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Serum Albumin (serum + albumin)
Kinds of Serum Albumin Terms modified by Serum Albumin Selected AbstractsMolecular Interaction between a Gadolinium,Polyoxometalate and Human Serum AlbuminEUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 34 2009Li Zheng Abstract Polyoxometalates (POMs) show promising antibacterial, antiviral (particularly anti-HIV), antitumor, and anticancer activities, but the mechanism of these potential therapeutic effects remains to be elucidated at the molecular level. The interaction between the Gd-containing tungstosilicate [Gd(,2 -SiW11O39)2]13, and human serum albumin (HSA) was studied by several techniques. Fluorescence spectroscopy showed an energy transfer between the single tryptophan residue of HSA and the POM. Circular dichroism led to the conclusion that the POM significantly altered the secondary structure of HSA. Isothermal titration calorimetry revealed an enthalpy-driven binding reaction between HSA and the POM, resulting in the formation of a 1:1 complex.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009) [source] Bovine Serum Albumin and Lysozyme Adsorption on Calcium Phosphate ParticlesADVANCED ENGINEERING MATERIALS, Issue 1-2 2010Berit Mueller Two model proteins that are oppositely charged at neutral pH , bovine serum albumin (BSA) and lysozyme, with acidic and alkaline isoelectric points, respectively , are used to investigate the protein adsorption behaviour of hydroxyapatite and beta-tricalcium phosphate (, -TCP) particles. Both calcium phosphate based particles are highly relevant for the fabrication of bioactive and resorbable bone implants. The investigations are carried out by combining zeta potential and Vis spectroscopy measurements. The changes of zeta potential and isoelectric point are determined as a function of added protein. Both proteins form a monolayer on , -TCP, while on hydroxyapatite only semi-monolayers were measured. For BSA, a side-on adsorption mode is suggested, whereas end-on adsorption appears to be most likely for lysozyme. The zeta potential curves as a function of adsorbed protein show that plateaus of the protein amounts adsorbed increase with charge saturation. In addition, the spatial charge distribution of both proteins is modelled to get a further understanding of the initial adsorption orientation of the biomolecules, supporting the findings from the experimental data. The reported findings can be transferred to the adsorption behaviour of a variety of proteins on calcium phosphate surfaces and are helpful for the fabrication of bone-analogous calcium phosphate/protein nanocomposites. [source] Stabilization of PbS Nanocrystals by Bovine Serum Albumin in its Native and Denatured StatesADVANCED FUNCTIONAL MATERIALS, Issue 9 2009Mandeep Singh Bakshi Abstract PbS nanocrystals (NCs) are synthesized in aqueous phase within a temperature range of 40,80,°C in the presence of native and denatured states of bovine serum albumen (BSA) as the capping/stabilizing agent. The NCs are characterized with the help of field-emission scanning electron microscopy, high-resolution transmission electron microscopy, X-ray diffraction, and energy-dispersive X-ray analysis. At 40,°C, large ball-shaped NCs (145,±,37,nm) with small surface protrusions are formed when 1,×,10,4,g mL,1 BSA is used. As the reaction temperature is increased towards 80,°C, the size of NCs decreases and they acquire somewhat cubic geometries (49.1,±,7.0,nm) due to a change in the capping behavior of BSA between its native and denatured states. The native and denatured states of BSA are simultaneously studied by fluorescence spectroscopy using tryptophan emission, and pH measurements with respect to time and temperature. Gel electrophoresis is used to determine the polarity of the BSA capped NCs. Only the small sized NCs conjugated with relatively larger amounts of BSA show a displacement towards the positively charged electrode in comparison to larger NCs with lower amounts of BSA capping. It was concluded that the denatured state of BSA is more effective in controlling the crystal growth of PbS than its native state especially in the low concentration range. [source] Lower Levels of Serum Albumin and Total Cholesterol Associated with Decline in Activities of Daily Living and Excess Mortality in a 12-Year Cohort Study of Elderly JapaneseJOURNAL OF AMERICAN GERIATRICS SOCIETY, Issue 3 2008Tomonori Okamura MD OBJECTIVES: To examine the association between levels of serum albumin and total cholesterol (TC) and risk of subsequent mortality and future decline in activities of daily living (ADLs) in elderly people. DESIGN: Population-based cohort study. SETTING: National Integrated Project for Prospective Observation of Non-Communicable Disease and Its Trends in the Aged, 1980. PARTICIPANTS: One thousand eight hundred forty-four Japanese individuals aged 60 to 74 randomly selected throughout Japan and followed for 12.4 years. MEASUREMENTS: Decline in ADLs and mortality. RESULTS: After adjusting for other covariates, the multivariable odds ratios (ORs) of impaired ADLs were highest in the lowest albumin quartile (,40 g/L) for women. The multivariable OR of having a composite outcome of death or impaired ADL for the lowest albumin quartile compared with the highest was 1.56 (95% confidence interval (CI)=1.94,2.57) for men and 3.06 (95% CI=1.89,4.95) for women. Serum albumin was significantly and inversely associated with a composite outcome of death or impaired ADLs in the group below the median of TC in both sexes (multivariable OR for 1-g/L increase in serum albumin=0.88 for men (95% CI=0.79,0.97) and 0.79 for women (95% CI=0.72,0.87)), which was not significantly associated in the group with TC at or above the median. CONCLUSION: In the Japanese general population, low-normal serum albumin and TC levels are associated with loss of activity during old age, especially for women. [source] The Value of Serum Albumin and High-Density Lipoprotein Cholesterol in Defining Mortality Risk in Older Persons with Low Serum CholesterolJOURNAL OF AMERICAN GERIATRICS SOCIETY, Issue 9 2001Stefano Volpato MD OBJECTIVES: To investigate the relationship between low cholesterol and mortality in older persons to identify, using information collected at a single point in time, subgroups of persons with low and high mortality risk. DESIGN: Prospective cohort study with a median follow-up period of 4.9 years. SETTINGS: East Boston, Massachusetts; New Haven, Connecticut; and Iowa and Washington counties, Iowa. PARTICIPANTS: Four thousand one hundred twenty-eight participants (64% women) age 70 and older at baseline (mean 78.7 years, range 70,103); 393 (9.5%) had low cholesterol, defined as ,160 mg/dl. MEASUREMENTS: All-cause mortality and mortality not related to coronary heart disease and ischemic stroke. RESULTS: During the follow-up period there were 1,117 deaths. After adjustment for age and gender, persons with low cholesterol had significantly higher mortality than those with normal and high cholesterol. Among subjects with low cholesterol, those with albumin> 38 g/L had a significant risk reduction compared with those with albumin ,38 g/L (relative risk (RR) = 0.57; 95% confidence interval (CI) = 0.41,0.79). Within the higher albumin group, high-density lipoprotein cholesterol (HDL-C) level further identified two subgroups of subjects with different risks; participants with HDL-C <47 mg/dl had a 32% risk reduction (RR = 0.68; 95% CI = 0.47,0.99) and those with HDL-C ,47 mg/dl had a 62% risk reduction (RR = 0.38; 95% CI = 0.20,0.68), compared with the reference category; those with albumin ,38 g/L and HDL-C <47 mg/dl. CONCLUSIONS: Older persons with low cholesterol constitute a heterogeneous group with regard to health characteristics and mortality risk. Serum albumin and HDL-C can be routinely used in older patients with low cholesterol to distinguish three subgroups with different prognoses: (1) high risk (low albumin), (2) intermediate risk (high albumin and low HDL-C), and (3) low risk (high albumin and high HDL-C). [source] Encapsulation and/or Release Behavior of Bovine Serum Albumin within and from Polylactide-Grafted Dextran MicrospheresMACROMOLECULAR BIOSCIENCE, Issue 4 2004Tatsuro Ouchi Abstract Summary: Polylactide (PLA)-grafted dextran (Dex- graft -PLA) of various contents of sugar units was synthesized by anionic polymerization of L -lactide (L -LA) using the alkoxide of partially trimethylsilylated dextran (TMSDex) and subsequently removing the trimethylsilyl (TMS) groups. The copolymer showed different solubility from L -LA homopolymer with increasing the content of sugar units. We prepared bovine serum albumin (BSA)-loaded microspheres (MS)s according to a water-in-oil-in-water emulsion-solvent evaporation/extraction method using methylene chloride/DMSO as an organic cosolvent. MSs prepared from Dex- graft -PLA [MS(Dex- graft -PLA)s] exhibited higher loading efficiency of BSA than MSs prepared from PLLA [MS(PLLA)s]. The in vitro release rate of BSA from MS(Dex- graft -PLA) was faster than that from MS(PLLA). BSA released from MS(Dex- graft -PLA) maintained the secondary structure of native BSA to a great extent, compared with BSA released from MS(PLLA). Confocal fluorescence images of the differential interference micrographs over the fluorescence images of MS(PLLA) and MS(Dex- graft -PLA). [source] A Novel Approach to Magnetic Nanoadsorbents with High Binding Capacity for Bovine Serum AlbuminMACROMOLECULAR RAPID COMMUNICATIONS, Issue 3 2007Yabin Sun Abstract Magnetic nanoadsorbents using Fe3O4 nanoparticles as cores and poly(methyl acrylic acid) (PMAA) as ionic exchange groups were prepared through our novel approach. Two steps were involved in this approach: the first was to functionalize the magnetic nanoparticles (MNPs) with methacrylate double bonds via the combination of ligand exchange and condensation of methacryloxypropyltrimethoxysilane(MPS); the second was to graft PMAA chains onto the surface of MNPs through radical polymerization. The success of the various surface functionalization steps was ascertained using FTIR and XPS. The as-synthesized PMAA-coated MNPs were effective in binding bovine serum albumin (BSA) with a high capacity of 1,300 mg,·,g,1. [source] Flavin-sensitized Photo-oxidation of Lysozyme and Serum AlbuminPHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 4 2009Yazhou Zhang The excited state processes of riboflavin, flavin mononucleotide and flavin adenine dinucleotide in argon-saturated aqueous solution were studied in the presence of lysozyme or bovine serum albumin (BSA). UV,Vis absorption and fluorescence spectroscopy indicates that the noncovalent flavin-protein binding is relatively weak. Quenching of the flavin triplet state by BSA, observed by time-resolved photolysis, is less efficient than by lysozyme. Light-induced oxidation of the two proteins and reduction of the three flavins were studied. The quantum yields of the former and latter in the absence of oxygen are up to 0.1 and 0.04, respectively. The effects of pH and sensitizer and protein concentrations were examined in greater detail. The proposed reaction is electron transfer from the tryptophan moiety to the flavin triplet rather than excited singlet state. [source] Molecular Recognition in Partially Folded States of a Transporter Protein: Temperature-dependent Specificity of Bovine Serum AlbuminPHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 3 2008Debapriya Banerjee The specificity of molecular recognition of a transporter protein bovine serum albumin (BSA) in its different partially folded states has been studied. In order to avoid complications due to chemical denaturation, we have prepared thermally induced partially folded states of the protein. The partially folded states have been structurally characterized by circular dichroism and differential thermal analysis techniques. The change in the globular structure of the protein as a consequence of thermal unfolding has also been characterized by dynamic light scattering. Steady state, picosecond-resolved fluorescence and polarization gated spectroscopies on the ligands (DCM, LDS 750) in the protein reveal the dynamics of the binding sites and the specificity of ligand binding of BSA. Picosecond resolved Förster resonance energy transfer studies on the donor DCM and acceptor LDS 750 confirm that the specificity of ligand binding in the binding site is maintained up to 70°C. At 75°C, the protein loses its specificity of recognition at the aforesaid site. [source] Binding of Warfarin Influences the Acid-Base Equilibrium of H242 in Sudlow Site I of Human Serum AlbuminPHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 5 2006Jennifer L. Perry ABSTRACT Sudlow Site I of human serum albumin (HSA) is located in subdomain IIA of the protein and serves as a binding cavity for a variety of ligands. In this study, the binding of warfarin (W) is examined using computational techniques and isothermal titration calorimetry (ITC). The structure of the docked warfarin anion (W,) to Site I is similar to that revealed by X-ray crystallography, with a calculated binding constant of 5.8 × 105M,1. ITC experiments (pH 7.13 and I = 0.1) carried out in three different buffers (MOPs, phosphate and Tris) reveal binding of W, is accompanied by uptake of 0.30 ± 0.02 protons from the solvent. This measurement suggests that the binding of W, is stabilized by an ion-pair interaction between protonated H242 and the phenoxide group of W,. [source] Photophysics in Motionally constrained Bioenvironment: Interactions of Norharmane with Bovine Serum Albumin,PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 2 2005Arabinda Mallick ABSTRACT Steady-state photophysics of norharmane (NHM), a bioactive alkaloid, has been studied in the presence of a model transport protein, bovine serum albumin (BSA). The emission spectrum undergoes a remarkable change upon addition of BSA to the aqueous solution of NHM in buffer. Addition of BSA leads to a marked increase in the fluorescence anisotropy of the neutral species of NHM, although the fluorescence anisotropy for the cationic species is almost invariant to BSA addition, suggesting that the neutral species is located in a motionally restricted environment of BSA, whereas the cationic species remains in the bulk aqueous phase. The binding constant (K) and free energy change (,G) for the probe-protein binding have been calculated from the fluorescence data. Light has been thrown on the action of urea on protein-bound NHM. The denaturation study suggests that the protein, in its native form, binds with NHM. Polarity of the microenvironment around the probe has been determined from a comparison of the fluorescence properties of the two prototropic species of NHM in water-dioxane mixture with varying composition. [source] A chloroplast transgenic approach to hyper-express and purify Human Serum Albumin, a protein highly susceptible to proteolytic degradationPLANT BIOTECHNOLOGY JOURNAL, Issue 2 2003Alicia Fernández-San Millán Summary Human Serum Albumin (HSA) accounts for 60% of the total protein in blood serum and it is the most widely used intravenous protein in a number of human therapies. HSA, however, is currently extracted only from blood because of a lack of commercially feasible recombinant expression systems. HSA is highly susceptible to proteolytic degradation in recombinant systems and is expensive to purify. Expression of HSA in transgenic chloroplasts using Shine-Dalgarno sequence (SD), which usually facilitates hyper-expression of transgenes, resulted only in 0.02% HSA in total protein (tp). Modification of HSA regulatory sequences using chloroplast untranslated regions (UTRs) resulted in hyper-expression of HSA (up to 11.1% tp), compensating for excessive proteolytic degradation. This is the highest expression of a pharmaceutical protein in transgenic plants and 500-fold greater than previous reports on HSA expression in transgenic leaves. Electron micrographs of immunogold labelled transgenic chloroplasts revealed HSA inclusion bodies, which provided a simple method for purification from other cellular proteins. HSA inclusion bodies could be readily solubilized to obtain a monomeric form using appropriate reagents. The regulatory elements used in this study should serve as a model system for enhancing expression of foreign proteins that are highly susceptible to proteolytic degradation and provide advantages in purification, when inclusion bodies are formed. [source] Characterization of a Ruthenium(III)/NAMI-A Adduct with Bovine Serum Albumin that Exhibits a High Anti-Metastatic Activity,ANGEWANDTE CHEMIE, Issue 9 2010Mimi Liu Ru-ndum erneuert: Röntgenabsorptionsspektroskopische Studien belegen, dass der RuIII -Wirkstoff NAMI-A alle seine Cl, - und S-Donor-Liganden gegen N-Donoren und Carboxylatogruppen von Rinderserumalbumin (BSA) austauschen kann (siehe Schema). Das RuIII -BSA-Addukt verstärkt Zell-Substrat-Wechselwirkungen ebenso stark wie NAMI-A (das sich im Zellkulturmedium binnen Minuten in RuIII -BSA umwandelt). [source] The Structure of the Sugar Residue in Glycated Human Serum Albumin and Its Molecular Recognition by Phenylboronate.CHEMINFORM, Issue 32 2003Jan Rohovec No abstract is available for this article. [source] Synthesis of Gold Microplates Using Bovine Serum Albumin as a Reductant and a StabilizerCHEMISTRY - AN ASIAN JOURNAL, Issue 1 2010Leslie Au Abstract Gold microplates were synthesized in aqueous solutions by reducing HAuCl4 with the hydroxyl groups in both serine and threonine of bovine serum albumin (BSA), which is a globular protein in its native state. In this article, we systematically investigated the effects of temperature, pH value, the concentration of BSA, and ionic species on the reduction kinetics and thus the size and morphology of the final product. The optimal experimental conditions for producing uniform Au microplates include the following: an elevated temperature in the range of 55,65,°C, an acidic solution with pH,3, and the presence of NaCl (0.14,M). We found that if any one of these parameters was deviated from the optimal condition, Au microplates would not be formed in high yields. We also found that the surfaces of the as-synthesized Au microplates were covered by a dense array of BSA bumps. [source] The Influence of Surface Composition of Nanoparticles on their Interactions with Serum AlbuminCHEMPHYSCHEM, Issue 14 2010Dr. Lennart Treuel Abstract Interactions between differently functionalised silver and gold nanoparticles (NPs) as well as polystyrene nanoparticles with bovine serum albumin (BSA) are studied using circular dichroism (CD) spectroscopy. It is found that the addition of NPs to the protein solution destroys part of the helical secondary structure of the protein as a result of surface adsorption. From the loss of free protein and hence the extent of their structural change adsorption equilibrium constants are derived. The results reveal that citrate-coated gold and silver NPs exhibit much stronger interactions with BSA than polymeric or polymer-coated metallic NPs. It is therefore concluded that for the particles considered, the influence of surface composition on the interaction behaviour dominates that of the core. [source] Conformational Stability of Bovine Serum Albumin in Aqueous Amides: A Further Insight into the Mechanism of Urea Acting on the ProteinCHINESE JOURNAL OF CHEMISTRY, Issue 6 2010Lin Ma Abstract The binding distances of fluorescein to bovine serum albumin (BSA) in formamide-water and N,N -dimethyl- formamide-water mixtures were determined by fluorescence quenching method and compared with the values in urea-water mixtures in our previous work. The results, together with the analysis of fluorescence spectra, were utilized to probe the conformational stability of protein in aqueous amides, providing a further insight into the mechanism of urea acting on protein. The spectral properties of BSA showed significant difference in the aqueous solutions of the three kinds of amide and indicated that both NH2 group and C=O group could form hydrogen bond with the protein, serving as donor and acceptor, respectively. However, the results revealed that the multiple hydrogen bonds of NH2 group with back bond and hydrophilic side chains of the protein played a key role in the nonspecific urea-mediated network of intramolecular interaction due to its higher hydrogen bonding capability compared to C=O group. [source] A High Performance Theory for Thermodynamic Study on the Binding of Human Serum Albumin with Erbium ChlorideCHINESE JOURNAL OF CHEMISTRY, Issue 2 2009G. Rezaei BEHBEHANI Abstract A thermodynamic study of the interaction between erbium(III) chloride (Er3+) and human serum albumin (HSA) was studied at pH=7.0, 27 and 37 °C in phosphate buffer by isothermal titration calorimetry (ITC). The present study reports the thermodynamic parameters that govern HSA-Er3+ interactions. The extended solvation theory was used to reproduce the enthalpies of HSA-Er3+ interactions over the whole range of Er3+ concentrations. The binding parameters recovered from the new model were attributed to the structural change of HSA and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Er3+ ions with negative cooperativity. The enhancement of complex formation by Er3+ and concomitant increase in ?S suggest that the metal ion plays a role in increasing the number of hydrophobic contacts. The binding parameters discovered from the extended solvation model indicate that the stability of HSA molecule is increased as a result of its interaction with Er3+ ions. [source] Interaction of Co(II) with Bovine Serum Albumin under UV C IrradiationCHINESE JOURNAL OF CHEMISTRY, Issue 8 2007He-Dong Zhang Abstract The interaction of Co(II) with BSA under UV C (253.7 nm) irradiation under physiological conditions has been studied by UV-vis spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The quenching rate constant kq and the association constant Ka were calculated according to Stern-Volmer equation based on the quenching of the fluorescence of BSA by Co(II). [source] Study on Interaction of Ginsenosides with Bovine or Human Serum Albumin Using Wavelength Modulation Surface Plasmon Resonance BiosensorCHINESE JOURNAL OF CHEMISTRY, Issue 5 2006Xia Liu Abstract To use a newly developed wavelength modulation surface plasmon resonance (SPR) biosensor, an experimental protocol was developed to investigate the interaction of ginsenosides with serum albumin. With a known concentration of the ginsenosides, bound percentages of the ginsenosides with human serum albumin (HSA) or bovine serum albumin (BSA) were obtained. SPR technique could require no labeling and this method provided the detailed information on association and disassociation of molecules in real time. The results indicate that the sensitivity of wavelength modulation SPR biosensor is sufficient for detection and characterization of binding events involving low-molecular weight compounds and their immobilized protein targets. [source] Study on the Interaction of Ketoconazole with Human and Bovine Serum Albumins by Fluorescence SpectroscopyCHINESE JOURNAL OF CHEMISTRY, Issue 12 2008Qing-Lian GUO Abstract The binding of ketoconazole to human serum albumin and bovine serum albumin was studied by using fluorescence and ultraviolet spectroscopy. The measurements were performed in 0.1 mol·L,1 phosphate buffer solution at pH=7.40±0.1. Decreasing of quenching constant was observed in association with temperature increase. Our findings show that the quenching mechanism of fluorescence of serum albumins by ketoconazole was static quenching because of compound formation. The thermodynamic parameters ,G, ,H, and ,S at different temperatures were calculated, showing that the electrostatic interactions and hydrophobic interaction are the main forces for the binding of ketoconazole to serum albumins. The distance r between the donor (Trp-214) and acceptor (ketoconazole) was obtained according to fluorescence resonance energy transfer theory. [source] Effects of the Interaction of Rifamycin SV with Serum Albumins on the Resonance Rayleigh Scattering Spectra and Their Analytical ApplicationCHINESE JOURNAL OF CHEMISTRY, Issue 5 2008Ji-Dong YANG Abstract In pH 4.5,4.8 Britton-Robinson buffer solution, rifamycin SV (i.e. rifamycin sodium) can react with serum albumin such as human serum albumin (HSA) and bovine serum albumin (BSA) to form macromolecular complexes by electrostatic attraction and hydrophobic force. As a result, the resonance Rayleigh scattering (RRS) of the drug was enhanced remarkably and the RRS peaks were at 374 and 552 nm. The enhancement of RRS (,I) is directly proportional to the concentration of HSA or BSA. The linear ranges and the detection limits are 0.03,6.0 µg/mL and 9.0 ng/mL for HSA, and 0.01,8.0 µg/mL and 2.0 ng/mL for BSA, respectively. In this work, a sensitive, selective, simple and fast method for the determination of trace amounts of serum albumin by RRS technique has been developed, which was applied to the determination of serum albumin in the synthesized samples and human urine samples with satisfactory results. [source] An investigation into the use of serum albumin in pressure sore predictionJOURNAL OF ADVANCED NURSING, Issue 2 2000Denis Anthony RMN RGN BA MSc PhD AMIEE An investigation into the use of serum albumin, in pressure sore prediction Objectives To ascertain the relevance of serum albumin and serum sodium as predictors of pressure sores in addition to the Waterlow score. Design Observational study of patients at risk of developing decubitus ulcers. Setting Staffordshire, in the midlands of the United Kingdom. Participants 773 elderly hospital in-patients of a district general hospital. Measurements Waterlow scores and serum albumin and sodium. Development of a pressure sore. Results Logistic regression analysis of serum albumin, serum sodium and the Waterlow score showed the Waterlow score and serum albumin were significant predictors of pressure sores. Conclusions Serum albumin may, in this patient group (in-patients over 64 years of age), be a useful predictor of pressure sore occurrence, though further work is needed to establish whether this is the case. Risk assessment of pressure sores can possibly be improved by adding serum albumin to one of the pre-existing tools such as the Waterlow score. [source] Lower Levels of Serum Albumin and Total Cholesterol Associated with Decline in Activities of Daily Living and Excess Mortality in a 12-Year Cohort Study of Elderly JapaneseJOURNAL OF AMERICAN GERIATRICS SOCIETY, Issue 3 2008Tomonori Okamura MD OBJECTIVES: To examine the association between levels of serum albumin and total cholesterol (TC) and risk of subsequent mortality and future decline in activities of daily living (ADLs) in elderly people. DESIGN: Population-based cohort study. SETTING: National Integrated Project for Prospective Observation of Non-Communicable Disease and Its Trends in the Aged, 1980. PARTICIPANTS: One thousand eight hundred forty-four Japanese individuals aged 60 to 74 randomly selected throughout Japan and followed for 12.4 years. MEASUREMENTS: Decline in ADLs and mortality. RESULTS: After adjusting for other covariates, the multivariable odds ratios (ORs) of impaired ADLs were highest in the lowest albumin quartile (,40 g/L) for women. The multivariable OR of having a composite outcome of death or impaired ADL for the lowest albumin quartile compared with the highest was 1.56 (95% confidence interval (CI)=1.94,2.57) for men and 3.06 (95% CI=1.89,4.95) for women. Serum albumin was significantly and inversely associated with a composite outcome of death or impaired ADLs in the group below the median of TC in both sexes (multivariable OR for 1-g/L increase in serum albumin=0.88 for men (95% CI=0.79,0.97) and 0.79 for women (95% CI=0.72,0.87)), which was not significantly associated in the group with TC at or above the median. CONCLUSION: In the Japanese general population, low-normal serum albumin and TC levels are associated with loss of activity during old age, especially for women. [source] The Value of Serum Albumin and High-Density Lipoprotein Cholesterol in Defining Mortality Risk in Older Persons with Low Serum CholesterolJOURNAL OF AMERICAN GERIATRICS SOCIETY, Issue 9 2001Stefano Volpato MD OBJECTIVES: To investigate the relationship between low cholesterol and mortality in older persons to identify, using information collected at a single point in time, subgroups of persons with low and high mortality risk. DESIGN: Prospective cohort study with a median follow-up period of 4.9 years. SETTINGS: East Boston, Massachusetts; New Haven, Connecticut; and Iowa and Washington counties, Iowa. PARTICIPANTS: Four thousand one hundred twenty-eight participants (64% women) age 70 and older at baseline (mean 78.7 years, range 70,103); 393 (9.5%) had low cholesterol, defined as ,160 mg/dl. MEASUREMENTS: All-cause mortality and mortality not related to coronary heart disease and ischemic stroke. RESULTS: During the follow-up period there were 1,117 deaths. After adjustment for age and gender, persons with low cholesterol had significantly higher mortality than those with normal and high cholesterol. Among subjects with low cholesterol, those with albumin> 38 g/L had a significant risk reduction compared with those with albumin ,38 g/L (relative risk (RR) = 0.57; 95% confidence interval (CI) = 0.41,0.79). Within the higher albumin group, high-density lipoprotein cholesterol (HDL-C) level further identified two subgroups of subjects with different risks; participants with HDL-C <47 mg/dl had a 32% risk reduction (RR = 0.68; 95% CI = 0.47,0.99) and those with HDL-C ,47 mg/dl had a 62% risk reduction (RR = 0.38; 95% CI = 0.20,0.68), compared with the reference category; those with albumin ,38 g/L and HDL-C <47 mg/dl. CONCLUSIONS: Older persons with low cholesterol constitute a heterogeneous group with regard to health characteristics and mortality risk. Serum albumin and HDL-C can be routinely used in older patients with low cholesterol to distinguish three subgroups with different prognoses: (1) high risk (low albumin), (2) intermediate risk (high albumin and low HDL-C), and (3) low risk (high albumin and high HDL-C). [source] Structural and ligand-binding properties of serum albumin species interacting with a biomembrane interfaceJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 11 2007Takamitsu Kosa Abstract In the process of drug development, preclinical testing using experimental animals is an important aspect, for verification of the efficacy and safety of a drug. Serum albumin is a major binding protein for endogenous and exogenous ligands and regulates their distribution in various tissues. In this study, the structural and drug-binding properties of albumins on a biomembrane surface were investigated using reverse micelles as a model membrane. In reverse micelles, the secondary structures of all albumins were found, to varying degrees, to be intermediate between the native and denatured states. The tertiary structures of human and bovine albumin were similar to those of the native and intermediate states, respectively, whereas those of the dog, rabbit, and rat were in a denatured state. Thus, bovine albumin is an appropriate model for studying structural changes in human albumin in a membrane-water phase. Binding studies also showed the presence of species difference in the change in binding capacity of albumins during their interaction with reverse micelles. Among the albumins, rat albumin appears to be a good model for the protein-mediated drug uptake of human albumin in a biomembrane environment. These findings are significant in terms of the appropriate extrapolation of pharmacokinetics and pharmacodynamics data in various animals to humans. © 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96: 3117,3124, 2007 [source] Association of Serum Pentosidine With Arterial Stiffness in Hemodialysis PatientsARTIFICIAL ORGANS, Issue 3 2010YiLun Zhou Abstract Pentosidine is an advanced glycation end product (AGE). The present study was undertaken to investigate the association of serum pentosidine with carotid distensibility as a measure of arterial stiffness in hemodialysis patients. One hundred and three patients on maintenance hemodialysis were recruited. The distensibility coefficient of the common carotid artery was evaluated by an ultrasonic phase-locked echo-tracking system. Serum pentosidine was measured by competitive enzyme-linked immunosorbent assay. Serum albumin, lipid profile, calcium, phosphorus, intact parathyroid hormone (iPTH), high-sensitivity C-reactive protein (hs-CRP), and oxidized low-density lipoprotein (ox-LDL) levels were also measured. Correlation was determined by linear and multiple stepwise regression analysis. Serum pentosidine level studied in hemodialysis patients was 0.54 ± 0.13 µg/mL. No significant difference in serum pentosidine level was noted between patients with and without diabetes (0.59 ± 0.10 µg/mL vs. 0.53 ± 0.13 µg/mL, P = 0.062) as well as between patients with and without prior cardiovascular disease (CVD) history (0.56 ± 0.14 µg/mL vs. 0.53 ± 0.12 µg/mL, P = 0.206). In multivariate regression analysis, only age (, = 0.363, P < 0.001) and ox-LDL (, = 0.262, P = 0.004) were identified as independent determinants for serum pentosidine. Serum pentosidine was significantly correlated with carotid distensibility (r = ,0.387, P < 0.001), as well as age, ox-LDL, and hs-CRP. After adjustment for age, blood pressure, history of diabetes, prior CVD history, lipid profile, calcium, phosphorus, iPTH, hs-CRP, and ox-LDL, serum pentosidine was still negatively correlated with distensibility (, = ,0.175, P = 0.044). Serum pentosidine was independently associated with carotid distensibility in hemodialysis patients. This finding suggested that the accumulation of AGE might be an important pathway in the development of arterial stiffness in end-stage renal disease. [source] Serum Albumin-Catalyzed Trigger System by Using a Tandem Kemp Elimination/,-Elimination ReactionCHEMBIOCHEM, Issue 5 2005Guillaume Boucher Dr. Prodrug activation: Serum albumins (BSA or HSA) are shown to catalyze a reaction cascade that involves the ring-opening of an isoxazole ring followed by a ,-elimination reaction, as per the scheme. The 4-(aryloxymethyl)isoxazole derivative of estrone is selectively removed in vitro by albumins, thus demonstrating the potential of this new protective group. [source] Molecular recognition of sugars by lanthanide (III) complexes of a conjugate of N, N -bis[2-[bis[2-(1, 1-dimethylethoxy)-2-oxoethyl]amino]ethyl]glycine and phenylboronic acidCONTRAST MEDIA & MOLECULAR IMAGING, Issue 4 2007Elisa Battistini Abstract A novel conjugate of phenylboronic acid and an Ln(DTPA) derivative, in which the central acetate pendant arm was replaced by the methylamide of L -lysine, was synthesized and characterized. The results of a fit of variable 17O NMR data and a 1H NMRD profile show that the water residence lifetime of the Gd(III) complex (150,ns) is shorter than that of the parent compound Gd(DTPA)2, (303,ns). Furthermore, the data suggest that several water molecules in the second coordination sphere of Gd(III) contribute to the relaxivity of the conjugate. The Ln(III) complexes of this conjugate are highly suitable for molecular recognition of sugars. The interaction with various sugars was investigated by 11B NMR spectroscopy. Thanks to the thiourea function that links the phenylboronic acid targeting vector with the DTPA derivative, the interactions are stronger than that of phenylboronic acid itself. In particular, the interaction with N -propylfructosamine, a model for the glucose residue in glycated human serum albumin (HSA), is very strong. Unfortunately, the complex also shows a rather strong interaction with hexose-free HSA (KA,=,705,±,300). Copyright © 2007 John Wiley & Sons, Ltd. [source] Similarity of permeabilities for Ficoll, pullulan, charge-modified albumin and native albumin across the rat peritoneal membraneACTA PHYSIOLOGICA, Issue 4 2009D. Asgeirsson Abstract Aim:, Compared to neutral globular proteins, neutral polysaccharides, such as dextran, pullulan and Ficoll, appear hyperpermeable across the glomerular filtration barrier. This has been attributed to an increased flexibility and/or asymmetry of polysaccharides. The present study investigates whether polysaccharides are hyperpermeable also across the continuous capillaries in the rat peritoneum. Methods:, In anaesthetized Wistar rats, FITC,Ficoll or FITC,pullulan together with 125I-human serum albumin (RISA) or neutralized 125I-bovine serum albumin (nBSA) were given intravenously, after which peritoneal dialysis (PD) using conventional PD fluid (Gambrosol 1.5%) was performed for 120 min. Concentrations of FITC-polysaccharides and radioactive albumin species in plasma and dialysis fluid were analysed with high-performance size exclusion chromatography and a gamma counter respectively. Transperitoneal clearance values were calculated for polysaccharides in the molecular radius range 36,150 Ĺ, and for RISA and nBSA. Results:, Ficoll and pullulan showed more or less identical permeabilities, compared to RISA and nBSA, across the peritoneal membrane. Although RISA-clearance, 5.50 ± 0.28 (,L min,1; ±SEM), tended to be lower than the clearances of Ficoll36Ĺ (6.55 ± 0.25), pullulan36Ĺ (6.08 ± 0.22) and nBSA (6.56 ± 0.23), the difference was not statistically significant. This is in contrast to the hyperpermeability exhibited by polysaccharides across the glomerular filtration barrier and also contrasts with the charge selectivity of the latter. Conclusion:, The phenomenon of molecular flexibility is more important for a macromolecule's permeability through the glomerular filter than across the continuous peritoneal capillary endothelium. Furthermore, it seems that charge plays a subordinate role in the steady-state transport across the combined peritoneal capillary,interstitial barrier. [source] | ||||||||||||||||||||||||||||||||||