Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A refined sensor for CD4+ lymphocyte count was developed and evaluated by comparison to flow cytometry. The micropillar structured sensor surface was cast in PDMS polymer and surface modified to gain biocompatibility and CD4-cell capturing properties. The sensor works by pure capillary action and sample filling and rinsing is performed without external equipment. Whole blood samples showed acceptable agreement (79%) with flow cytometry, however when diluting the blood in PBS buffer we discovered that a larger number of cells were drawn into the sensor microchannel compared to the initial sample, explained by enhanced shear-induced cell migration. Using plasma or PBS with glycerol or albumin additives as diluting media greatly influenced this cell behavior, showing the importance of controlling the dilution media when working with devices based on capillary filling. The sensors need to be further tested with blood samples with lower CD4-counts (< 500 cells/microliters), which are clinically relevant.
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PMID:A PDMS-based disposable microfluidic sensor for CD4+ lymphocyte counting. 1854 75

Magnesium and its alloys are highly degradable metals that are potentially useful as biomaterials, especially in orthopaedic and cardiovascular applications. However, the in vivo corrosion has proved to be too high. Because of the complexity of in vivo conditions, a careful study of the corrosion of magnesium in synthetic solutions that simulate the in vivo environment is necessary as a first approach to predict the actual in vivo situation. The aim of this work was to evaluate the influence of the electrolyte composition on the corrosion behavior of magnesium and two Mg-alloys in synthetic biological media. Pure magnesium and its alloys (AZ31 and LAE442) were employed in the experiments. Electrochemical potentiodynamic polarization curves were recorded in sodium chloride and PBS electrolytes with different chloride ion and albumin concentration. Optical and SEM observations complemented by EDX analysis were made. The results showed that magnesium corrosion is localized in chloride- and albumin-containing buffer solutions. They also showed that the chloride concentration and the presence of buffer and protein strongly affect the electrochemical behavior of magnesium and magnesium alloys.
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PMID:Degradation of magnesium and its alloys: dependence on the composition of the synthetic biological media. 1856 9

Maghemite (gamma-Fe(2)O(3)) nanoparticles of 15.0 +/- 2.1 nm in diameter were prepared by nucleation, followed by controlled growth of magnetic iron oxide thin films onto gelatin nuclei. Functionalization of these magnetic nanoparticles with activated double bonds was accomplished by interacting divinyl sulfone with the gelatin coating of the gamma-Fe(2)O(3) nanoparticles. The activated double bonds were then used for covalent binding, via Michael addition reaction, of recombinant factor VIIa and human serum albumin to the surface of these nanoparticles. Recombinant factor VIIa was also physically bound to the magnetic nanoparticles by interacting this factor with the human serum albumin conjugated gamma-Fe(2)O(3) nanoparticles. The influence of factor VIIa concentration on the immobilization yield has been elucidated. Leakage of the bound factor VIIa into PBS containing 4% albumin was insignificant. The coagulant activity of the physically adsorbed recombinant factor VIIa was similar to that of the free one and was significantly better than that of the covalently bound. The blood half-life of free factor VIIa is short, about 2-3 h, because of digestion by proteolytic enzymes and inhibitory effects. Stabilization of factor VIIa against trypsin (a model proteolytic enzyme) and chloromethyl ketone-type inhibitor was accomplished by conjugation of the factor to the gamma-Fe(2)O(3) nanoparticles. This stabilization may extend the blood half-life of factor VIIa. Therefore, IV injection of factor VIIa conjugated gamma-Fe(2)O(3) nanoparticles instead of free factor may avoid the frequent dosing and reduce the cost of hemophilia treatment.
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PMID:Synthesis and characterization of recombinant factor VIIa-conjugated magnetic iron oxide nanoparticles for hemophilia treatment. 1910 92

The present investigation was aimed at exploring dendrimer-mediated solubilization and formulation development followed by in vitro, in vivo assessment of piroxicam (PXM) nanocomposite. For this, two dendrimer generations (3.0G and 4.0G) were synthesized and characterized by IR, (1)H NMR spectroscopic and electron microscopy techniques. The optimized formulations containing 0.2% w/v of PXM loaded PAMAM dendrimer at pH 7.4 referred to as 0.2-D(3)P(7.4) (3.0G) and 0.2-D(4)P(7.4) (4.0G) resulted in significant enhancements of PXM solubility approximately by 107- and 222-fold, respectively. The in vitro release behavior of PXM from the formulation in medium-I (PBS 7.4) and medium-II (PBS with 1% albumin) and stability studies were also favorable. Pharmacokinetic study showed higher area under curve (AUC(0-->t); microg/mL/h) of 293.78 +/- 2.04 and 321.54 +/- 2.37 with optimized 0.2-D(3)P(7.4) and 0.2-D(4)P(7.4) formulations, respectively, as opposed to 279.11 +/- 1.48 with plain PXM. The elimination half-life of the drug encapsulated in the formulation was significantly higher (0.2-D(3)P(7.4), 36.6 and 0.2-D(4)P(7.4), 41.1; h) than that of pure drug (33.7 h; p < 0.005), and the overall elimination rate constant of formulations was also less as compared to free drug (p < 0.005). Pharmacodynamic assessment by rat-paw model of 0.2-D(3)P(7.4) and 0.2-D(4)P(7.4) formulations displayed inhibition levels of 54.21 +/- 1.25% and 59.33 +/- 0.63%, respectively, which are higher than those of plain PXM (41.81 +/- 2.9) formulations, after the sixth hour of administration. The second, fourth and eighth hour organ distribution data showed significantly higher recovery of PXM in rat paw with dendrimer-based formulations in comparison to plain PXM. However, comparison of overall data suggested 4.0G-based formulations to be superior to 3.0G as well as pure PXM.
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PMID:Dendimer-mediated solubilization, formulation development and in vitro-in vivo assessment of piroxicam. 1923 41

CdSe and CdSe/CdS core/shell nanoparticles (NPs) were synthesized by using Gemini surfactant, 1,10-bis(alpha-hexadecyl pyridine) decamethylene dibromide (abbreviated Py-16-10-16), as a soft template. Subsequent analysis revealed that the as-synthesized CdSe NPs and CdSe/CdS core/shell NPs were highly luminescent with quantum yields of 18% and 35%, respectively, compared with Rhodamine 6G (95%). Furthermore, when the nanoparticles were conjugated with bovine serum albumin (BSA) in PBS buffer solution (pH 7.40), the fluorescence intensity of the BSA system was quenched by the addition of CdSe/TGA or CdSe/CdS/TGA NPs, while the fluorescence intensities of CdSe/TGA and CdSe/CdS/TGA NPs were enhanced by the addition of BSA. This enhancement and quenching of the fluorescence intensity by conjugating with BSA could be used to determine the albumin concentration.
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PMID:Controlled synthesis of CdSe and CdSe/CdS core/shell nanoparticles using Gemini surfactant Py-16-10-16 and their bioconjugates with BSA. 1939 33

C5L2 is a recently identified receptor for C5a/C5adesArg, C3a and C3adesArg (ASP). C5a/C5adesArg bind with high affinity, with no identified activation. By contrast, some studies demonstrate C3a/ASP binding/activation to C5L2; others do not. Our aim is to critically evaluate ASP/C3adesArg-C5L2 binding and bioactivity. Cell-associated fluorescent-ASP (Fl-ASP) binding to C5L2 increased from transiently transfected<stably transfected<Fl-ASP-sorted C5L2-HEK for both human C5L2 and mouse C5L2. Transfected C5L2-CHO cells had similar results. Endogenous C5L2 expression increased from 3T3-L1 preadipocytes<3T3-L1 adipocytes<primary mouse adipocytes. Non-transfected cells+/-Fl-ASP demonstrated background fluorescence only. In adherent C5L2-HEK (Fl-ASP sorted) and 3T3-L1 cells, blocking with 10% fetal calf serum, protamine sulfate or ovalbumin prevented (125)I-ASP non-specific binding (NSB, no cells), while albumin increased NSB. Binding to non-transfected HEK was comparable to NSB. Optimal specific binding was obtained at 20 degrees C (vs. 4 degrees C) in PBS or serum-free medium with K(d) 83.7+/-23.7 nM (C5L2-HEK), 66+/-15 nM (C5L2-CHO) and 76+/-14.3 nM (3T3-L1 preadipocytes); (125)I-C5a binding had greater affinity. Fl-ASP-C5L2 binding was comparable and concentration dependent (K(d) 31 nM (direct binding) and IC(50) 35 nM (competition binding) regardless of conditions). Recombinant ASP (rASP) produced in modified Escherichia coli Origami (DE3) (allowing folding and disulphide bridge formation), purified under non-denaturing conditions demonstrated 10x greater bioactivity vs. proteolytically derived plasma ASP for triglyceride synthesis and fatty acid uptake in 3T3-L1 adipocytes and preadipocytes while adipose tissue from C5L2 KO mice was non-responsive. rASP stimulation of adipocyte BODIPY-fatty acid uptake demonstrated EC(50) 115+/-93 nM and maximal stimulation of 413+/-33%, p<0.001. ASP binding has distinct characteristics that lead to C5L2 activation and increased bioactivity.
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PMID:Recombinant C3adesArg/acylation stimulating protein (ASP) is highly bioactive: a critical evaluation of C5L2 binding and 3T3-L1 adipocyte activation. 1976 7

Surface-induced thrombosis is a major complication in the development of blood-contacting medical devices. Serum albumin has the ability to bind to a wide variety of compounds, including drugs, and neither cells nor proteins adsorb to an albumin-coated surface. These properties of albumin are useful for improving the blood compatibility of biomaterial surfaces. In the present study, we prepared a water-insoluble film by cross-linking pharmaceutical grade recombinant human serum albumin aiming to the clinical applications, and loaded the film with a synthetic antiplatelet drug, cilostazol. The resultant film possessed native albumin characteristics such as drug binding ability and resistance to cell adhesion. Mouse fibroblast L929 cells did not adhere on the albumin film, just as they did not adhere on native albumin-coated surfaces. Furthermore, when the albumin film carrying cilostazol was placed in PBS containing Tween-80, the release of cilostazol was sustained over 144 h. The results indicate that the surface coating with thus prepared albumin film can confer the biomaterials with antithrombogenic surface by virtue of its non-adhesiveness to cells and its release of cilostazol.
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PMID:Drug-carrying albumin film for blood-contacting biomaterials. 2033 98

Curcumin (CCM), a yellow natural polyphenol extracted from turmeric (Curcuma longa), has potent anti-cancer properties as has been demonstrated in various human cancer cells. However, the widespread clinical application of this efficient agent in cancer and other diseases has been limited by its poor aqueous solubility and bioavailability. In this study, we prepared novel CCM-loaded human serum albumin (HSA) nanoparticles (CCM-HSA-NPs) for intravenous administration using albumin bound technology. Field emission scanning electron microscopy (FE-SEM) and dynamic light scattering (DLS) investigation confirmed a narrow size distribution in the 130-150nm range. Furthermore, CCM-HSA-NPs showed much greater water solubility (300-fold) than free CCM, and on storage, the biological activity of CCM-HSA-NPs was preserved with negligible activity loss. In vivo distributions and vascular endothelial cells transport studies demonstrated the superiority of CCM-HSA-NPs over CCM. Amounts of CCM in tumors after treatment with CCM-HSA-NPs were about 14 times higher at 1h after injection than that achieved by CCM. Furthermore, vascular endothelial cell binding of CCM increased 5.5-fold, and transport of CCM across a vascular endothelial cell monolayer by Transwell testing was 7.7-fold greater for CCM-HSA-NPs than CCM. Finally, in vivo antitumor tests revealed that CCM-HSA-NPs (10 or 20mg/kg) had a greater therapeutic effect (50% or 66% tumor growth inhibition vs. PBS-treated controls) than CCM (18% inhibition vs. controls) in tumor xenograft HCT116 models without inducing toxicity. We attribute this potent antitumor activity of CCM-HSA-NPs to enhanced water solubility, increased accumulation in tumors, and an ability to traverse vascular endothelial cell.
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PMID:Preparation and characterization of water-soluble albumin-bound curcumin nanoparticles with improved antitumor activity. 2103 30

We present a general approach for the selective imaging and killing of cancer cells using protein-activated near-infrared emitting and cytotoxic oxygen generating nanoparticles. Poly(propargyl acrylate) (PA) particles were surface modified through the copper-catalyzed azide/alkyne cycloaddition of azide-terminated indocyanine green (azICG), a near-infrared emitter, and poly(ethylene glycol) (azPEG) chains of various molecular weights. The placement of azICG onto the surface of the particles allowed for the chromophores to complex with bovine serum albumin when dispersed in PBS that resulted in an enhancement of the dye emission. In addition, the inclusion of azPEG with the chromophores onto the particle surface resulted in a synergistic ninefold enhancement of the fluorescence intensity, with azPEGs of increasing molecular weight amplifying the response. Human liver carcinoma cells (HepG2) overexpress albumin proteins and could be employed to activate the fluorescence of the nanoparticles. Preliminary PDT studies with HepG2 cells combined with the modified particles indicated that a minor exposure of 780 nm radiation resulted in a statistically significant reduction in cell growth.
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PMID:Selective imaging and killing of cancer cells with protein-activated near-infrared fluorescing nanoparticles. 2148 May 31

Four kinds of covalent serum albumin (BSA or HSA) conjugates of beta-tetrakis[(3,5-dicarboxy)phenoxy]-phthalocyaninatozinc (1) and beta-octakis [(3, 5-dicarboxy) phenoxy]-phthalocyaninatozinc (2) were synthesized by the approach of amide bond. The molar ratio of phthalocyanine to albumin in conjugates were found to be 6 - 7.1. Their absorption spectra were measured in PBS solution. When conjugated to albumin, compound 1 displays more distinct monomer absorption characteristics (with the maximum absorption at 677 nm) than its free form. Compound 2 in albumin framework exists mostly in monomer form, which is beneficial to photodynamic therapy in aqueous solution. Both 2-BSA and 2-HSA show a sharp and intense Q-band at 681 nm and 682 nm with the molar extinction coefficient of 2.01 x 10(5) and 2.05 x 10(5) mol(-1) L cm(-1) respectively. The Q-band absorption spectra and existent state of phthalocyanine 1 or 2 in conjugates were not affected by the pH value of aqueous solution, which are obviously different from that of the corresponding free phthalocyanine.
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PMID:[Synthesis and spectroscopic properties of covalent albumin conjugates of phthalocyanine zincs substituted with metadicarboxyphenoxyl groups]. 2180 May 92


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