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PubMed2006

Inhibition of calcium oxalate crystallization by commercial human serum albumin and human urinary albumin isolated from two different race groups: evidence for possible molecular differences.

This study was undertaken to investigate the inhibitory activity of urine-derived (as opposed to serum-derived) albumin towards calcium oxalate crystallization and to compare the relative inhibitory strengths of this protein in subjects from South Africa's black and white population groups. Albumin was purified from the urines of 20 males in each race group using immunoaffinity chromatography. The purified proteins, as well as commercial human serum albumin were tested for their inhibition of calcium oxalate crystallization in ultra-filtered urines from both groups. Irrespective of its origin, albumin was found to be an inhibitor of calcium oxalate aggregation. Albumin derived from black subjects was superior to that from white subjects in this regard while urine-derived albumin was superior to that derived from serum. The composition of the urine in which the experiments were conducted influenced the inhibitory activity of the individual proteins. The different inhibitory activity of the proteins under identical conditions provides evidence that suggests molecular differences exist between them.

Albumins↗
PubMed1979

Immunochemistry of serum albumin. VI. A dynamic approach to the immunochemical cross reactions of proteins using serum albumins from various species as models.

Antisera against bovine serum albumin were raised in two rabbits. Serial bleedings were obtained at different times after the first immunization, and antisera from these serial bleedings were not mixed but were kept and studied separately. The immunochemical cross-reactions of these antisera with serum albumins from bovine, goat, sheep, porcine, horse, human and chicken were determined by immunoadsorbent studies. These were done by titration so that the values of maximum (plateau) binding by each albumin of radioiodinated antibodies were determined. In each rabbit, the immunochemical cross-reactivity was not static but increased progressievly with time after the first immunization. In the interval 7 days to 398 days the increases in cross-reaction were extremely large. pH dissociation studies revealed that, together with the increase in cross-reactivity of a given albumin with time after immunization, there was a restriction in the antibody heterogeneity towards populations possessing higher affinity. These results provide a rational explanation for the different values of cross-reactivities for a given albumin from different laboratories. The findings are analyzed in relation to the antigenic structure of albumin and their significance in evolutionary studies discussed.

Animals↗
PubMed1996

Complete structure of the human alpha-albumin gene, a new member of the serum albumin multigene family.

The nucleotide sequence of the human alpha-albumin gene, including 887 bp of the 5'-flanking region and 1311 bp of the 3-flanking region (24,454 in total), was determined from three overlapping lambda phage clones. The sequence spans 22,256 bp from the cap site to the polyadenylylation site, revealing a gene structure of 15 exons separated by 14 introns. The methionine initiation codon ATG is within exon 1; the termination codon TGA is within exon 14. Exon 15 is entirely untranslated and contains the polyadenylylation signal AATAAA. The deduced polypeptide chain is composed of a 21-amino-acid leader peptide, followed by 578 amino acids of the mature protein. There are seven repetitive DNA elements (Alu and Kpn) in the introns and 3-flanking region. The sizes of the 15 alpha-albumin exons match closely those of the albumin, alpha-fetoprotein, and vitamin D-binding protein genes. The exons are symmetrically placed within the three domains of the individual proteins, and they share a characteristic codon splitting pattern that is conserved among members of the gene family. The results provide strong evidence that alpha-albumin belongs to, and most likely completes with, the serum albumin gene family. Based on structural similarity, alpha-albumin appears to be most closely related to alpha-fetoprotein. The complete structure of this family of four tandemly linked genes provides a well-characterized approximately 200 kb locus in the 4q subcentromeric region of the human genome.

Albumins↗
PubMed1961

The immune response of rabbits tolerant to bovine serum albumin to the injection of other heterologous serum albumins.

Immunological tolerance produced in rabbits by neonatal injections of BSA can be terminated by a series of injections of certain heterologous serum albumins which cross-react with BSA. Injections of albumins distantly related to BSA were more effective in terminating the tolerant state than injections of albumins closely related to BSA. It was concluded from results obtained with several heterologous albumins that immunological tolerance to BSA is directed to both the over-all antigenic or physical-chemical composition of the protein and the individual determinant groups present on the protein. Several possible mechanisms were given to explain the ability of cross-reacting albumins to terminate the tolerant state of BSA-tolerant rabbits. A possible relationship between the termination of tolerance in BSA-tolerant rabbits injected with cross-reacting albumins and autoimmunily was discussed. It was also suggested that the relative ease with which tolerance could be established to heterologous serum proteins in comparison to bacterial antigens is the result of the close serological and physical-chemical relationship of the heterologous serum proteins to the serum proteins of the rabbit. Rabbits injected with 500 mg of BSA during the first 5 days of life failed to form antibody capable of either eliciting an immune elimination of an injection of I* BSA given 3 to 4 months later or complexing with the circulating I* BSA.

Animals↗
PubMed1992

Colloid solutions in the critically ill. A randomised comparison of albumin and polygeline 2. Serum albumin concentration and incidences of pulmonary oedema and acute renal failure.

All patients admitted to an Intensive Care Unit were assigned randomly to one of two groups, A and B. Group A received colloid volume replacement as 4.5% albumin whilst group B received a synthetic colloid, polygeline. This study describes the changes in serum albumin concentration in survivors and nonsurvivors in the two groups during their stay in the Intensive Care Unit. The incidences of renal failure and pulmonary oedema were also assessed. Serum albumin concentration decreased in all nonsurvivors. In survivors the serum albumin concentration decreased to a greater extent in the synthetic colloid group than in the albumin group. Despite the differences in serum albumin concentration there were no significant differences between the groups in the incidences of pulmonary oedema or renal failure.

Acute Kidney Injury↗
PubMed1991

Effects of serum-isolated vs synthetic bilirubin-albumin complexes on dye-binding methods for estimating serum albumin.

Bush and Reed reported (Clin Chem 1987;33:821-3) that the reaction of albumin with bromcresol purple but not with bromcresol green underestimated the concentration of albumin in synthetically obtained bilirubin-albumin (Bd) by 29%. Their unproven assumption was that chemically synthesized Bd behaved in a manner indistinguishable from the natural Bd in icteric serum. Here we verify that Bd, whether synthetically obtained or isolated from serum, causes an underestimation of albumin in the bromcresol purple but not in the bromcresol green method. The molar ratio of Bd from either source to underestimated albumin approximates 1.0, suggesting that one molecule of Bd would react equivalently to a molecule of albumin in the bromcresol purple method. This underestimation might falsely suggest hypoalbuminemia in patients with increased serum Bd.

Adult↗
PubMed1978

[The behavior of albumin in acute and chronic liver damage. III. Intrahepatic and serum albumin concentrations in human liver diseases].

In 305 patients examined by liver biopsy albumin and the entire soluble protein in the liver puncture as well as albumin in the serum were estimated quantitatively. A significant decrease of the serum albumin level in active cirrhoses and biliary liver damages confirmed the importance of the hypalbuminaemia as facultative symptom of a liver damage. The lacking specifity was emphasized by the low albumin serum concentrations in malignomas and after the intake of contraceptive hormones. The hypalbuminaemia and the increased content of soluble liver protein in the bioptic material might enrich the diagnostics of the activity in cirrhoses. The diagnostic value of the decrease of the relative proportion of albumin is low, since of all liver diseases examined the active cirrhosis alone was accompanied by a significant decrease. The estimation of the albumin content in the bioptically got liver tissue had in contrast to the animal experiment no diagnostic value for liver diseases.

Albumins↗
PubMed1980

Coordinate secretion of mouse alphafetoprotein, mouse albumin and rat albumin by mouse hepatoma-rat hepatoma hybrid cells.

Mouse heptoma cells that secrete large amounts of alpha-fetoprotein (AFP) and albumin have been crossed with rat hepatoma cells that secret only albumin, and in relatively small amounts, to investigate the influence of each parental genome upon the expression of serum proteins. All of the ten independent hybrid clones examined produce mouse AFP and both mouse and rat albumin; none produces rat AFP. The absence of production of rat AFP by the hybrids suggests that different mechanisms are involved in the initiation and in the maintenance of expression of this function. The secretion of the three proteins by the hybrid cells is coordinate: Whatever the growth phase (exponential or stationary) and irrespective of the amounts produced over a wide range, the ratio secreted of mouse AFP to mouse albumin is near to one, and that of mouse albumin to rat albumin is near to five. In addition, even though the pattern of protein secretion during the growth cycle of hybrid cells is different from those of both parents, the products of both parental genomes conform to the new hybrid pattern. Finally, some hybrids secrete less of the proteins with increasing numbers of cell generations, yet all three continue to be secreted in coordinate fashion. Since the rates of secretion of serum proteins probably reflect their rates of synthesis, we conclude that coordinate secretion indicates coordinate synthesis, and may reflect coordinate transcription of the relevant genes.

Albumins↗
PubMed1993

Antibodies specific for human albumin function as blocking antibodies when attached to erythrocyte-bound albumin.

Albumin is shown to be firmly bound to human red blood cells using the techniques of flow cytometry, immunoblotting, and complement fixation. The interactions between antibodies attached to the cell bound albumin and the complement system are examined. Antibodies specific for human serum albumin bind to albumin on erythrocytes and activate both homologous and heterologous complement in the absence of hemolysis. Moreover, treatment of erythrocytes with anti-albumin antibodies renders the cells resistant to classical pathway mediated lysis initiated by a passive lysis system. Thus, erythrocyte-bound anti-albumin antibodies appear to function in a manner similar to "blocking" antibodies described in some bactericidal systems.

Antibodies↗
PubMed1990

Developmental changes in blood-nerve transfer of albumin and endoneurial albumin content in rat sciatic nerve.

The rate of entry of albumin into the endoneurial space and its content within that compartment during development were investigated by measuring the permeability coefficient-surface area product to 125I-albumin (PSA) of the blood-nerve interface (BNI), endoneurial residual plasma volume (Vp), blood-nerve interface index to albumin, and endoneurial water content in sciatic nerves of rats ranging in age from 1 to 24 weeks. There was a 30-fold reduction in PSA and a 4-fold decrease in Vp from 2 to 24 weeks, indicating that the endoneurial capillaries and perineurium become less permeable during development. On the other hand, the Alb-BNI index was relatively small at 1 week, increased to a peak value around 6-8 weeks, and then decreased to adult values by 13 weeks. The smaller Alb-BNI index in the neonatal period is consistent with endoneurial albumin being cleared across a permeable perineurium by epineurial lymphatics. Subsequently, as the perineurium becomes less permeable, endoneurial albumin content increases. It then decreases as the endoneurial capillary permeability also decreases. Additionally, metabolic clearance of albumin, especially during the first 2-3 weeks, by axons and glia to meet the nutritive requirements of rapid axonal growth and myelination could be partly responsible for a lower Alb-BNI index. It is suggested that in the developing nerve, the combination of epineurial lymphatics and a relatively permeable perineurium, together with axonal and glial uptake and protein catabolism aid in the clearance of plasma-derived osmolytes from the endoneurial space, and thus prevent the elevation of endoneurial hydrostatic pressure and onset of oedema that would have been seen in an adult nerve with a comparably permeable BNI.

Aging↗
PubMed1984

Albumin Redhill, a human albumin variant.

Albumin Redhill, a variant human albumin with the same C-terminal amino acid as albumin A but with arginine at the N-terminus has been isolated by chromatofocusing from the sera of an English family. Albumin Redhill appears to contain two sites of mutation in its protein chain and is probably a proalbumin. The ability of albumin Redhill to bind Ni(II) or Cu(II) ions is considerably less than that of albumin A.

Aged↗
PubMed1993

Inhibition of angiotensin-converting enzyme reduces urinary albumin excretion but not regional albumin clearance in experimental diabetes.

Albuminuria and increased regional albumin clearance are known to develop concomitantly in diabetes. The anti-proteinuric effect of angiotensin-converting enzyme inhibitor therapy is well established. We studied whether angiotensin-converting enzyme inhibitor therapy with perindoprilat in comparison with conventional antihypertensive treatment could influence the development of increased regional albumin clearance as well as albuminuria in experimental diabetes. Rats with streptozotocin-induced diabetes were randomized into a saline group (n = 7), a perindoprilat (1 mg/kg per day) group (n = 8), and a hydralazine (3 mg/kg per day) group (n = 6); six rats served as non-diabetic controls. After 6-8 weeks, blood pressure was equally reduced in the perindoprilat- and hydralazine-treated groups (P < 0.01). Twenty-four-hour urinary protein and albumin excretion were increased in diabetic rats compared to control rats (P < 0.001). Hydralazine did not reduce 24 h protein or albumin excretion, whereas perindoprilat treatment reduced both (P < 0.001) to levels comparable to those of control rats. Regional albumin clearance, assessed in the eye, ileum, lung, skeletal muscle and skin, was clearly elevated in diabetic rats compared to control rats; however, neither drug therapy had an effect on albumin clearance.

Albumins↗
PubMed1993

Albumin levels in pregnancy: a hypothesis--decreased levels of albumin are related to increased levels of alpha-fetoprotein.

Serum albumin levels decrease during pregnancy while the concentration of most other maternal serum proteins of hepatic origin remain stable or increase. In a study of 289 women, most maternal characteristics such as race, age, smoking, a history of previous low birth-weight, infant sex and gestational age at delivery were not related to maternal serum albumin levels at 18 or 30 weeks' gestational age. The degree of maternal obesity significantly correlated with the concentration of albumin. There was a significant negative correlation in individual women between maternal serum levels of albumin and alpha-fetoprotein, with high levels of maternal serum alpha-fetoprotein predicting lower levels of albumin. We hypothesize that there may be a negative feedback effect of alpha-fetoprotein of fetal origin on the maternal production of albumin during pregnancy.

Body Mass Index↗
PubMed2003

Urinary albumin to osmolality ratio predicts 24-hour urine albumin excretion in diabetes mellitus.

BACKGROUND: Urinary albumin to creatinine ratio (ACR) in a single urine sample has been proposed to provide an estimate of microalbuminuria by adjusting for variability in urine concentrations. We hypothesized that adjusting the urine albumin concentration of single-void specimens for actual urine osmolality (urinary albumin to osmolality ratio [AOR]) may provide a more accurate estimate of 24-hour urine albumin excretion rates (AERs). METHODS: Patients with diabetes mellitus (DM; n = 136) had urinary concentrations of albumin, glucose, and creatinine and osmolality measured on single-void samples, and albumin levels, on 24-hour samples. Microalbuminuria is defined as an AER between 30 and 300 mg/d. RESULTS: Correlation between AOR on single-void samples and AER on 24-hour samples (r = 0.87; P < 0.001) was similar to that between ACR and AER (r = 0.88; P < 0.001). Using a cutoff value of 18.4 mg/kg/mOsm x 10(2) (18.4 mg/mmol x 10(2)) for AOR resulted in a sensitivity and specificity of 82% and 86% in detecting microalbuminuria, respectively. The area under the curve (AUC) for AOR was 0.89. Using a cutoff value of 15.0 mg/g (1.7 mg/mmol) for ACR resulted in a sensitivity and specificity of 85% and 85% in detecting microalbuminuria, respectively. The AUC for ACR was 0.90. The ability of AOR to predict AER was maintained at varying degrees of glycosuria (glucose < 100 mg/dL [<5.5 mmol/L]; r = 0.77; 100 to 750 mg/dL [5.5 to 42 mmol/L]; r = 0.85; and >750 mg/dL [>42 mmol/L]; r = 0.92). CONCLUSION: Urinary AOR correlates closely with 24-hour microalbuminuria determination, and the correlation is not appreciably affected by glycosuria. Thus, AOR can be used as an alternative test to ACR in the assessment of microalbuminuria in the population with DM.

Adolescent↗
PubMed1996

Targeting of drug to the hepatocytes by fatty acids. Influence of the carrier (albumin or galactosylated albumin) on the fate of the fatty acids and their analogs.

PURPOSE: The aim of this study was to evaluate the potential of fatty acids as shuttles to deliver xenobiotic inside the hepatocytes as well as to study the mechanism of incorporation into isolated hepatocytes when bound to native albumin or galactosylated albumin. Theoretically, they can enter into the hepatocytes after recognition of the Fatty Acid Binding Protein (FABPPM), or remain bound to galactosylated proteins and enter into these cells by a process known as receptor mediated endocytosis after selective recognition of the asialoglycoprotein receptor (ASGPR). METHODS: We synthesized a 3H-benzoyl adduct of lauric acid (BLA) (benzoyl adduct chosen to mimic any low molecular weight drug or contrast agent), and compared the behavior of BLA with oleic acid for their binding properties to carrier-proteins and the uptake mechanism by isolated hepatocytes. RESULTS: No significant difference was found in the binding properties of BLA for albumin and galactosylated albumin. The incorporation into the hepatocytes was found essentially depending on the FABPPM transport system whenever BLA was bound to albumin or to galactosylated albumin in the incubation medium: indeed, the transport was inhibited by phloretin (inhibitor of sodium dependent transport), increased when the free part of BLA was higher, and BLA was recovered in the cytosolic fraction of the hepatocytes. CONCLUSIONS: This study showed the convenience in using fatty acids as drug carriers possessing tropism for the hepatocytes.

Albumins↗
PubMed1985

Comparison of kinetic study of the photochemical changes of (ZZ)-bilirubin IX alpha bound to human serum albumin with that bound to rat serum albumin.

It has been stated by McDonagh, Palma & Lightner [(1982) J. Am. Chem. Soc. 104, 6867-6871] that complexing of bilirubin with serum albumin has a marked species-dependent influence on bilirubin photoisomerization in vitro and in vivo. Therefore the kinetics for the quantitatively important reaction: (Formula: see text) of the photochemical interconversion between bilirubin and its photoisomers bound to human or rat serum albumin in aqueous solution, assayed by h.p.l.c., was used to elucidate the observed species-dependent difference. The relative rate constants for bilirubin bound to human serum albumin, except for k4, the rate of interconversion from (ZZ)-bilirubin into (EZ)-bilirubin, proved to be considerably larger than those for bilirubin bound to rat serum albumin. In accordance with these rate constants, the formation of photoisomers of bilirubin bound to human serum albumin, except for (EZ)-bilirubin, is very rapid and much greater than that for bilirubin bound to rat serum albumin.

Animals↗
PubMed1975

Brdicka currents observed with bovine serum albumin and completely reduced bovine serum albumin in the presence of urea.

In ammonia buffers of varying composition and pH, native bovine serum albumin and completely reduced bovine serum albumin, denoted by p(SH)35, yield quite different Brdicka current-voltage (i-E) curves, but they are identical in the presence of 5 mM calcium chloride. This means that in the presence of calcium, bovine serum albumin becomes completely reduced to p(SH)35. In 8 M urea and ammonia buffers the Brdicka i-E patterns of serum albumin and p(SH)35 are identical even in the absence of calcium, the effect of calcium on the first wave being negligible while calcium slightly increases the second wave. The maximum polarographic effect is attained at urea concentrations of about 5-6 M. Quite generally, the appearance of a second Brdicka wave is attributed to complexation of Co(II) with S- and a group of ligands that is different on the second than on the first wave. The effect of calcium on Brdicka currents of bovine serum albumin in the absence of urea is attributed to an orientation of the protein on the surface of the electrode such that all disulfide groups are reduced and with other ligands can complex with Co(ii). Denaturation of bovine serum albumin in buffers with a pH less than 10.5, and which are 8 M in area, is (polarographically) completely reversible if dilution is made within 15 minutes after preparation. Changes in Brdlcka I-E patterns upon longer aging at varying pH are attributed-in part at least-to dimerization of the denatured protein by interaction of pS- in one molecule with -S-S-in another.

Ammonia↗
PubMed2005

Randomized trial of volume expansion with albumin or saline in children with severe malaria: preliminary evidence of albumin benefit.

BACKGROUND: Metabolic acidosis is the best predictor of death in children with severe falciparum malaria; however, its treatment presents a therapeutic dilemma, because acidosis and hypovolemia may coexist with coma, which can be associated with elevated intracranial pressure. We postulated that volume resuscitation with albumin might correct acidosis and hypovolemia with a lower risk of precipitating cerebral edema than crystalloid. In an open-label, randomized, controlled trial, we compared the safety of resuscitation with albumin to saline in Kenyan children with severe malaria. METHODS: We randomly assigned children with severe malaria and metabolic acidosis (base deficit, >8 mmol/L) to receive fluid resuscitation with either 4.5% albumin or normal saline. A control (maintenance only) group was only included for patients with a base deficit of <15 mmol/L. The primary outcome measure was the percentage reduction in base deficit at 8 h. Secondary end points included death, the requirement for rescue therapies, and neurological sequelae in survivors. RESULTS: Of 150 children recruited for the trial, 61 received saline, 56 received albumin, and 33 served as control subjects. There was no significant difference in the resolution of acidosis between the groups; however, the mortality rate was significantly lower among patients who received albumin (3.6% [2 of 56 patients]) than among those who received saline (18% [11 of 61]; relative risk, 5.5; 95% confidence interval, 1.2-24.8; P=.013). CONCLUSIONS: In high-risk children with severe malaria and acidosis, fluid resuscitation with albumin may reduce mortality. Our study design did not enable us to determine whether saline administration is preferable to fluid restriction or whether saline administration is actually hazardous. Further studies are needed to confirm our findings before definitive treatment recommendations can be made.

Acidosis↗