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PubMed1992

High-affinity binding of warfarin, salicylate and diazepam to natural mutants of human serum albumin modified in the C-terminal end.

High-affinity binding of warfarin, salicylate and diazepam to four natural mutants of human serum albumin was studied by equilibrium dialysis at pH 7.4. The mutants Alb Milano Fast and Alb Vanves possess single amino acid substitutions close to the C-terminus, namely 573 Lys-->Glu and 574 Lys-->Asn, respectively. By contrast, Alb Catania and Alb Venezia are chain termination mutants in which several amino acids have been changed or deleted. Binding of warfarin to the variants was lower than binding to normal (wild-type) albumin (Alb A). The association constants were 73% (Alb Milano Fast, Alb Vanves and Alb Catania) or 67% (Alb Venezia) of that determined for Alb A. The results obtained with salicylate were more dependent on the type of mutation. The constants were either comparable to the normal value (Alb Catania) or reduced to 64% (Alb Milano Fast), 71% (Alb Vanves) or 43% (Alb Venezia) of that value. Diazepam binding to the variants was normal, except for binding to Alb Venezia in which case the association constant was reduced to 76% of that calculated for Alb A. The results are in accordance with the view that warfarin, salicylate and diazepam bind to three different high-affinity sites. It is proposed that the sites for warfarin and salicylate are situated rather close to each other in domain II, and that these high-affinity sites are relatively susceptible to conformational changes of the protein. By contrast, the primary diazepam site is placed closer to, or within, domain III of albumin and seems to be less affected by conformational changes in the protein molecule.

Binding Sites↗
PubMed1999

Peritoneal fluid kinetics: comparison between polyglucose solution and albumin solution.

Polyglucose (PG) solution has been shown to be capable of inducing peritoneal ultrafiltration despite its hypo-osmolality. However, the mechanism of osmosis by PG is not clear. In this study, we compared the fluid kinetics of albumin (ALB) solution (thought to be an ideal solution that should induce ultrafiltration through colloid osmosis) and PG solution. A 4-hour dwell study with frequent sampling was conducted in Sprague-Dawley rats (six rats in each group). The study used 25 mL of dialysate buffer, 10% ALB dialysis solution, 15% ALB dialysis solution, 20% ALB dialysis solution, or 7.5% PG solution, with 131I albumin as an intraperitoneal volume marker. All solutions were prepared by adding ALB or PG to a base dialysis solution (without osmotic agent). The initial osmolality values of the five solutions were 250 mOsm/kg, 284 mOsm/kg, 300 mOsm/kg, 320 mOsm/kg, and 280 mOsm/kg, and the dialysate drainage volumes at 4 hours were 17.0 +/- 0.8 mL, 22.4 +/- 0.8 mL, 25.4 +/- 0.6 mL, 27.3 +/- 0.9 mL, and 26.3 +/- 0.6 mL (buffer, 10% ALB, 15% ALB, 20% ALB, and 7.5% PG groups, respectively). The higher initial osmolality in the ALB groups was partially due to the sodium content in the ALB powder. The intraperitoneal volume was decreasing in the 10% ALB group, rather stable in the 15% ALB group, but slowly increasing in the 20% ALB group. In the PG group, intraperitoneal volume decreased initially and then started to increase after 2 hours. This pattern was closely related to the increase in the dialysate osmolality (to higher than plasma level). At 4 hours, the dialysate osmolality was significantly higher (and higher than plasma level) in the PG group as compared to all the ALB groups. No differences in peritoneal fluid absorption rate were observed among the four treatment groups. In the 15% ALB and 20% ALB groups, the transcapillary ultrafiltration rate (Qu) was lower in the later part of the dwell than in the initial part of the dwell; in the PG group, the opposite pattern was observed. Our results suggest that the osmosis of albumin dialysis solution is different from the osmosis of polyglucose solution. Polyglucose solution induces net ultrafiltration only when the dialysate osmolality increase to higher than plasma level, suggesting that degradation of polyglucose may be important for effective ultrafiltration.

Albumins↗
PubMed2002

Albumin transcytosis in mesothelium.

Apparent permeability to albumin (P(alb)) was measured with (125)I-albumin in specimens of rabbit parietal pericardium from lumen to interstitium (L-I) and from interstitium to lumen (I-L). With albumin concentration (C(alb)) 0.5%, P(alb) (x 10(-5) cm/s) L-I at 37 degrees C was 0.172 +/- 0.019 SE; it decreased to 0.092 +/- 0.022 I-L at 37 degrees C, 0.089 +/- 0.021 L-I at 12 degrees C, and 0.084 +/- 0.018 I-L at 12 degrees C. These findings provide evidence for an active transport L-I, likely transcytosis. With C(alb) 2.5%, 0.05%, and 0.005%, P(alb) L-I at 37 degrees C was 0.188 +/- 0.023, 0.156 +/- 0.021, and 0.090 +/- 0.021, respectively; at 12 degrees C it was 0.089 +/- 0.017, 0.083 +/- 0.019, and 0.087 +/- 0.026, respectively. Hence, active albumin transport ceases with C(alb) 0.005%; P(alb) values I-L at 12 degrees C and with C(alb) 0.005% are similar and provide diffusional permeability. With physiological C(alb) (approximately 1%), active albumin flux was approximately 5 x 10(-4) micromol x h(-1) x cm(-2). Apparent permeability to FITC-dextran 70 (P(dx)) was also measured. P(dx) (x 10(-5) cm/s) L-I at 37 degrees C with C(alb) 0.5% was 0.095 +/- 0.018; it decreased to 0.026 +/- 0.004 I-L (37 degrees C, C(alb) 0.5%), 0.038 +/- 0.007 at 12 degrees C (L-I, C(alb) 0.5%), 0.030 +/- 0.009 with C(alb) 0.005% (L-I, 37 degrees C), and 0.032 +/- 0.011 with nocodazole (L-I, 37 degrees C, C(alb) 0.5%). These findings provide evidence for transcytosis and confirm conclusions drawn from P(alb). Vesicular liquid flow, computed from vesicular dextran flux (fluid-phase only), was approximately 3.5 microl x h(-1) x cm(-2). Transcytosis seems a relevant mechanism, removing protein and liquid from serous cavities.

Albumins↗
PubMed2004

S-nitrosoalbumin-mediated relaxation is enhanced by ascorbate and copper: effects in pregnancy and preeclampsia plasma.

S-nitrosoalbumin (SNO-Alb) is a major reservoir of releasable nitric oxide (NO) in plasma. In preeclampsia, a pregnancy-specific disorder associated with endothelial dysfunction, we previously found significant elevations in plasma SNO-Alb concentrations and decreased plasma ascorbate (Asc) levels. This increased SNO-Alb may result from low-plasma Asc if Asc, along with transition metals (eg, copper [Cu]) are necessary for release of NO from S-nitrosothiols. We propose that vasodilator effects of SNO-Alb, mediated by release of NO, are fully realized only when Asc/Cu availability is sufficient. Relaxation responses to SNO-Alb or the control reduced human serum albumin (SH-Alb), and responses to pooled plasma from normal or preeclamptic pregnancies were examined in isolated mouse arteries. Arteries preconstricted with phenylephrine were exposed to SNO-Alb or SH-Alb at physiologically relevant concentrations. When free Cu was added in excess (10 mumol/L), NO release was not dependent on Asc. However, when Cu was added at lower (physiological) levels, NO release was dependent on Asc. The addition of Asc and Cu to SNO-Alb stimulated vasodilatory responses in isolated arteries >90%, whereas no change in the SH-Alb (5%) response was observed. Preeclampsia plasma with higher levels of SNO-Alb caused arteries to relax 44.1+/-4.7%, whereas normal pregnancy plasma caused 11.9+/-4.2% relaxation (P=0.007). These data indicate that SNO-Alb alone or in plasma can act as a potent vasodilator, and that sufficient Asc/Cu promotes this action. We suggest that the higher circulating levels of SNO-Alb, in women with preeclampsia, reflect a deficiency in Asc/Cu-mediated release of NO from SNO-Alb.

Adult↗
PubMed1986

Renal plasma membrane receptors for certain modified serum albumins. Evidence for participation of a heparin receptor.

Binding of formaldehyde-treated (f-alb), reduced-carboxymethylated (ac-alb) or reduced-acetamidated (am-alb) bovine serum albumins to purified rat renal plasma membranes was studied. Radioiodinated f-alb or ac-alb bound to kidney membranes while am-alb neither bound significantly nor competed with f-alb binding to kidney membranes. The binding was specific, saturable and heat- and proteinase-sensitive. Competition studies showed that f-alb and ac-alb sites may be the same on these membranes. To determine the role played by charge in binding, competition experiments with polyanions were performed. Polyanions such as nucleic acid or glycosaminoglycans were effective competitors of f-alb binding to cell membranes. Heparin was especially inhibitory, being several-fold more so than chondroitin sulphate. Completely reduced and carboxymethylated albumin was a better competitor than its partially modified counterpart. Furthermore, f-alb was a significant competitor of [35S]heparin binding to kidney membranes. Also, partially purified heparin receptor demonstrated specific binding of 125I-f-alb. These data suggest that a heparin receptor is responsible for binding and internalization of intravenously injected f-alb. A Scatchard plot revealed two classes of receptors with dissociation constants of 3.2 X 10(-6) M and 4.7 X 10(-5) M.

Animals↗
PubMed2003

The role of advanced glycation end products in retinal microvascular leukostasis.

PURPOSE: A critical event in the pathogenesis of diabetic retinopathy is the inappropriate adherence of leukocytes to the retinal capillaries. Advanced glycation end-products (AGEs) are known to play a role in chronic inflammatory processes, and the authors postulated that these adducts may play a role in promoting pathogenic increases in proinflammatory pathways within the retinal microvasculature. METHODS: Retinal microvascular endothelial cells (RMECs) were treated with glycoaldehyde-modified albumin (AGE-Alb) or unmodified albumin (Alb). NFkappaB DNA binding was measured by electromobility shift assay (EMSA) and quantified with an ELISA: In addition, the effect of AGEs on leukocyte adhesion to endothelial cell monolayers was investigated. Further studies were performed in an attempt to confirm that this was AGE-induced adhesion by co-incubation of AGE-treated cells with soluble receptor for AGE (sRAGE). Parallel in vivo studies of nondiabetic mice assessed the effect of intraperitoneal delivery of AGE-Alb on ICAM-1 mRNA expression, NFkappaB DNA-binding activity, leukostasis, and blood-retinal barrier breakdown. RESULTS: Treatment with AGE-Alb significantly enhanced the DNA-binding activity of NFkappaB (P = 0.0045) in retinal endothelial cells (RMECs) and increased the adhesion of leukocytes to RMEC monolayers (P = 0.04). The latter was significantly reduced by co-incubation with sRAGE (P < 0.01). Mice infused with AGE-Alb demonstrated a 1.8-fold increase in ICAM-1 mRNA when compared with control animals (P < 0.001, n = 20) as early as 48 hours, and this response remained for 7 days of treatment. Quantification of retinal NFkappaB demonstrated a threefold increase with AGE-Alb infusion in comparison to control levels (AGE Alb versus Alb, 0.23 vs. 0.076, P < 0.001, n = 10 mice). AGE-Alb treatment of mice also caused a significant increase in leukostasis in the retina (AGE-Alb versus Alb, 6.89 vs. 2.53, n = 12, P < 0.05) and a statistically significant increase in breakdown of the blood-retinal barrier (AGE Alb versus Alb, 8.2 vs. 1.6 n = 10, P < 0.001). CONCLUSIONS: AGEs caused upregulation of NFkappaB in the retinal microvascular endothelium and an AGE-specific increase in leukocyte adhesion in vitro was also observed. In addition, increased leukocyte adherence in vivo was demonstrated that was accompanied by blood-retinal barrier dysfunction. These findings add further evidence to the thinking that AGEs may play an important role in the pathogenesis of diabetic retinopathy.

Animals↗
PubMed2006

The relationship between albumin, other plasma proteins and variables, and age in the acute phase response after liver resection in man.

A large series of plasma albumin (ALB, g/dl) and simultaneous blood and clinical measurements were prospectively performed on 92 liver resection patients, and processed to assess the correlations between ALB, other plasma proteins, additional variables and clinical events. The measurements were performed preoperatively and at postoperative day 1, 3 and 7 in all patients, and subsequently only in those who developed complications or died. In patients who recovered normally ALB was 4.3 +/- 0.4 g/dl (mean +/- SD) preoperatively, 3.7 +/- 0.7 at day 1 and 3, and 3.9 +/- 0.4 at day 7. In patients with complications its decrease was more prolonged. In non-survivors it was 3.4 +/- 0.4 preoperatively, 3.0 +/- 0.4 at day 1, and then decreased further. Regression analysis showed direct correlations between ALB and pseudo-cholinesterase (CHE, U/l, nv 5300-13000), cholesterol (CHOL, mg/dl), iron binding capacity (IBC, mg/dl), prothrombin activity (PA, % of standard reference) and fibrinogen, an inverse correlation with blood urea nitrogen (BUN, mg/dl) for any given creatinine level (CREAT, mg/dl), and weaker direct correlations with hematocrit, other variables and dose of exogenous albumin. An inverse relationship found between ALB and age (AGE, years) became postoperatively (POSTOP) also a function of outcome, showing larger age-related decreases in ALB associated with complications (COMPL: sepsis, liver insufficiency) or death (DEATH). Main overall correlations: CHE = 287.4(2.014)(ALB), r = 0.73; CHOL = 16.5(1.610)(ALB) (1.001)(ALKPH), r = 0.71; IBC = 68.6(1.391)(ALB), r = 0.64; PA = 13.8 + 16.0(ALB), r = 0.51; BUN = 21.3 + 20.2(CREAT) - 6.2(ALB), r = 0.91; ALB = 5.0-0.013(AGE) - {0.5 + 0.003(AGE)( COMPL ) + 0.012(AGE)( DEATH )}( POSTOP ), r = 0.74 [p < 0.001 for each regression and each coefficient; ALKPH = alkaline phosphatase, U/l, nv 98-279, independent determinant of CHOL; discontinuous variables in italics label the change in regression slope or intercept associated with the corresponding condition]. These results suggest that altered albumin synthesis (or altered synthesis unable to compensate for albumin loss, catabolism or redistribution) is an important determinant of hypoalbuminemia after hepatectomy. The correlations with age and postoperative outcome support the concept that hypoalbuminemia is a marker of pathophysiologic frailty associated with increasing age, and amplified by the challenges of postoperative illness.

Acute-Phase Reaction↗
PubMed1984

Effect of antigen charge on immune complex interaction with glomerular cells in culture.

The effect of antigen charge on immune complex (IC) interaction with glomerular cells was evaluated using cultured rabbit glomerular cells. Rat albumin (Alb) was modified to produce a cationic charge; isoelectric point (pI) 7.4-8.0; anionic charge, pI 4.0-4.2; or left unmodified, pI 6.2-6.4. I125-IC (100 micrograms Alb in complex) was incubated with cells for 44 hr. Cationic Alb IC (CAT IC) interaction was 7 and 10 times greater than unmodified (UM) and anionic (AN) IC, 7596 +/- 613 vs 1016 +/- 176 and 746 +/- 106 pg I125-Alb/micrograms cell protein, mean +/- SE (P less than 0.01). A 10-fold excess of unlabeled CAT Alb decreased CAT IC interaction (6342 +/- 432 vs 1246 +/- 296 pg I125-Alb/micrograms cell protein, P less than 0.01) increased UM IC (981 +/- 186 vs 3994 +/- 394 pg I125-Alb/micrograms cell protein, P less than 0.01), and had no effect on AN IC. A 10-fold excess unlabeled CAT IC increased interaction of both CAT IC (7067 +/- 514 vs 37,416 +/- 3026 pg I125-Alb/micrograms cell protein) and UM IC (994 +/- 123 vs 12,922 +/- 566 pg I125-Alb/micrograms cell protein) but not of AN IC. Incubation of cells with CAT, UM, or AN Alb followed by specific antibody demonstrated increased antibody interaction with cells exposed to CAT Alb (15,212 +/- 676 vs 3866 +/- 406 and 1785 +/- 206 pg I125-IgG/microgram cell protein for UM and AN Alb, respectively).

Albumins↗
PubMed2002

Measurement of hemoglobin and albumin adducts of naphthalene-1,2-oxide, 1,2-naphthoquinone and 1,4-naphthoquinone after administration of naphthalene to F344 rats.

Naphthalene-1,2-oxide (NPO), 1,2-naphthoquinone (1,2-NPQ) and 1,4-naphthoquinone (1,4-NPQ) are the major metabolites of naphthalene that are thought to be responsible for the cytotoxicity and genotoxicity of this chemical. We measured cysteinyl adducts of these metabolites in hemoglobin (Hb) and albumin (Alb) from F344 rats dosed with 100-800 mg naphthalene per kg body weight. The method employs cleavage and derivatization of these adducts by trifluoroacetic anhydride and methanesulfonic acid followed by gas chromatography-mass spectrometry in negative ion chemical ionization mode. Cysteinyl adducts of both proteins with NPO, and 1,2- and 1,4-NPQ (designated NPO-Hb and -Alb, 1,2-NPQ-Hb and -Alb, and 1,4-NPQ-Hb and -Alb, respectively) were produced in a dose-dependent manner. Of the two structural isomers resulting from NPO, levels of NPO1 adducts were greater than those of NPO2 adducts in both Hb and Alb, indicating that aromatic substitution is favored in vivo at positions 1 over 2. Of the quinone adducts, 1,2-NPQ-Hb and -Alb were produced in greater quantities than 1,4-NPQ-Hb and -Alb, indicating either that the formation of 1,2-NPQ from NPO is favored or that more than one pathway leads to the formation of 1,2-NPQ. The shapes of the dose-response curves were generally nonlinear at doses above 200 mg naphthalene per kg body weight. However, the nature of nonlinearity differed, showing evidence of supralinearity for NPO-Hb, NPQ-Hb and NPQ-Alb and of sublinearity for NPO-Alb. Low background levels of 1,2-NPQ-Hb and -Alb and 1,4-NPQ-Hb and -Alb were detected in control animals without known exposure to naphthalene. However, the corresponding NPO-Hb and -Alb adducts were not detected in control animals.

Acetylcysteine↗
PubMed1998

A new assay for albumin and hemoglobin adducts of 1,2- and 1,4-benzoquinones.

A new method has been developed to detect mono-S-substituted cysteinyl adducts of 1,2- and 1,4-benzoquinone (BQ) in hemoglobin (Hb) and albumin (Alb). After reacting the protein with trifluoroacetic anhydride and methanesulfonic acid, the resulting isomers of O,O',S-tris-trifluoroacetyl-hydroquinone and -catechol are extracted and detected by gas-chromatography-mass spectrometry in the negative-ion chemical ionization mode. The limit of detection of the assay is about 20 pmol adduct/g protein. This assay was employed to quantitate mono-S-substituted background adducts in human and rat Hb and Alb and benzene-specific adducts in Hb and Alb from F344 rats following a single oral dosage of 50-400 mg [13C6]benzene/kg body wt. In Alb, a dose-related increase in both [13C6]1,2- and [13C6]1,4-BQ adducts was observed with [[13C6]]1,4-BQ-Alb] >> [[13C6]1,2-BQ-Alb]. The formation of [13C6]1,2-BQ-Alb was linear with increasing dosage of benzene with a slope of 2.3 (pmol adduct/g protein)/(mg/kg body wt.) (S.E. = 0.18, R2 = 0.91). However, at dosages above about 100 mg [13C6]benzene/kg body wt., the levels of 1,4-BQ-Alb were greater than proportional to the dosage. Mono-S-substituted adducts of [13C6]1,2-BQ and [13C6]1,4-BQ were not detected in Hb. The background ([12C6]) adducts of 1,2- and 1,4-BQ in 20 F344 rats were estimated (in nmol adduct/g of protein) to be 3.9 (S.E. = 0.23) and 4.9 (S.E. = 0.30) in Hb and 2.7 (S.E. = 0.24) and 11.4 (S.E. = 0.60) in Alb. At the highest dosage of 400 mg [13C6]benzene/kg body wt., background levels of 1,2-BQ-Alb were about 4-fold higher than those of the benzene-specific adducts whereas the benzene-specific levels of 1,4-BQ-Alb were about 7-fold higher than those of the background adducts. Background levels of 1,2- and 1,4-BQ adducts in 10 portions of commercial human proteins were found to be (in nmol adduct/g of protein) 1.6 (S.E. = 0.05) and 0.85 (S.E. = 0.04) in Hb and 1.6 (S.E. = 0.06) and 8.9 (S.E. = 0.36) in Alb.

Acetic Anhydrides↗
PubMed1997

Purification and partial amino acid sequences of two distinct albumins from turtle plasma.

Two putative albumins, denoted Alb-1 (apparent molecular mass of 67 kDa) and Alb-2 (68 kDa), were purified from plasma of the emydid turtle (Trachemys scripta). Concentrations in serum or plasma were determined by radioimmunoassay using 125I-labeled Alb-1. In juvenile turtles (less than 2 years of age), serum concentrations of Alb-1 and Alb-2 were 2.72 +/- 0.23 mg/ml and 1.68 +/- 0.22 mg/ml, respectively, while concentrations in plasma pooled from adult turtles were 4.2 mg/ml and 2.6 mg/ml, respectively. The two albumins are immunologically distinct from one another as determined by both radioimmunoassay with 125I-labeled Alb-1 and Western blot analysis with antichicken albumin antiserum. Determination of the amino acid compositions of Alb-1 and Alb-2, and of albumin purified from plasma of the common snapping turtle (Chelydra serpentina), suggested that Alb-1 is more similar to albumins of other animals than is Alb-2. This was also indicated by Western blot analysis and by determining the N-terminal amino acid sequences of Alb-1 (40 residues) and Alb-2 (15 residues). Thus, it appears that two distinct forms of albumin are synthesized by T. scripta, possibly as a result of gene duplication and divergence.

Amino Acid Sequence↗
PubMed1994

Macromolecular permeability across the blood-nerve and blood-brain barriers.

The permeability of insulin (Ins), nerve growth factor (NGF), albumin (Alb), transferrin (Trf), and IgG across the blood-nerve barrier (BNB) and blood-brain barrier (BBB) in normal adult rats was quantified by measuring the (permeability coefficient x surface area) product (PS) with the i.v. bolus-injection technique in the cannulated brachial vein and artery using radioiodinated proteins. The PS values of the BNB for IgG and Alb were low: 0.079 +/- 0.029 x 10(-6) and 0.101 +/- 0.088 x 10(-6) ml.g-1.s-1, (mean +/- SD, respectively). The PS values for NGF and Trf were 16.1-fold and 25.5-fold higher than for Alb. The PS for Ins across the BNB was 33.190 +/- 2.053 x 10(-6) ml.g-1.s-1--a remarkable 329-fold increase compared with Alb. The PS values of the BBB for IgG and Alb in different brain regions were all low, from 0.028 +/- 0.017 to 0.151 +/- 0.035 x 10(-6) ml.g-1.s-1 (mean +/- SD). NGF and Trf had comparable PS values from 13- to 32-fold higher than for Alb, except for the brain stem, where the PS for Trf was 66-fold higher than for Alb. The mean PS for Ins across the BBB ranged from 15.78 +/- 5.45 x 10(-6) ml.g-1.s-1 for the cortex to 22.62 +/- 7.50 x 10(-6) ml.g-1.s-1 for the brain stem--again a remarkable 105- to 390-fold increase relative to Alb. Because reliable PS measurements were obtained for all proteins tested, the BBB and BNB cannot be considered impermeable to proteins--a concept that has plagued brain- and nerve-barrier research. The low PS values for IgG and Alb indicate low rates of transfer; however, Alb, in particular, is the major protein of endoneurial and ventricular fluid, which suggests that these PS values may be significant. Ins had the highest PS values, which likely reflect the mechanism of transport across the barriers--that is, receptor-mediated transport. Because NGF and Trf had PS values 13- to 66-fold higher than for Alb, whether this reflects receptor-mediated uptake, adsorptive-mediated transcytosis, or some other mechanism is unclear. That the PS values for NGF and Trf differ from Alb and IgG clearly suggests, however, a different uptake mechanism. Finally, the remarkably high PS values for Ins across the BBB and BNB identify this protein and its putative receptor on capillary endothelial cells as a potential target for drug delivery into the central and peripheral nervous systems.

Albumins↗
PubMed2003

Unilateral ureteroperitoneostomy in the management of hypoproteinemia in nephrotic rats with normal renal function.

Maintenance of serum albumin levels within normal limits is difficult to achieve in nephrotic children with normal renal functions who are unresponsive to specific treatment. One approach in such children is unilateral nephrectomy with rapid progression to renal failure. Peritoneal membrane is permeable to fluids, electrolytes and proteins, and peritoneal space has been used for total parenteral alimentation. Experimental ureteroperitoneostomy has been reported not to cause any significant side effect. The aim of this study was to evaluate the effects of unilateral ureteroperitoneostomy on serum and urine protein levels in rats with adriamycin-induced nephrosis. Adriamycin nephrosis was induced in 45 male Wistar rats. After two weeks, unilateral nephrectomy (Nx), unilateral ureteroperitoneostomy (Up) and sham operated (Sh) groups, each including 15 rats were formed. Serum creatine (S(Cr)) and albumin (S(alb)), and daily urinary protein excretion (U(pro)) were determined before adriamycin injection (week 0), before operations (week 2) and at the end of 6th week in all rats. In addition, percent change in serum albumin (deltaS(alb)) and urine protein levels (deltaU(pro)) between weeks 0-2, 0-6 and 2-6 were calculated for each group (e.g.; deltaS(alb) 0-2 = [S(alb) week 2-S(alb) week 0]/S(alb) week 0 x 100). Then, these parameters were compared within and between the groups. Furthermore, peritoneal tissue samples were obtained from the rats in Sh and Up groups to be examined for pathological changes. S(Cr) did not change within and in between the groups during the study period. S(alb) decreased significantly at weeks 2 and 6 with respect to week 0 in all three groups. In addition, although S(alb) tended to decrease at week 6 with respect to week 2 in all groups, this was significant only in Sh group. U(pro) increased significantly at weeks 2 and 6 with respect to week 0, and at week 6 with respect to week 2 in all groups. However, S(alb) and U(pro) were not different between the three groups at weeks 0.2 and 6. On the other hand, deltaS(alb) and deltaU(pro) were not different between Sh vs. Nx and Nx vs. Up rats, but deltaS(alb) 0-6, deltaS(alb) 2-6 and deltaU(pro) 0-6 were significantly lower in Up group compared to Sh group. Histopathological examination of peritoneal samples revealed significantly higher fibrosis score in Up group compared to Sh group. In conclusion, unilateral ureteroperitoneostomy may one important therapeutic selection in the treatment of intractable nephrotic syndrome. However, peritoneal fibrosis could be a concern for further use of peritoneum in case of end stage renal failure.

Albumins↗
PubMed2004

Glomerular permeability activity: prevalence and prognostic value in pediatric patients with idiopathic nephrotic syndrome.

BACKGROUND: A circulating factor that increases in vitro glomerular permeability to albumin (P alb ) has been isolated from patients with recurrence of focal segmental glomerulosclerosis in their renal allografts. The prevalence and prognostic significance of permeability activity has not been examined in children with idiopathic nephrotic syndrome (INS). METHODS: P alb activity level was determined in sera from 26 children with new-onset INS before the initiation of therapy by using an in vitro assay. Permeability factor was considered present if P alb was greater than 0.5. The following clinical and laboratory data for patients were tabulated: demographic information, serum albumin and cholesterol concentrations, calculated glomerular filtration rate, age at disease onset, response to corticosteroid treatment, and long-term outcome. RESULTS: Patients ranged in age from 2 to 18 years, and 19 patients (73%) were male. Mean P alb was 0.45 +/- 0.04 (SEM). P alb in patients with a steroid-responsive course (n = 17) did not differ from that of patients with steroid-resistant disease (n = 9). Percentages with P alb greater than 0.5 did not differ between patients with steroid-responsive and steroid-resistant disease (47% and 33%, respectively). P alb was determined after 41 +/- 5 months in 6 patients with steroid-responsive INS. These patients had normal serum creatinine concentrations, and 4 of 6 patients were in prolonged remission. P alb at the onset of INS before therapy was 0.51 +/- 0.09 (P alb > 0.5 in 2 patients) and was not changed at follow-up (P alb = 0.40 +/- 0.12; P alb > 0.5 in 2 patients). CONCLUSION: Permeability activity, defined as P alb greater than 0.5, is present in pretreatment serum samples from nearly half the children with INS. The presence of permeability activity does not predict clinical response to steroid treatment, renal histopathologic characteristics, or clinical outcome at up to 5 years of follow-up.

Adolescent↗
PubMed1999

Blood compatibility of surfaces with immobilized albumin-heparin conjugate and effect of endothelial cell seeding on platelet adhesion.

Endothelial cell (EC) seeding significantly improves the blood compatibility of artificial surfaces. Although a coating consisting of albumin and heparin (alb-hep) is a suitable substrate for seeded ECs, binding of ECs to the substrate further improves when small amounts of fibronectin are present in the alb-hep coating. Alb-hep conjugate was immobilized on carbon dioxide gas plasma-treated polystyrene (PS-CO(2)), thereby significantly increasing the recalcification time of blood plasma exposed to this surface. Furthermore, surface-immobilized alb-hep conjugate inhibited exogenous thrombin. Heparin activity was reduced by adding fibronectin on top of a monolayer of alb-hep conjugate, but not by simultaneous coating of fibronectin and alb-hep conjugate. Coating of PS-CO(2) with alb-hep conjugate significantly decreased contact activation (FXII activation). The number of platelets deposited from blood plasma on PS-CO(2) coated with alb-hep conjugate was twice as high as on PS-CO(2) coated with albumin. Addition of fibronectin to alb-hep conjugate-coated PS-CO(2) had no significant effect on the number of adhered platelets. Seeding of the substrates with ECs significantly reduced the number of adhered platelets under stationary conditions. Platelets deposited onto endothelialized surfaces were primarily found on endothelial cell edges, and sparingly on areas between ECs. In conclusion, alb-hep conjugate-coated surfaces display anticoagulant activity. ECs adhering to and proliferating on this coating significantly decrease the number of platelets which adhere to the surface. Therefore, alb-hep conjugate-coated surfaces form a suitable substrate for seeding of ECs in low density. Although application of fibronectin on top of the coating decreases the anticoagulant activity to some extent, it might be useful in view of the improved adherence of ECs to the coating.

Animals↗
PubMed1991

Correction of fructosamine value for serum albumin and globulin concentrations.

Using the data of 131 patients with non-insulin dependent diabetes mellitus (NIDDM), the correction formulas of fructosamine value ([FRA]) were devised to standardize the uncorrected [FRA] to serum albumin concentrations ([ALB]) of 4 g/dl, globulin concentrations ([GLB]) of 3 g/dl, and total protein concentrations ([TP]) of 7 g/dl. The following formula was derived for its maximum correlation coefficient (r) between corrected [FRA] ([FRAc]) and fasting blood glucose concentration ([G]); [FRAc] = [FRA]x33.3/(7.6 [ALB]+[GLB]). In these 131 diabetic patients, r between uncorrected [FRA] and [G] at 2 weeks ago was 0.562. When corrected by [FRA]x33.3/(7.6 [ALB]+[GLB]), [FRA]x4/[ALB], [FRA]+30 (4-[ALB]), [FRA]+23 (4-[ALB]), [FRA]+30 (7-[TP]), [FRA]x7/[TP], and [FRA]x3/[GLB], r was, respectively, 0.616, 0.612, 0.595, 0.589, 0.582, 0.581 and 0.478. In 24 patients with NIDDM whose [ALB] is either above 4.5 g/dl or below 3.5 g/dl, r between uncorrected [FRA] and [G] was as low as 0.389 without positive correlation. By using our correction formulas of [FRA]x33.3/(7.6 [ALB]+[GLB]) or [FRA] x 4/[ALB], r was statistically increased, respectively, to 0.769 or 0.788 (P less than 0.05 in both cases) in contrast to no significant increase of r by other formulas being at 0.598, 0.556, 0.540, 0.562 and 0.121. Based on these analyses, it is concluded that our correction formula of [FRA] by [FRAc]=[FRA]x33.3/(7.6 [ALB]+[GLB]) accurately reflects [G] in NIDDM even with hypo- or hyper-albuminemia, and [FRAc]=[FRA]x4/[ALB] is useful for practical application for its simplicity.

Diabetes Mellitus, Type 2↗
PubMed2004

Serum levels of calcium and albumin in survivors versus nonsurvivors after critical injury.

PURPOSE: Injured patients who require aggressive resuscitation with intravenous (IV) fluids and blood products will frequently acquire low levels of serum calcium (CA) and albumin (ALB) in the intensive care unit (ICU) as result of this therapy. The purpose of this longitudinal study was to determine the time course of CA and ALB during ICU admission in survivors (S) compared to nonsurvivors (N) after major trauma. The study design is to verify if CA, ALB, or albumin-corrected CA can be used as indicators of patient survivability after critical injury. MATERIALS AND METHODS: CA and ALB values were retrospectively recorded in 64 random subjects (S= 32 and N= 32) admitted to the Trauma ICU for 3 or more days. CA and ALB data points were partitioned into 6 time frames of ICU care. Mean values and standard error of the mean for each frame were obtained to depict parametric differences in the time profiles for S versus N. Subgroup analysis was used to determine the impact of blood transfusions on CA and ALB levels. Albumin-corrected CA was computed for every patient at each measurement point and then partitioned into the 6 time frames of ICU care. Parametric t-test and nonparametric rank sum analysis were used to evaluate the ability of CA, ALB, and ALB-corrected CA at discriminating S from N. Each predictive covariate was ranked, divided into quartiles (grades = normal, mild, moderate, severe), and correlated with patient survival likelihood (viz., ratio of S to N in each quartile). RESULTS: Parametric and non-parametric analysis of collected data indicates that the response patterns of CA were significantly different ( P<.00005 ) in S versus N. Time profiles of CA and ALB exhibited similar reductions in both S and N during the resuscitation phase (ie, "hypocalcemia of trauma"). But from these nadir points, CA response patterns in S tended to steadily elevate toward normal levels (ie, "responders"), while N exhibited no such increase in CA values (ie, "nonresponders"). Data revealed that survival likelihood in trauma patients after 3 ICU days is proportional to the upward response of CA from depressed values present after the initial resuscitation. Decreased CA levels after 3 ICU days were associated with decreased survival (Table 1). Rank sum testing showed that values of CA corrected for ALB creates less obvious difference in S and N than uncorrected CA. Subgroup analysis showed a linear decrease in CA and ALB levels with increasing units of blood transfused during treatment for trauma. CONCLUSIONS: CA changes during ICU care demonstrate distinct response patterns (P <.00005) for survivors versus nonsurvivors. The magnitude of upward response in CA after the fluid resuscitation phase is a marker that correlates with a patient's ability to withstand the physiologic stresses encountered during ICU treatment after major trauma. Our findings indicate that uncorrected CA values are a better guide for calcium replacement therapy in trauma patients than albumin-adjusted CA. This study suggests that response patterns of CA can be a useful reference to aid in monitoring the progress of critically injured patients.

Adult↗
PubMed1999

Protein adducts as dosimeters of human exposure to styrene, styrene-7,8-oxide, and benzene.

Cysteinyl adducts of hemoglobin (Hb) and albumin (Alb) formed via reactions with reactive species were measured in 48 subjects exposed to styrene (0.24-55.2 ppm) and to styrene-7,8-oxide (SO) (2.65-107 ppb) in a factory producing boats in the USA. Hb and Alb adducts were also investigated among 88 workers exposed to benzene (0-138 ppm) in several Chinese factories. The particular adducts were S-(2-hydroxy-1-phenylethyl) cysteine, from reactions of SO with Alb (designated SO-Alb), and S-phenylcysteine, from reactions of the CYP450 benzene metabolite, benzene oxide (BO), with Hb and Alb (designated BO-Hb and BO-Alb, respectively). The relationships between adduct levels and exposures were investigated in both studies. The estimated slopes varied considerably among the particular combinations of adduct and agent to which the workers were exposed, ranging from 0.815 pmol BO-Hb/g Hb per ppm benzene to 24400 pmol SO-Alb/g Alb per ppm SO. We used these estimated slopes, along with kinetic constants, to predict the systemic doses of SO and BO in humans per mg of styrene, SO or benzene per kg body weight, under certain assumptions. Using RX to signify the particular electrophile (SO or BO) the doses of RX to the blood per unit of dose varied between 2.21 and 4110 nM RX-h/mg agent per kg b.w. The dose of RX to the blood arising from inhalation of SO was almost 2000 times that of styrene (i.e. 4110 vs. 2.21 nM RX/mg agent per kg b.w.) and 430-781 times that of benzene (i.e. 4110 vs. 5.26-9.55 nM RX/mg agent per kg b.w.), depending upon the study. Comparable estimates of the blood dose of BO were obtained from adducts of Hb and Alb and two independent studies of BO-Alb yielded similar dose estimates. These results point to the utility of protein adducts as dosimeters of reactive electrophilic species in occupational studies. Finally, significant levels of background adducts of SO and BO with Hb and Alb were observed among workers, among control subjects and in commercial human proteins. Levels of these background adducts were too great to have arisen from non-occupational exposures to styrene or benzene or from cigarette smoking.

Air Pollutants↗