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albumin human [keywords]
- Gallium-68 Neomannosylated Human Serum Albumin-Based PET/CT Lymphoscintigraphy for Sentinel Lymph Node Mapping in Non-small Cell Lung Cancer. [JOURNAL ARTICLE]
- Ann Surg Oncol 2014 Aug 26.
To develop imaging of lymphatics with resolution greater than that of lymphoscintigraphy using technetium-99 m neomannosyl human serum albumin ((99m)Tc-MSA), we developed a Gallium-68 ((68)Ga) MSA for positron emission tomography (PET). This study is the first clinical trial to evaluate the feasibility of sentinel node detection using this novel (68)Ga tracer for the management of non-small cell lung cancer.We enrolled 34 patients (20 men, 14 women; mean age, 64.3 ± 10.4 years) who were candidates for lobectomy with mediastinal lymph node dissection for clinical stage I non-small cell lung cancer. (68)Ga-MSA was administered in one injection into the peritumoral region, and lymphoscintigraphy was performed by PET/CT just before surgery. All harvested lymph nodes were cut into 2 mm slices and were ultimately diagnosed using formalin-fixed and paraffin-embedded sections with hematoxylin and eosin staining.The sentinel nodes were well visualized by PET/CT imaging from 15 to 120 min, and especially within 60 min, after injection. In all patients (100 %), sentinel nodes could be identified on PET/CT. The number of sentinel nodes identified was 1.9 ± 0.9 (range 1-5) per patient. The maximum standardized uptake values were 2882.2 ± 2124.3 in the tumor and 82.5 ± 159.0 in the sentinel nodes. Eight of 34 patients (23.5 %) had metastases in 13 sentinel nodes. No false-negative sentinel nodes were detected in any of the eight patients with N1 or N2 disease (0 %).(68)Ga-MSA appears to be a promising tracer for sentinel node identification in non-small cell lung cancer.
- Human serum albumin adsorption onto octadecyldimethylsilyl-silica gradient surface. [JOURNAL ARTICLE]
- Colloids Surf B Biointerfaces 1994 Jun 30; 2(5):481-491.
The effects of long-range electrostatic repulsion and short-range hydrophobic attraction on human serum albumin adsorption were studied as a function of the surface density of octadecyldimethylsilyl chains (C18) on silica. A C18 surface density gradient was prepared on fused silica plates. The water contact angles increased smoothly from 12° to 105° in the 12.5 mm long gradient region. The maximal fractional surface coverage of the C18 chains was calculated to be 0.92. Fluorescein-5-isothiocyanate-labeled human serum albumin (FITC-HSA) adsorption from dilute buffer solution onto the C18 gradient surface was measured using spatially resolved total internal reflection fluorescence (TIRF) spectroscopy. FITC-HSA adsorbed progressively more onto the surfaces with higher hydrophobicity. When the fractional surface coverage of C18 chains was larger than 0.42 the adsorption saturation of FITC-HSA leveled off. The adsorption kinetics of FITC-HSA changed from a transport-limited process at moderate-to-high C18 surface coverages to an adsorption-limited process at lower C18 surface coverages. The kinetics of FITC-HSA adsorption, including the convective-diffusive transport of protein to the surface, were modeled as a simple binding process with a single forward and reverse rate. The apparent binding constant, derived from the initial forward and reverse binding rates, depended more strongly on the C18 surface coverage in 0.165 M buffer than in 0.025 M buffer.
- The Five-To-Six-Coordination Transition of Ferric Human Serum Heme-Albumin Is Allosterically-Modulated by Ibuprofen and Warfarin: A Combined XAS and MD Study. [Journal Article]
- PLoS One 2014; 9(8):e104231.
Human serum albumin (HSA) is involved physiologically in heme scavenging; in turn, heme-albumin (HSA-heme-Fe) displays globin-like properties. Here, the allosteric effect of ibuprofen and warfarin on the local atomic structure around the ferric heme-Fe (heme-Fe(III)) atom of HSA-heme-Fe (HSA-heme-Fe(III)) has been probed by Fe-K edge X-ray absorption spectroscopy (XAS). The quantitative analysis of the Fe-K edge extended X-ray absorption fine structure (EXAFS) signals and modeling of the near edge (XANES) spectral features demonstrated that warfarin and ibuprofen binding modify the local structure of the heme-Fe(III). Combined XAS data analysis and targeted molecular dynamics (MD) simulations provided atomic resolution insights of protein structural rearrangements required to accommodate the heme-Fe(III) upon ibuprofen and warfarin binding. In the absence of drugs, the heme-Fe(III) atom is penta-coordinated having distorted 4+1 configuration made by the nitrogen atoms of the porphyrin ring and the oxygen phenoxy atom of the Tyr161 residue. MD simulations show that ibuprofen and warfarin association to the secondary fatty acid (FA) binding site 2 (FA2) induces a reorientation of domain I of HSA-heme-Fe(III), this leads to the redirection of the His146 residue providing an additional bond to the heme-Fe(III) atom, providing the 5+1 configuration. The comparison of Fe-K edge XANES spectra calculated using MD structures with those obtained experimentally confirms the reliability of the proposed structural model. As a whole, combining XAS and MD simulations it has been possible to provide a reliable model of the heme-Fe(III) atom coordination state and to understand the complex allosteric transition occurring in HSA-heme-Fe(III) upon ibuprofen and warfarin binding.
- Binding of Doxyl Stearic Spin Labels to Human Serum Albumin. An EPR Study. [JOURNAL ARTICLE]
- J Phys Chem B 2014 Aug 25.
The binding of spin labeled fatty acids (SLFAs) to the human serum albumin (HSA) examined by electron paramagnetic resonance (EPR) spectroscopy was studied to evaluate the potential of the HSA/SLFA/EPR technique as a biomarking tool for cancer. A comparative study was performed on two spin labels with nitroxide groups attached at opposite ends of the fatty acid (FA) chain, 5-doxyl stearic (5-DS) and 16-doxyl stearic (16-DS) acid. The effects of incubation time, different [SLFA]:[HSA] molar ratios, ethanol, and temperature showed that the position of the nitroxide group produces certain differences in binding between the two SLFAs. Spectra for different [SLFA]:[HSA] molar ratios were decomposed into two spectral components, which correspond to the weakly and strongly bound SLFA. The reduction of SLFA with ascorbate showed the existence of two component process, fast and slow, confirming the decomposition results. Warfarin has no effect on the binding of the two SLFAs, whereas ibuprofen significantly decreases the binding of 5-DS, and has no effect on 16-DS. Together, the results of this study indicate that both SLFAs, 5-DS and 16-DS, should be used for the study of HSA conformational changes in blood induced by various medical conditions.
- Cobalt(II) complexes with the antimicrobial drug enrofloxacin: Structure, antimicrobial activity, DNA- and albumin-binding. [JOURNAL ARTICLE]
- Eur J Med Chem 2014 Aug 13.:189-201.
The cobalt(II) complexes with the quinolone antimicrobial agent enrofloxacin (Herx) in the presence of the nitrogen-donor heterocyclic ligands pyridine (py), 2,2'-bipyridylamine (bipyam), 1,10-phenanthroline (phen), 2,2'-bipyridine (bipy) or the oxygen-donor ligand N,N-dimethylformamide (DMF) were synthesized and characterized. The crystal structures of complexes [Co(erx)2(py)2]·MeOH·6H2O and [Co(erx)2(bipyam)]·4.5MeOH·1.25H2O were determined by X-ray crystallography. The deprotonated enrofloxacinato ligands are bidentately bound to cobalt(II) ion through the pyridone oxygen and a carboxylato oxygen. The antimicrobial activity of the complexes was tested against five different microorganisms (Escherichia coli XL1, Xanthomonas campestris ATCC33013, Staphylococcus aureus ATCC29213, Bacillus cereus ATCC11778 and Bacillus subtilis ATCC6633) and the complexes were more active than free Herx. The binding of the complexes to calf-thymus DNA (CT DNA) was monitored by spectroscopic techniques, viscosity measurements, cyclic voltammetry and by mobility shift experiments in agarose gel electrophoresis with CT DNA and plasmid DNA (pDNA). All complexes exhibited a preference for binding to the supercoiled structure of the pDNA. The ability of the complexes to displace ethidium bromide (EB) from the EB-DNA complex was also investigated. The experiments indicated intercalation as the most possible mode and the DNA-binding strength of the complexes were also calculated. The complexes bind to human or bovine serum albumin protein exhibiting relatively high binding constant values.
- Adsorbents for Apheresis Prepared from Polysaccharides of Algae that Threaten Ecosystem Services. [Journal Article]
- Chem Biodivers 2014 Aug; 11(8):1140-50.
In this work, we investigated whether materials isolated from algae that threaten ecosystems can be used for human benefit. We converted acidic polysaccharides (ulvan) from the alga Ulva pertusa into soft hydrogel materials. In addition to ulvan, the hydrogels also contained alginate in a polyion complex with chitosan. Cross-linking the hydrogel with glutaraldehyde reduced polysaccharide elution from the polyion complex gel. We also found that both ulvanchitosan and alginatechitosan gels were able to remove urea and heavy metals from aqueous solution. This is clinically significant, since during apheresis, toxic compounds such as urea have to be removed from the bloodstream of patients. Importantly, albumin was not removed by the hydrogels, implying that this vital protein can be returned to the bloodstream following dialysis.
- Donor Smoking Is Associated With Pulmonary Edema, Inflammation and Epithelial Dysfunction in Ex Vivo Human Donor Lungs. [JOURNAL ARTICLE]
- Am J Transplant 2014 Aug 21.
Although recipients of donor lungs from smokers have worse clinical outcomes, the underlying mechanisms are unknown. We tested the association between donor smoking and the degree of pulmonary edema (as estimated by lung weight), the rate of alveolar fluid clearance (AFC; measured by airspace instillation of 5% albumin) and biomarkers of lung epithelial injury and inflammation (bronchoalveolar lavage [BAL] surfactant protein-D (SP-D) and IL-8) in ex vivo lungs recovered from 298 organ donors. The extent of pulmonary edema was higher in current smokers (n = 127) compared to nonsmokers (median 408 g, interquartile range [IQR] 364-500 vs. 385 g, IQR 340-460, p = 0.009). Oxygenation at study enrollment was worse in current smokers versus nonsmokers (median PaO2 /FiO2 214 mm Hg, IQR 126-323 vs. 266 mm Hg, IQR 154-370, p = 0.02). Current smokers with the highest exposure (≥20 pack years) had significantly lower rates of AFC, suggesting that the effects of cigarette smoke on alveolar epithelial fluid transport function may be dose related. BAL IL-8 was significantly higher in smokers while SP-D was lower. These findings indicate that chronic exposure to cigarette smoke has important effects on inflammation, gas exchange, lung epithelial function and lung fluid balance in the organ donor that could influence lung function in the lung transplant recipient.
- The effect of cupric and ferric ions on antioxidant properties of human serum albumi. [JOURNAL ARTICLE]
- Gen Physiol Biophys 2014 Aug 22.
The interaction of both ferric (Fe3+) and cupric (Cu2+) ions with human serum albumin (HSA) was assayed at a temperature of 27°C in aqueous solution using isothermal titration calorimetry. The association equilibrium constant and the molar enthalpy for one binding is 1.7×10(5) M-1 and -31.37 kJ•M-1, respectively. To obtain the binding parameters of metal ion-protein interaction over the whole range of Fe3+ concentrations, the extended solvation model was applied. The solvation parameters obtained from this model were attributed to the structural change of HSA. The binding parameters obtained from the extended solvation model indicate that the stability of HSA was decreased as a result of its binding with ferric ions, which cause dampening the antioxidant property of HSA. Cuperic ion increases the stability of HSA considerably, indicating that the antioxidant property of human serum albumin are increased as a result of its interaction with cupric ion.
- The Cardiovascular Effect of the Uremic Solute Indole-3 Acetic Acid. [JOURNAL ARTICLE]
- J Am Soc Nephrol 2014 Aug 21.
In CKD, uremic solutes may induce endothelial dysfunction, inflammation, and oxidative stress, leading to increased cardiovascular risk. We investigated whether the uremic solute indole-3 acetic acid (IAA) predicts clinical outcomes in patients with CKD and has prooxidant and proinflammatory effects. We studied 120 patients with CKD. During the median study period of 966 days, 29 patients died and 35 experienced a major cardiovascular event. Kaplan-Meier analysis revealed that mortality and cardiovascular events were significantly higher in the higher IAA group (IAA>3.73 µM) than in the lower IAA group (IAA<3.73 µM). Multivariate Cox regression analysis demonstrated that serum IAA was a significant predictor of mortality and cardiovascular events after adjustments for age and sex; cholesterol, systolic BP, and smoking; C-reactive protein, phosphate, body mass index, and albumin; diastolic BP and history of cardiovascular disease; and uremic toxins p-cresyl sulfate and indoxyl sulfate. Notably, IAA level remained predictive of mortality when adjusted for CKD stage. IAA levels were positively correlated with markers of inflammation and oxidative stress: C-reactive protein and malondialdehyde, respectively. In cultured human endothelial cells, IAA activated an inflammatory nongenomic aryl hydrocarbon receptor (AhR)/p38MAPK/NF-κB pathway that induced the proinflammatory enzyme cyclooxygenase-2. Additionally, IAA increased production of endothelial reactive oxygen species. In conclusion, serum IAA may be an independent predictor of mortality and cardiovascular events in patients with CKD. In vitro, IAA induces endothelial inflammation and oxidative stress and activates an inflammatory AhR/p38MAPK/NF-κB pathway.
- Stable Isotope Labelling Method For The Investigation Of Protein Haptenation By Electrophilic Skin Sensitisers. [JOURNAL ARTICLE]
- Toxicol Sci 2014 Aug 21.
The risk of contact sensitisation is a major consideration in the development of new formulations for personal care products. However, developing a mechanistic approach for non-animal risk assessment requires further understanding of haptenation of skin proteins by sensitising chemicals, which is the molecular initiating event causative of skin sensitisation. The non-stoichiometric nature of protein haptenation results in relatively low levels of modification, often of low abundant proteins, presenting a major challenge for their assignment in complex biological matrices such as skin. Instrumental advances over the last few years have led to a considerable increase in sensitivity of mass spectrometry (MS) techniques. We have combined these advancements with a novel dual-labeling/LC-MS(E) approach to provide an in-depth direct comparison of human serum albumin (HSA) haptenation by 2,4-dichloro-1-nitrobenezene (DNCB), 5-chloro-2-methyl-4-isothiazolin-3-one (MCI), trans-cinnamaldehyde and 6-methyl coumarin. These data have revealed novel insights into the differences in protein haptenation between sensitisers with different reaction mechanisms and sensitising potency; the extreme sensitisers DNCB and MCI were shown to modify a greater number of nucleophilic sites than the moderate sensitiser cinnamaldehyde; and the weak/non-sensitiser 6-methyl coumarin was restricted to only a single nucleophilic residue within HSA. The evaluation of this dual labelling/LC-MS(E) approach using HSA as a model protein has also demonstrated that this strategy could be applied to studying global haptenation in complex mixtures of skin related proteins by different chemicals.