous polymorphisms in ABCG5/G8 (Q604E, D19H, Y54C, T400K, and A632V) and a promoter variant in CYP7A1 (A-204C) in 337 hypercholesterolemic patients treated with atorvastatin 10mg. The ABCG8 H19 allele was significantly associated with a greater LDL cholesterol reduction relative to the wild type D19 allele (39.6% versus 36.6%, P = 0.043). This difference was enhanced in non-carriers of the CYP7A1 promoter polymorphism (42.7% versus 38.2%, P = 0.048), and was diminished in accordance with the number of CYP7A1 variant alleles (1.8% in heterozygotes and 0.2% in homozygotes). Combination analysis of these polymorphisms explained a greater percentage of LDL cholesterol response variation (8.5% difference across subgroups) than did single polymorphism analysis (4.2% in CYP7A1 and 3.0% in ABCG8 D19H). The other ABCG5/G8 polymorphisms did not show any significant interactions with the CYP7A1 polymorphism. We conclude that the ABCG8 H19 and CYP7A1 C-204 alleles appear to interact in a dose-dependent manner on atorvastatin response. |
| Interactions between metabolism and intracellular distribution of cholesterol and sphingomyelin Ridgway, N. D. (2000), Biochim Biophys Acta 1484(2-3): 129-41. Abstract: There is ample evidence from experimental models and human metabolic disorders indicating that cholesterol and sphingomyelin (SM) levels are coordinately regulated. Generally it has been observed that altering the cellular content of sphingomyelin or cholesterol results in corresponding changes in mass and/or synthesis of the other lipid. In the case of cholesterol synthesis and trafficking, SM regulates the capacity of membranes to absorb cholesterol and thereby controls sterol flux between the plasma membrane and regulatory pathways in the endoplasmic reticulum. This relationship exemplifies the importance of cholesterol/sphingolipid-rich domains in cholesterol homeostasis, as well as other aspects of cell signaling and transport. Evidence for regulation of sphingomyelin metabolism by cholesterol is less convincing and dependent on the model system under study. Sphingomyelin biosynthetic rates are not dramatically affected by alterations in cholesterol balance suggesting that sphingomyelin or its metabolites serve other indispensable functions in the cell. A notable exception is the robust and specific regulation of both SM and cholesterol synthesis by 25-hydroxycholesterol. This finding is reviewed in the context of the role of oxysterol binding protein and its putative role in cholesterol and SM trafficking between the plasma membrane and Golgi apparatus. |
| Interactions between phosphatidylcholines and cholesterol in monolayers at the air/water interface Dynarowicz-Latka, P. and K. Hac-Wydro (2004), Colloids Surf B Biointerfaces 37(1-2): 21-5. Abstract: Mixtures of cholesterol and synthetic phospholipids, differing in saturation of phosphatidylcholine (PC) acyl chains, such as distearoyl phosphatidylcholine (DSPC), stearoyl-oleoyl phosphatidylcholine (SOPC) and dioleoyl phosphatidylcholine (DOPC) have been studied as floating Langmuir monolayers at the air/water interface. In order to examine the influence of a polar group, distearoyl phosphatidylethanolamine (DSPE) was chosen. The films were spread at room temperature on aqueous subphases and characterized by the surface pressure-area (pi-A) isotherms and compression modulus (C(s)(-1)) values. The interactions were examined by analyzing the mean molecular areas and quantified by the excess free energy of mixing values. The obtained results indicate that the affinity of cholesterol to saturated/unsaturated phosphatidylcholines does not differ significantly, and revealed strong influence of the kind of a polar group on the cholesterol-phospholipid interactions. On the other hand, the apolar group structure was found to modify the stoichiometry of sterol-PC complexes. |
| Interactions between poly(2-ethylacrylic acid) and lipid bilayer membranes: effects of cholesterol and grafted poly(ethylene glycol) Needham, D., J. Mills, et al. (1998), Faraday Discuss(111): 103-10; discussion 137-57. Abstract: The exchange of the protonatable polymer, poly(2-ethylacrylic acid) (PEAA), has been studied with vesicle membranes containing cholesterol from 0 to 60 mol% or PEG2000-lipid (5 mol%). The release of an entrapped dye from 100 nm extruded liposomes was used as an assay for membrane perturbation by the polymer as a function of pH. The inclusion of cholesterol was found to reduce the pH at which the polymer caused release of the dye from the lipid vesicles, and the degree of polymer protonation (i.e., degree of hydrophobicity) correlated well with the increase in elastic expansion modulus of the vesicle bilayer. The results are discussed in terms of a balance between polymer solubility and membrane expansion. With respect to the PEG barrier, the presence of 5 mol% PEG2000, which represents full surface coverage, did not prevent PEAA from inducing contents release, demonstrating that highly hydrated polymeric layers are not effective barriers for other water soluble polymers, and may point to some association between the two polymers. |
| Interactions of apolipoprotein E genotype, total cholesterol level, age, and sex in prediction of Alzheimer's disease: a case-control study Jarvik, G. P., E. M. Wijsman, et al. (1995), Neurology 45(6): 1092-6. Abstract: OBJECTIVE: The joint effects of total cholesterol (TC) levels and the APOE genotype in Alzheimer's disease (AD) were evaluated because of previous reports that the APOE locus epsilon 4 allele was associated with both late-onset AD and elevated TC. DESIGN: Logistic regression was used to determine the effects of the APOE genotype, TC, age, and sex on prediction of AD in a community-based study of 206 cases and 276 controls. RESULTS: The relationship of the APOE genotype and AD was dependent on TC, age, and sex. However, current TC level does not fully explain the epsilon 4-Alzheimer's disease association. Affected men with higher TC and age under 80 years had the highest epsilon 4 allele frequencies. The epsilon 4 frequency declined significantly with age. SIGNIFICANCE: A pathologic role of higher TC or cholesterol-based differential survival of epsilon 4-carrying individuals may be involved in the relationship of the epsilon 4 allele with AD. The observed association of the APOE genotype and AD is expected to depend on the age, sex, and TC distributions of a given sample. |
| Interactions of cholesterol with cyclodextrins in aqueous solution Nishijo, J., S. Moriyama, et al. (2003), Chem Pharm Bull (Tokyo) 51(11): 1253-7. Abstract: The interaction of cholesterol with several cyclodextrins (CDs) was investigated in water using solubility method. It was found that heptakis (2,6-di-O-methyl)-beta-CD (DOM-beta-CD) forms two types of soluble complex, with molar ratios of 1: 1 and 1: 2 (cholesterol: DOM-beta-CD), and neither a soluble nor insoluble complex is formed between cholesterol and alpha-CD, beta-CD, and gamma-CD, although a minor soluble complex formation was observed between cholesterol and 2-hydroxylpropyl-beta-CD. The thermodynamic parameters for 1: 1 and 1: 2 complex formation of cholesterol with DOM-beta-CD obtained from the changes in K with temperature are as follows: DeltaG degrees (1: 1)=-11.6 kJ/mol at 25 degrees C (K(1: 1)=1.09x10(2) M(-1)); DeltaH degrees (1: 1)=-3.38 kJ/mol; TDeltaS degrees (1: 1)=8.25 kJ/mol; DeltaG degrees (1: 2)=-27.1 kJ/mol at 25 degrees C (K(1: 2)=5.68x10(4) M(-1)); DeltaH degrees (1: 2)=-3.96 kJ/mol; and TDeltaS degrees (1: 2)=23.2 kJ/mol. The formation of the 1: 2 complex occurred much more easily than that of the 1: 1 complex. The driving force for 1: 1 and 1: 2 complex formation was considered to be mainly hydrophobic interaction. Also, based on the measurements of proton nuclear magnetic resonance spectra and studies with Corey-Pauling-Koltun atomic models, the probable structutures of the 1: 2 complex were estimated. |
| Interactions of cholesterol with lipid bilayers: the preferred configuration and fluctuations Kessel, A., N. Ben-Tal, et al. (2001), Biophys J 81(2): 643-58. Abstract: The free energy difference associated with the transfer of a single cholesterol molecule from the aqueous phase into a lipid bilayer depends on its final location, namely on its insertion depth and orientation within the bilayer. We calculated desolvation and lipid bilayer perturbation contributions to the water-to-membrane transfer free energy, thus allowing us to determine the most favorable location of cholesterol in the membrane and the extent of fluctuations around it. The electrostatic and nonpolar contributions to the solvation free energy were calculated using continuum solvent models. Lipid layer perturbations, resulting from both conformational restrictions of the lipid chains in the vicinity of the (rigid) cholesterol backbone and from cholesterol-induced elastic deformations, were calculated using a simple director model and elasticity theory, respectively. As expected from the amphipathic nature of cholesterol and in agreement with the available experimental data, our results show that at the energetically favorable state, cholesterol's hydrophobic core is buried within the hydrocarbon region of the bilayer. At this state, cholesterol spans approximately one leaflet of the membrane, with its OH group protruding into the polar (headgroup) region of the bilayer, thus avoiding an electrostatic desolvation penalty. We found that the transfer of cholesterol into a membrane is mainly driven by the favorable nonpolar contributions to the solvation free energy, whereas only a small opposing contribution is caused by conformational restrictions of the lipid chains. Our calculations also predict a strong tendency of the lipid layer to elastically respond to (thermally excited) vertical fluctuations of cholesterol so as to fully match the hydrophobic height of the solute. However, orientational fluctuations of cholesterol were found to be accompanied by both an elastic adjustment of the surrounding lipids and by a partial exposure of the hydrophobic cholesterol backbone to the polar (headgroup) environment. Our calculations of the molecular order parameter, which reflects the extent of orientational fluctuations of cholesterol in the membrane, are in good agreement with available experimental data. |
| Interactions of cholesterol with lipid membranes and cyclodextrin characterized by calorimetry Tsamaloukas, A., H. Szadkowska, et al. (2005), Biophys J 89(2): 1109-19. Abstract: Interactions of cholesterol (cho) with different lipids are commonly believed to play a key role in the formation of functional domains in membranes. We introduce a novel approach to characterize cho-lipid interactions by isothermal titration calorimetry. Cho is solubilized in the aqueous phase by reversible complexation with methyl-beta-cyclodextrin (cyd). Uptake of cho into the membrane is measured upon a series of injections of lipid vesicles into a cyd/cho solution. As an independent assay, cho release from membranes is measured upon titrating lipid/cho mixed vesicles into a cyd solution. The most consistent fit to the data is obtained with a mole fraction (rather than mole ratio) partition coefficient and considering a cho/cyd stoichiometry of 1:2. The results are discussed in terms of contributions from 1), the transfer of cho from cyd into a hypothetical, ideally mixed membrane and 2), from nonideal interactions with POPC. The latter are exothermic but opposed by a strong loss in entropy, in agreement with cho-induced acyl chain ordering and membrane condensation. They are accompanied by a positive heat capacity change which cannot be interpreted in terms of the hydrophobic effect, suggesting that additive-induced chain ordering itself increases the heat capacity. The new assays have a great potential for a better understanding of sterol-lipid interactions and yield suggestions how to optimize cho extraction from membranes. |
| Interactions of cholesterol with the membrane lipid matrix. A solid state NMR approach Leonard, A. and E. J. Dufourc (1991), Biochimie 73(10): 1295-302. Abstract: The effects of cholesterol on the structure and dynamics of dimyristoylphosphatidylcholine (DMPC) model membranes have been monitored as functions of temperature and cholesterol concentration in the membrane. The use of deuterium labels both on the cholesterol fused ring system and on the lipid chains in conjunction with solid state deuterium nuclear magnetic resonance (2H-NMR) afforded to monitor the degree of ordering of both molecules in a mixed system. The degree of ordering of the lipid head group was followed by phosphorus-31 (31P)-NMR. New findings on the effect of cholesterol on DMPC may be summarized as follows: i) cholesterol disorders the lipid chains below temperature of the DMPC gel-to-fluid transition (Tc) and orders them above; the effect is linear with cholesterol concentration at 0 and 60 degrees C but for intermediate temperatures, a saturation effect is observed at 20-30 mol %; ii) the ordering-disordering effects are perceived similarly by all chain segments with, however, a greater sensitivity for positions near the bilayer center; iii) below Tc, the lipid head group is considerably disordered by increasing amounts of cholesterol but slightly affected above; iv) the degree of ordering of cholesterol is quasi temperature independent for fractions greater than or equal to 30%; v) the average orientation of the cholesterol rigid body is perpendicular to the bilayer surface and exhibits little variations with temperature and cholesterol concentration. Variations in membrane dynamics are interpreted in terms of cholesterol-induced changes in bilayer thickness.(ABSTRACT TRUNCATED AT 250 WORDS) |
| Interactions of cholesterol/cholesteryl esters with dimyristoylphosphatidylcholine bilayers Husain, R., P. H. Beswick, et al. (1990), Biochem Soc Trans 18(2): 325. |
| Interactions of cholesterol-containing liposomes with serum lipoproteins Zakharova, T. S., A. S. Ivanov, et al. (1991), Biomed Sci 2(6): 629-33. Abstract: The interaction of liposomes containing different amounts of cholesterol with low-density lipoproteins from human serum was investigated. The efficiency of the interaction was found to depend on the cholesterol content of the liposomes and was highest for liposomes with the maximum cholesterol:phospholipid molar ratio. These liposomes selectively and effectively interacted with low-density lipoproteins; up to 90% of lipoprotein particles interacted with liposomes in serum. Fusion of particles with liposomes was observed during the interaction. |
| Interactions of cyclosporin A with phospholipid membranes: effect of cholesterol Soderlund, T., J. Y. Lehtonen, et al. (1999), Mol Pharmacol 55(1): 32-8. Abstract: Cyclosporin A (CsA) is a highly hydrophobic drug used to prevent graft rejection after organ transplantation. Interactions of CsA with phosphatidylcholine as well as with binary mixtures containing phosphatidylcholine and cholesterol were investigated by measuring the penetration of CsA into lipid monolayers at an air/water interface, by differential scanning calorimetry, and by imaging with fluorescence microscopy the effects of CsA on the lateral distribution of a fluorescent probe, 1-palmitoyl-2-(N-4-nitrobenz-2-oxa-1, 3-diazol)aminocaproyl-phosphocholine, in monolayers. Film penetration studies revealed the association of CsA with lipids to be a biphasic process. Cholesterol diminished the intercalation of CsA into the monolayer at surface pressures of >19 mN/m. CsA broadened the main transition of dimyristoylphosphatidylcholine (DMPC)/beta-cholesterol (10:1, mol/mol) multilamellar vesicles. The behavior of the transition enthalpy was more complex; the behavior of DMPC/beta-cholesterol multilamellar vesicles in the XCsA of 0 to 0.1 showed at most ratios a increase, but several well distinct dips were observed. The results are interpreted in terms of regular structures in tertiary alloy. Influence of CsA on lateral organization could be verified for lipid domains observed by fluorescence microscopy of lipid monolayers. More specifically, CsA altered the distribution of 1-palmitoyl-2-(N-4-nitrobenz-2-oxa-1, 3-diazol)aminocaproyl-phosphocholine in a dipalmitoylphosphatidylcholine film and in DPPC/beta-cholesterol (88:10, mol/mol) mixtures in a manner that suggests that CsA partitions into the boundaries between fluid and gel domains. To our knowledge, this constitutes the first demonstration of a change in lipid domain morphology to be induced by a drug molecule. |
| Interactions of dicarboxylic porphyrins with unilamellar lipidic vesicles: drastic effects of pH and cholesterol on kinetics Kuzelova, K. and D. Brault (1995), Biochemistry 34(35): 11245-55. Abstract: The effect of pH on the transfer of deuteroporphyrin from dimyristoylphosphatidylcholine (DMPC) unilamellar vesicles to human serum albumin is investigated using a stopped-flow with fluorescence detection. The kinetics of this process allows for the determination of the rate constants for the porphyrin exist from the outer vesicle layer to the bulk aqueous medium (koff), and for its movement from the inner to the outer vesicle layer (kto). Both koff and kto are found to strongly depend on the pH. The observed behavior can be described by classical titration curves and is most likely due to protonation equilibria involving the two carboxylic groups of the porphyrin. A pH increase accelerates the exist of the porphyrin. The reverse effect is observed for its movement through the bilayer. The presence of cholesterol in the DMPC bilayer also strongly affects the interactions of the porphyrin with the vesicles. The rate constant kto is dramatically reduced by increasing the cholesterol content. An irregularity is noted around 10-20 mol % cholesterol. The results are discussed in relation to the preferential uptake of porphyrins by tumors, a basis of photodynamic therapy, and to possible pH-mediated relocalization of porphyrins among subcellular structures. |
| Interactions of lipid metabolism and intestinal physiology with Tremella fuciformis Berk edible mushroom in rats fed a high-cholesterol diet with or without Nebacitin Cheng, H. H., W. C. Hou, et al. (2002), J Agric Food Chem 50(25): 7438-43. Abstract: Male adult Wistar rats were randomly divided into six groups in a 2 x 3 factorial design and fed diets containing different levels of Tremella fuciformis Berk (TFB) dietary fiber (0, 5, or 10%) and 1 g of cholesterol/100 g of diet with or without 0.7% Nebacitin for 4 weeks. TFB contained 6.2% soluble dietary fiber and 57.3% insoluble dietary fiber. The results showed that the serum LDL-cholesterol, hepatic total cholesterol, and triglyceride levels were significantly decreased (P < 0.05) in the rats fed diets with TFB content with or without Nebacitin. However, the serum total cholesterol, VLDL-cholesterol, and triglyceride levels were significantly decreased (P < 0.05) by Nebacitin. In feces, the presence of TFB (T5, T10, AT5, and AT10) in the diet significantly increased the total neutral steroids and bile acid excretions and undigested fiber concentrations as compared to T0 or AT0. In the small intestine, the Nebacitin diets increased the weights of both cecum and colon-rectum contents and lowered short-chain fatty acid (SCFA) concentrations of serum and cecal contents more than no Nebacitin diets did. It was suggested that the hypocholesterolemic effect of TFB dietary fiber may be mediated by the increase in fecal neutral steroids and total bile acids excretion and the increase in SCFA productions. The TFB edible mushroom dietary supplement altered the intestinal physiology of the rats. |
| Interactions of N-stearoyl sphingomyelin with cholesterol and dipalmitoylphosphatidylcholine in bilayer membranes Maulik, P. R. and G. G. Shipley (1996), Biophys J 70(5): 2256-65. Abstract: Differential scanning calorimetry and x-ray diffraction have been utilized to investigate the interaction of N-stearoylsphingomyelin (C18:0-SM) with cholesterol and dipalmitoylphosphatidylcholine (DPPC). Fully hydrated C18:0-SM forms bilayers that undergo a chain-melting (gel -->liquid-crystalline) transition at 45 degrees C, delta H = 6.7 kcal/mol. Addition of cholesterol results in a progressive decrease in the enthalpy of the transition at 45 degrees C and the appearance of a broad transition centered at 46.3 degrees C; this latter transition progressively broadens and is not detectable at cholesterol contents of >40 mol%. X-ray diffraction and electron density profiles indicate that bilayers of C18:0-SM/cholesterol (50 mol%) are essentially identical at 22 degrees C and 58 degrees C in terms of bilayer periodicity (d = 63-64 A), bilayer thickness (d rho-p = 46-47 A), and lateral molecular packing (wide-angle reflection, 1/4.8 A-(1)). These data show that cholesterol inserts into C18:0-SM bilayers, progressively removing the chain-melting transition and altering the bilayer structural characteristics. In contrast, DPPC has relatively minor effects on the structure and thermotropic properties of C18:0-SM. DPPC and C18:0-SM exhibit complete miscibility in both the gel and liquid-crystalline bilayer phases, but the pre-transition exhibited by DPPC is eliminated at >30 mol% C18:0-SM. The bilayer periodicity in both the gel and liquid-crystalline phases decreases significantly at high DPPC contents, probably reflecting differences in hydration and/or chain tilt (gel phase) of C18:0-SM and DPPC. |
| Interactions of pulmonary surfactant protein SP-A with monolayers of dipalmitoylphosphatidylcholine and cholesterol: roles of SP-A domains Yu, S. H., F. X. McCormack, et al. (1999), J Lipid Res 40(5): 920-9. Abstract: Pulmonary surfactant protein A (SP-A) is an oligomeric glycoprotein that binds dipalmitoylphosphatidylcholine (DPPC). Interactions of rat SP-A and recombinant SP-As with pure and binary monolayers of DPPC and cholesterol were studied using a rhomboid surface balance at 37 degrees C. A marked inflection at equilibrium surface tension (23 mN/m) in surface tension-area isotherm of a pure DPPC film was abolished by rat SP-A. The inflection was decreased and shifted to 18 mN/m with wild-type recombinant SP-A (SP-Ahyp). Both rat SP-A and SP-Ahyp decreased surface area reduction required for pure DPPC films to reach near zero surface tension from 30 to 25%. SP-Ahyp, E195Q,R197D, mutated in carbohydrate recognition domain (CRD) known to be essential for SP-A-vesicle interactions, conveyed a detrimental effect on DPPC surface activity. SP-ADeltaG8-P80, with deletion of collagen-like domain, had little effect. Both SP-Ahyp, C6S (Ser substitution for Cys6) and SP-Ahyp,DeltaN1-A7 (N-terminal segment deletion) which appear mainly as monomers on non-reducing SDS-PAGE analysis, increased required surface area reduction for minimal surface tension. All SP-As reduced collapse surface tension of a pure cholesterol film from 27 to 23 mN/m in the presence of Ca2+. When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. These results demonstrate the importance of CRD and N-terminal dependent oligomerization in SP-A-phospholipid associations. The findings further indicate that SP-A-cholesterol interactions differ from SP-A-DPPC interactions and may be nonspecific. |