Albumin concentration is diminished in patients with liver failure. Albumin infusion improves survival of cirrhotic patients with spontaneous bacterial peritonitis, and it is hypothesized that this may be due in part to its detoxifying capabilities. The aim of this study was to perform detailed quantitative and qualitative assessment of albumin function in patients with cirrhosis. Healthy controls and patients with acute deterioration of cirrhosis requiring hospital admission (n ؍ 34) were included. Albumin function was assessed using affinity of the fatty acid binding sites using a spin label (16 doxyl-stearate) titration and electron paramagnetic resonance spectroscopy and ischemia-modified albumin (IMA) was measured. Twenty-two patients developed acute-on-chronic liver failure. Twelve were treated with the Molecular Adsorbents Recirculating System (MARS) and 10 with standard medical therapy. For each parameter measured, the patients' albumin had reduced functional ability, which worsened with disease severity. Fifteen patients died, and IMA, expressed as an albumin ratio (IMAR), was significantly higher in nonsurvivors compared with survivors (P < 0.001; area under the receiver operating curve ؍ A lbumin is the major plasma protein and constitutes around 50% of the cell free protein in healthy individuals. It is produced exclusively in the liver, and therefore its concentration is reduced during hepatic dysfunction. 1 Following the Cochrane meta-analysis describing potential harmfully effect of albumin infusion in critically ill patients, there has been a reexamination of the use of albumin infusions for volume replacement. However, the results of the recently published SAFE study have provided new data confirming the safety of albumin infusion in critically ill patients. 2,3 Liver failure results in multiple organ dysfunction, and mortality rates without liver transplantation remain unacceptably high. 4 However, recovery is associated with complete reversal of multiorgan dysfunction. At present, in patients with cirrhosis, albumin is used mainly to replenish the circulating volume. With increasing severity of cirrhosis, there is a progressive increase in cardiac output, which is associated with a progressive reduction in individual organ blood flow. This peculiar circulatory disturbance is thought to occur as a result of splanchnic
Background:Proteins released by tumor cells can bind to serum albumin, leading to structural and functional modifications. We used electron spin resonance (ESR) spectroscopy to measure these changes in serum albumin and evaluate their utility for the diagnosis and monitoring of cancer. Methods: We used an ESR spectrometer and 16-doxyl stearic acid as spin probe to measure conformational changes in albumin in blood samples from a population of healthy donors and volunteers (n ؍ 349), patients with a wide variety of hematologic and nonhematologic malignancy (n ؍ 135), and patients with chronic diseases such as gastrointestinal and pulmonary disease, diabetes, and cirrhosis (n ؍ 91). We added differing amounts of 16-doxyl stearic acid spin probe in ethanol to 50 L of serum from each patient to create 3 different aliquots that differed in concentration of spin probe and ethanol, then incubated the aliquots for 10 min at 37°C with continuous shaking. We measured the ESR spectra of each aliquot in triplicate and used proprietary software (MedInnovation GmbH) to evaluate the ESR spectrum for differences between cancer patients and the other groups. Results: The diagnostic sensitivity and specificity of this test were 87.4% and 95.7%, respectively, for differentiating healthy individuals from cancer patients and 87.4%, and 85.7% for differentiating cancer patients
Human serum albumin accumulates low molecular weight biomarkers related to cancer. This accumulation can lead to allosteric modification of albumin and change its ability to bind essential fatty acids. Using 16-doxyl-stearic acid spin probe, which is specific for albumin, the serum samples of 98 patients with a variety of cancer types and 86 cancer free individuals were analysed by electron spin resonance (ESR) spectroscopy in order to evaluate cancer-induced modifications that occur to albumin. The ESR spectra showed significant differences between the investigated groups. These differences were most apparent in the intensities and widths of the spectral lines corresponding to the different types of albumin binding sites.
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