Serum albumin

About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.

Inflammation and Progression of CKD: The CRIC Study

Abstract: Background and objectives CKD is a global public health problem with significant mortality and morbidity. Design, setting, participants, & measurements We examined the multivariable association of plasma levels of IL-1, IL-1 receptor antagonist, IL-6, TNF- α , TGF- β , high–sensitivity C–reactive protein, fibrinogen, and serum albumin with progression of CKD in 3430 Chronic Renal Insufficiency Cohort study participants. Results Over a median follow-up time of 6.3 years, 899 participants reached the composite end point of ≥50% decline in eGFR from baseline or onset of ESRD. Elevated plasma levels of fibrinogen, IL-6, and TNF- α and lower serum albumin were associated with a greater decline in eGFR over time. After adjusting for demographics, BP, laboratory variables, medication use, and baseline eGFR, hazard ratios for the composite outcome were greater for the patients in the highest quartile of fibrinogen (hazard ratio, 2.05; 95% confidence interval, 1.64 to 2.55; P P α (hazard ratio, 1.94; 95% confidence interval, 1.52 to 2.47; P P P 0.001), serum albumin (hazard ratio, 1.52; 95% confidence interval, 1.24 to 1.87; P α (hazard ratio, 1.42; 95% confidence interval, 1.11 to 1.81; P Conclusions Elevated plasma levels of fibrinogen and TNF- α and decreased serum albumin are associated with rapid loss of kidney function in patients with CKD.

Albumin-deficient rat mutant

Abstract: An analbuminemic colony was established from Sprague-Dawley rats. Analbuminemia was inherited as an autosomal recessive trait. The rates of growth and reproduction of the mutant rats were no different from those of normal rats. Biochemically, the mutant was characterized by an extraordinarily low serum albumin content and a hyperlipidemia. Total serum protein in the mutant rat was similar to that of control Sprague-Dawley rats, with increased globulin. Serum cholesterol was inversely correlated with a decrease in albumin; the correlation coefficient for ablumin was --.92. These mutant rats may serve as a model of human familial analbuminemia and may also be useful in elucidating the functional roles of albumin.

Species Differences of Serum Albumins: I. Drug Binding Sites

Abstract: Purpose. The purpose of this study was the classification and identification of drug binding sites on albumins from several species in order to understand species differences of both drug binding properties and drug interaction on protein binding. Methods. Binding properties and types of drug-drug interaction on the different albumins were examined using typical site I binding drugs, warfarin (WF) and phenylbutazone (PBZ), and site II binding drugs, ibuprofen (IP) and diazepam (DZ) on human albumin. Equilibrium dialysis was carried out for two drugs and the free concentrations of drugs were then treated using the methods of Kragh-Hansen (Mol. Pharmacol. 34. 160−171, (1988)). Results. Binding affinities of site I drugs to bovine, rabbit and rat albumins were reasonably similar to human albumin. However, interestingly, those to dog albumin were considerably smaller than human albumin. On the other hand, binding parameters of DZ to bovine, rabbit and rat albumins were apparently different from those of human albumin. These differences are best explained by microenvironmental changes in the binding sites resulting from change of size and/or hydrophobicity of the binding pocket, rather than a variation in amino acid residues. Conclusions. We will propose herein that mammalian serum albumins used in this study contain specific drug binding sites: Rabbit and rat albumins contain a drug binding site, corresponding to site I on human albumin, and dog albumin contains a specific drug binding site corresponding to site II on the human albumin molecule.

Vitamin D binding protein (Gc-globulin).

Abstract: Introduction UNLIKE other hydrophobic hormone-binding systems in mammalian plasma, the binding protein for vitamin D and its metabolites circulates in remarkably higher titer (5 × 10−6 M) compared to its major circulating ligand 25-hydroxycholecalciferol (25-OHD3) (5 × 10−8 M), and displays a rapid turnover rate (1) (see Table 1). Initially characterized as group-specific component or Gc-globulin, its identity with the plasma vitamin D binding protein (DBP) was discovered in 1975 (2). This hepatic protein has a strong homology with serum albumin (ALB) and α-fetoprotein (AFP) (3, 4). Although many thousands of sera have been tested, deletion or gross alteration of the DBP gene has not been detected, lending support to the notion that such mutations might be lethal. Since analbuminemia and abnormalities of other plasma binding proteins do not appear to cause disease (5–7), DBP activities are presumably vital. In recent years, new observations on the structure, origin, associations, and activities of DBP hav...