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PubMed1989

[Assessment of nutritional status--a part of routine clinical diagnosis: cholinesterase activity as a nutritional indicator].

Nutritional assessment has not yet been established as integral part of basic clinical diagnostic procedures everywhere, eventhough the prognostic relevance of malnutrition is well known. One of the reasons is the lack of nutritional indicators, which are specific of and sensitive for changes of the nutritional status on the one hand, and routinely analyzed on the other. We report on the utility of serum cholinesterase, which has the shortest half-life of all plasma proteins, to identify malnourished patients. 54 internal inpatients with malignant diseases or in septic state were followed up prospectively with respect to courses of cholinesterase (CHE), albumin (ALB), transferrin (TRA), and body weight over periods of 4 weeks. A correct correlation to malnutrition was defined as plasma concentrations less than reference ranges or continuous concentr. fall greater than 10%. Based on 132 observations (65 with continuous weight loss, mean: -5.5% of original w.; 54 w. gain, mean +4.6%, 13 constant w.), changes of CHE had the highest correlation to weight changes (r = 0.79, p less than 0.001), compared to the courses of TRA- or ALB-levels (r = 0.65/0.68). Incorrect positive results (conc. fall or conc. less than ref. range without weight loss): absolute levels - CHE 4%, ALB 4%, TRA 22%; conc. courses - CHE 0%, ALB 0%, TRA 6%. Incorrect negative: absolute c. - CHE 63%, ALB 30%, TRA 28%; courses - CHE 15%, ALB 19%, TRA 17%. The common determination of CHE and ALB-courses allowed a correct identification of malnutrition in 96% of all observations, with the same result as the courses of ALB + TRA.(ABSTRACT TRUNCATED AT 250 WORDS)

Body Weight↗
PubMed1997

Capillary and aortic endothelia interact in situ with nonenzymatically glycated albumin and develop specific alterations in early experimental diabetes.

Diabetic mice (6 weeks duration) were studied to assess the interaction of advanced glycation endproduct-modified albumin (AGE-Alb) with micro- and macrovascular endothelium, and to evaluate the alterations induced in the ultrastructure of the lung, kidney, and aorta. [125I]-AGE-Alb and AGE-Alb-Au were perfused in situ in the vasculature; the total uptake was quantitated by spectrometry, and the endothelial pathways of AGE-Alb-Au and the morphological alterations of the vascular beds were examined by electron microscopy. The results showed that [125I]-AGE-Alb (0.567 microM) was taken up specifically and saturably by all organs studied, and particularly by the lung. AGE-Alb-Au endocytosis and transcytosis occurred in the pulmonary and aortic endothelia, and were enhanced in diabetic animals. Also in diabetic animals, AGE-Alb-Au was detected throughout the kidney glomerular basement membrane (GBM) and within open filtration slits of podocytes, suggesting altered barrier function. The structural modifications progressed, and at the end of the experimental period, in the lung approximately 28% of the capillaries and approximately 25% of the alveoli became compressed or even collapsed, due to the hyperplasia of extracellular matrix and interstitial connective tissue. The presence of adherent intravascular macrophages suggests the development of an inflammatory immune process. The structural modifications observed in kidney glomeruli included thickening (approximately 30%) of the GBM and the disappearance of diaphragms between the cellular processes of podocytes. The aortic endothelium displayed luminal foldings, increased number (2.8-fold) of Weibel-Palade bodies, and proliferation of basal lamina. Together, the results show that in diabetes there is enhanced vascular uptake of AGE-Alb and significant pathomorphological changes of micro- and macrovessels.

Animals↗
PubMed2006

Chymase increases glomerular albumin permeability via protease-activated receptor-2.

Increased infiltration of the kidney by mast cells is associated with proteinuria, and interstitial fibrosis in various renal diseases. Mast cells produce serine proteases including tryptase and chymase (MCC) that act via protease-activated receptors (PARs) to induce synthesis of fibrogenic cytokines by renal cells. In the present study, we investigated direct effect of MCC and role of PARs on glomerular albumin permeability (P(alb)). Isolated rat glomeruli were incubated with MCC (0.1, 1, 10, and 100 ng/ml) for 5-30 min in presence or absence of PAR-1 and PAR-2 blocking antibodies. P(alb) was determined from the change in glomerular volume in response to an albumin oncotic gradient. The effect of direct activation of PARs on P(alb) was verified by incubating glomeruli with synthetic hexapeptide known to activate PAR-1 and PAR-2. MCC increased P(alb) of isolated rat glomeruli in a dose- and time-dependent manner. Blocking PAR-2 prevented MCC-mediated increase in P(alb). RT-PCR analysis of glomerular RNA demonstrated the presence of constitutively expressed PAR-1, -2, and -3 and low levels of PAR-4. In addition, direct activation of PAR-2 by hexapeptide SLIGKV increased P(alb) comparable to MCC, whereas PAR-1 activation by TFLLRN had no effect on P(alb). Our results document that MCC induces increase in P(alb) and that this effect is mediated through PAR-2. MCC may also play a role in renal scarring. We propose that inhibiting MCC activity or blocking the activation of PAR-2 may provide new targets for therapy in renal diseases.

Albumins↗
PubMed1988

A receptor for formaldehyde-treated serum albumin on human placental brush-border membrane.

Formaldehyde-treated serum albumin (f-Alb) is known to be taken up and degraded by sinusoidal liver cells via receptor-mediated endocytosis. We report that 125I-labeled f-Alb (125I-f-Alb) binding to human placental brush-border membranes also occurs. This binding reached equilibrium within 40 min at 37 degrees C. Kinetic studies demonstrated the presence of saturable binding with an apparent Kd of 2.1 micrograms of f-Alb/ml and a maximal binding of 2.3 micrograms/mg of membrane protein at pH 7.5. Maximal binding was observed at between pH 7.5 and 8.0. 125I-f-Alb binding to the membranes was little inhibited by a 1000-fold molar excess of ovalbumin, human apo-transferrin and native bovine serum albumin. No binding was observed with membranes which had been pretreated with proteinase or trypsin. This f-Alb receptor was extremely heat-stable, since the binding was not abolished even by pretreatment of the membranes at 78 degrees C for 30 min. EDTA, Ca2+ and Mg/4 had no effect on 125I-f-Alb binding, so the binding was independent of divalent cations. These data suggest that a receptor specific for f-Alb exists on human placental brush-border membranes of syncytial trophoblasts.

Cations, Divalent↗
PubMedDate not supplied

The coracoacromial ligament: morphology and study of acromial enthesopathy.

The coracoacromial ligament (CAL), normally a superior restraint against humeral translation, is frequently involved in rotator cuff impingement pathology. However, surgical excision of the CAL is not always clinically successful. Little anatomic information exists about the morphology and function of this ligament. The CAL and glenohumeral joint in 56 cadaveric shoulders were examined in 31 cadavers. Nineteen dimensional parameters were obtained by direct measurement. In 16 shoulders, specific attention was directed at the anterior band of the CAL. Variation exists in the morphology of the CAL. The most common configuration of the CAL was two distinct ligamentous bands that could be classified anatomically as an anterolateral band (ALB) and posteromedial band (PMB). The ALB commonly extended to the posterolateral aspect of the acromion. Furthermore, it frequently extended anterolaterally to the acromion, ending in a coracoacromial falx. Spur formation had occurred in 10 of 16 shoulders evaluated and always appeared in the ALB. Spur formation in the ALB correlated with a focal CAL that was narrower, less divergent, shorter, and thicker than a diffuse CAL that did not have a spur. The mean angle of diversion between the ALB and PMB, when a spur was present, was 31 degrees compared with 45 degrees when no spur was present. CAL band thickness varied, with the ALB being thicker at the acromion than at the coracoid and the PMB being thicker at the coracoid than at the acromion. During arthroscopic subacromial decompression, failure to visualize the anterolateral corner of the acromion adequately may result in incomplete resection of the CAL, especially if the PMB is mistaken to be the entire ligament. Incomplete removal of the CAL may be a factor in clinical failures of arthroscopic subacromial decompression. The preferential location of spurs in the ALB suggests that it is a major load-bearing structure. Furthermore, the ALB is thicker at the acromion, suggesting increased strain. Our data suggest that a possible function of the CAL is to dampen stress on the acromion from muscle activity.

Acromion↗
PubMed2004

Sera from patients with collapsing focal segmental glomerulosclerosis increase albumin permeability of isolated glomeruli.

The collapsing variant of focal segment glomerulosclerosis (FSGS) is characterized by heavy proteinuria and rapid progression to renal failure. Its cause is not known. We have characterized a substance in the circulation of patients with classic FSGS that increases in vitro permeability of glomeruli to albumin (P(alb)) and causes proteinuria when injected into rats. Inclusion of normal serum prevents the increase in P(alb) caused by this FSGS factor. We investigated the effect of sera from patients with collapsing FSGS on P(alb), as well as the effect of inclusion of normal serum. Isolated glomeruli were incubated with serum from each of 11 patients with collapsing FSGS (1:50 dilution) or with patient serum and an equal volume of pooled normal serum. P(alb) was determined on the basis of changes in glomerular volume in response to an oncotic gradient. Sera from 10 of the 11 patients with collapsing FSGS increased P(alb) of isolated glomeruli to a value of 0.5 or greater. In each of the 5 cases tested, inclusion of normal serum abolished the increase in P(alb). Sera of patients with collapsing FSGS increased glomerular P(alb). Our finding that the increase in P(alb) is abolished by normal serum suggests that the substance and its mechanism of action are similar or identical to the FSGS factor we have isolated from the plasma of patients with recurrent FSGS. The presence of a circulating factor in collapsing FSGS has implications for prognosis and treatment in primary and recurrent collapsing FSGS.

Adolescent↗
PubMed2003

Chronic ethanol consumption impairs receptor-mediated endocytosis of MAA-modified albumin by liver endothelial cells.

Alcoholic liver disease has been associated with abnormalities in receptor-mediated endocytosis (RME) which results in abnormal degradation of metabolically altered proteins. Model systems using formaldehyde-modified albumin (f-Alb) have shown an impairment in RME following chronic alcohol consumption utilizing both in situ perfused rat livers and isolated rat liver endothelial cells (LECs). The discovery that alcohol metabolite derived aldehydes can modify proteins prompted a study to determine if malondialdehyde-acetaldehyde-modified albumin (MAA-Alb) would be degraded similar to that reported for f-Alb, and whether ethanol-fed rats would demonstrate an impaired RME with respect to this ligand which occurs as a consequence of chronic ethanol consumption. MAA-Alb was degraded slightly more than f-Alb in both in situ perfused livers and at the single cell level. This degradation was completely inhibited with 100x unlabeled f-Alb, which suggests the use of a similar receptor. Following alcohol consumption there was a 50-60% decrease in MAA-Alb degradation in whole livers and isolated LECs. Utilizing isolated LECs it was determined that impairment in internalization was the most likely mechanism for the decrease in the amount of MAA-Alb that was degraded. These data show that chronic alcohol consumption by rats does in fact impair RME of alcohol metabolite-derived adducted proteins, and this impairment is due to a defect in the post-internalization step rather than the binding or degradation of the modified protein.

Acetaldehyde↗
PubMedDate not supplied

In vivo formation of (+)-anti-benzo[a]pyrene diol-epoxide-plasma albumin adducts in fish.

Benzo[a]pyrene (BaP), a procarcinogenic polycyclic aromatic hydrocarbon (PAH), is bioactivated to BaP diol-epoxides (BPDEs) that can form adducts with DNA and blood proteins. We report here for the first time the in vivo formation of adducts between BPDE and plasma albumin (Alb) from two fish species experimentally exposed to BaP. Brook trout (Salvelinus fontinalis) received either a single i.p. dose (10 mg/kg) or two separate i.p. doses (25 mg/kg; 7 days apart) of BaP, and blood was collected 2 (single exposure) or 3 (multiple exposure) days post-treatment. Arctic charr (Salvelinus alpinus) received 10 i.p. doses (3 mg/kg; a single dose every 6 days), and blood was collected 2 days after the second, sixth, and 10th injections. BPDE-Alb adducts were measured by an improved HPLC/fluorescence method developed to detect and quantify BaP-tetrols released after acid hydrolysis of adducted Alb. HPLC/fluorescence chromatograms of Alb from BaP-treated fish revealed only BaP-tetrol I-1, thus indicating the formation of adducts exclusively via the (+)-anti-BPDE metabolite. Levels of (+)-anti-BPDE-Alb adduct ranged from 0.68 to 19.6 ng of tetrol I-1 per gram of Alb. Notably, adduct level was not related to BaP dose and there was no accumulation of adducts with repeated exposure, which may indicate a very short half-life (< 2 days) of plasma Alb in fish. The data suggest that BPDE-Alb adducts in fish could be useful as a non-destructive biomarker of recent exposure to bioactivated BaP.

7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide↗
PubMed1999

Lower serum zinc in major depression in relation to changes in serum acute phase proteins.

There is now some evidence that major depression is accompanied by activation of the inflammatory response system (IRS). Other signs of IRS activation, which have been reported in major depression are lowered serum zinc (Zn) and serum albumin (Alb) concentrations. In serum, Zn is closely bound to Alb. The aims of the present study were to replicate previous findings that major depression is accompanied by lowered serum Zn and Alb and to examine whether the decrease in serum Zn may be explained by that in serum Alb. The above variables were determined in 48 major depressed patients and in 15 age-sex-matched healthy volunteers. Serum Zn and Alb were significantly lower in major depressed patients than in normal volunteers. In healthy volunteers and major depressed patients, there were significant and positive correlations between serum Zn and Alb. We found that 53.8% of the variance in serum Zn could be explained by the combined effects of serum Alb and diagnostic classification. The results suggest that lower serum Zn in depression is in part explained by lowered serum Alb and by another depression-related mechanism. It is suggested that lower serum Zn in depression may be secondary to sequestration of metallothionein in the liver, which may be related to increased production of interleukin-6.

Acute-Phase Proteins↗
PubMed1994

Modified high-affinity binding of Ni2+, Ca2+ and Zn2+ to natural mutants of human serum albumin and proalbumin.

High-affinity binding of radioactive Ni2+, Ca2+ and Zn2+ to six genetic albumin variants and to normal albumin isolated from the same heterozygote carriers was studied by equilibrium dialysis at pH 7.4. The three cations bind differently to albumin. Ni2+ binds to a site in the N-terminal region of the protein which is partially blocked by the presence of a propeptide as in proalbumin (proAlb) Varese (Arg-2-->His), proAlb Christchurch (Arg-1-->Gln) and proAlb Blenheim (Asp1-->Val) and by the presence of only an extra Arg residue (Arg-1) as in Arg-Alb and albumin (Alb) Redhill. The association constants are decreased by more than one order of magnitude in these cases, suggesting biological consequences for the ligand. The additional structural changes in Alb Redhill have no effect on Ni2+ binding. Finally, the modification of Alb Blenheim (Asp1-->Val) reduces the binding constant to 50%. Ca2+ binding is decreased to about 60-80% by the presence of a propeptide and the mutation Asp1-->Val. Arg-1 alone does not affect binding, whereas Alb Redhill binds Ca2+ more strongly than the normal protein (125%). In contrast with binding of Ni2+ and Ca2+, albumin shows heterogeneity with regard to binding of Zn2+, i.e. the number of high-affinity sites was calculated to be, on average, 0.43. The binding constant for Zn2+ is increased to 125% in the case of proAlb Varese, decreased to 50-60% for proAlb Christchurch and Alb Redhill but is normal for proAlb Blenheim, Alb Blenheim and Arg-Alb. The effects of the mutations on binding of Ca2+ and Zn2+ indicate that primary binding, when operative, is to as yet unidentified sites in domain I of the albumin molecule.

Amino Acid Sequence↗
PubMed2004

Plasma expansion by polyethylene-glycol-modified albumin.

Systemic inflammatory response conditions are associated with capillary leak and haemodynamic compromise. Fluid resuscitation to reverse the ensuing hypovolaemia is, however, complicated by the decreased endothelium reflection coefficient to albumin and other colloids. We developed PEG-Alb (albumin covalently linked to polyethylene glycol) as a potential resuscitative agent. PEG was covalently linked to human albumin at multiple sites on the protein. The modified protein was heterogeneous when examined by SDS/PAGE, size-exclusion chromatography and SELDI-TOF MS (surface-enhanced laser-desorption ionization-time of flight MS). Based on size-exclusion chromatography and osmotic pressure data, the effective volume of PEG-Alb is increased 13- to 16-fold compared with unmodified albumin. In an LPS (lipopolysaccharide) model of shock, rats treated with PEG-Alb showed better blood pressure, lower Hct (haematocrit) consistent with haemodilution and less lung injury than rats treated with unmodified albumin or saline. In a CLP (caecal ligation and puncture) model of sepsis, PEG-Alb was more effective than albumin or saline in maintaining blood pressure and in decreasing Hct. When fluorescein-labelled PEG-Alb and Texas Red-labelled albumin were administered to rats with LPS- or CLP-induced shock, PEG-Alb was retained within blood vessels, whereas albumin extravasates into the interstitial space. Based on these data, PEG-Alb appears to be retained within blood vessels in models of capillary leak. PEG-Alb may ultimately be effective in the clinical treatment of shock associated with capillary leak.

Albumins↗
PubMed1992

Increased permeability across the blood-nerve barrier of albumin glycated in vitro and in vivo from patients with diabetic polyneuropathy.

The blood-nerve transfer of human plasma albumin glycated with D-glucose was investigated by measuring the permeability coefficient-surface area product (PS) of the blood-nerve barrier to radioiodinated albumin in normal adult rat sciatic nerve. Human albumin (ALB) from normal individuals, freshly isolated by CM-Affi-Gel Blue affinity chromatography, was glycated in vitro for 1, 3, 10, 19, and 30 weeks. Glycated ALB (gALB) was separated from the nonglycated form by boronate-affinity chromatography. The efficiency of this separation was assessed by chromatography of ALB glycated with [14C]glucose and by rechromatography of isolated ALB and gALB after radioiodination. The gALB was also shown to have a higher molecular weight and be completely separated from ALB after SDS/pore gradient electrophoresis in a Tris borate/EDTA buffer. After 1 week of glycation, the gALB PS was 2.2-fold greater than the ALB PS (0.724 +/- 0.063 x 10(-6) vs. 0.328 +/- 0.053 x 10(-6) ml.g-1.s-1; mean +/- SD; P less than 0.0001) and it increased with the time of glycation reaching a maximum value of 16.2-fold greater at 30 weeks (4.656 +/- 1.117 x 10(-6) vs. 0.288 +/- 0.042 x 10(-6) ml.g-1.s-1; mean +/- SD; P less than 0.0001). No change was observed in the residual endoneurial plasma volume. In addition, the PS of gALB isolated from patients with diabetic polyneuropathy was significantly increased (P less than 0.0001) compared to the PS for ALB isolated from the same patients. It is hypothesized that the increased permeability of gALB and presumably other glycated serum components across the blood-nerve barrier, as well as the observed quantitative increase in ALB, IgG, and IgM in sural nerve biopsies from patients with diabetic polyneuropathy contribute to the development of diabetic polyneuropathy over a prolonged period of time by mechanisms that might involve osmotic changes in the nerve microenvironment, direct toxic effects of glycated macromolecules on cells within the endoneurium, or nerve damage by classical immunological mechanisms due to trapping of glycated immunoglobulins within nerve.

Animals↗
PubMed2001

Regulation of vascular endothelial growth factor expression by advanced glycation end products.

Advanced glycation end products (AGEs) are generated during long term diabetes and are correlated with the development of diabetic complications, such as retinopathy. Diabetic retinopathy is characterized by an increased retinal neovascularization due to the action of the angiogenic factor, vascular endothelial growth factor (VEGF). In this report, we show that injection of insulin and glycated albumin (Alb-AGE) to mice increases VEGF mRNA expression in eyes. Insulin and Alb-AGE stimulate VEGF mRNA and protein expression in retinal epithelial cells (ARPE-19). Alb-AGE-induced VEGF expression is not modulated by the use of antioxidants, N-acetyl-l-cysteine or pyrrolidinedithiocarbamate, or by an inhibitor of phosphatidylinositol 3-kinase (PI3K), wortmannin. However, using an inhibitor of ERK activation, U0126, we show that Alb-AGE stimulates VEGF expression through an ERK-dependent pathway. Accordingly, we found that Alb-AGE activated mitogen-activate protein kinase, ERK1/2, JNK1/2, but not p38, and that Alb-AGE did not activate PI3K and PKB. Moreover, Alb-AGE activated the transcription factor, hypoxia inducible factor-1 (HIF-1) DNA binding activity. This activation is mediated by an increase in accumulation of the HIF-1alpha protein through an ERK-dependent pathway. Thus, stimulation of VEGF expression by Alb-AGE, through the activation of HIF-1, could play an important role in the development of diabetic retinopathy.

Albumins↗
PubMed2004

Characterization of Aplysia enticin and temptin, two novel water-borne protein pheromones that act in concert with attractin to stimulate mate attraction.

Mate attraction in Aplysia involves a long-distance water-borne signal (attractin) that is released during egg laying. Other pheromones are predicted to be released during egg laying that act in concert with albumen gland attractin to stimulate attraction, but their identities are unknown. To identify other candidate water-borne pheromones, we employed differential library screening of an albumen gland cDNA library, Northern blot analysis, purification, characterization, cloning, and expression of albumen gland proteins, matrix-assisted laser desorption ionization mass spectrometry, pheromone secretion assays, behavioral bioassays, immunolocalization studies, and comparative genomics. Four genes, Alb-23, Alb-24, Alb-69, and Alb-172, were highly expressed in Aplysia californica albumen glands and encoded novel proteins. The products of the Alb-24 ("enticin") and Alb-172 ("temptin") precursors were soluble and highly abundant in albumen gland extracts, whereas Alb-23 and Alb-69 were membrane-associated proteins. A comparative analysis showed that the predicted Aplysia brasiliana enticin and temptin proteins were 90 and 91% identical, respectively, to their A. californica homologs. T-maze attraction bioassay studies have previously demonstrated that egg cordons alone are attractive to Aplysia but that attractin alone is not. In the present study, however, the combination of attractin, enticin, and temptin was found to be significantly attractive to potential mates and doubled the number of animals attracted to this stimulus compared with control animals. The combined data strongly suggest that enticin and temptin are novel candidate water-borne protein pheromones that act in concert with attractin to attract Aplysia to form and maintain egglaying and mating aggregations.

Amino Acid Sequence↗
PubMed2006

Nebulized drug admixtures: effect on aerosol characteristics and albuterol output.

Although not recommended, co-administration of drugs separately prescribed for nebulization is done in real life. The impact of this practice on drug output and aerosol characteristics is poorly understood. We studied the effect of drug admixtures (DA) on aerosol characteristics and drug output of nebulized albuterol delivered by a continuous output (CONT) and a breath enhanced nebulizer (BEN). Albuterol was nebulized alone (ALB) and combined with cromolyn sodium (A+CRO), ipratropium bromide (A+IB), tobramycin (A+TOB), flunisolide (A+FLU), and n-acetylcysteine (A+NAC). A BEN (PARI LC Plus) and a CONT (Hudson T UP-DRAFT II) were tested at 8 liters per minute (Lpm) for 2 and 5 min, respectively. Albuterol output and aerosol characteristics were determined by impaction and chemical analysis. Mass median aerodynamic diameter (MMAD; microm) A+CRO reduced MMAD from 2.57 (ALB) to 1.29 with CONT. A+FLU increased MMAD from 2.71 (ALB) to 3.40 with BEN. Geometric standard deviation (GSD) A+CRO increased GSD from 2.66 (ALB) to 3.36 with CONT. GSD was 2.33 for ALB and was not changed by DA with BEN. BEN generated a smaller and less heterodisperse aerosol than CONT. Respirable fraction (RF%) was 74% for ALB and was not changed by DA with CON. A+TOB and A+FLU decreased RF% from 75%, to 70% and 67% (respectively) with BEN. Respirable mass (RM; microg) for ALB was 935 and was not changed by DA with CONT. A+IB and A+FLU increased RM from 917 (ALB) to 1172 and 1240, respectively, with BEN. Co-nebulization of albuterol with other drugs can affect its output and aerosol characteristics. In vivo data is needed to asses the clinical implications of our findings.

Adrenergic beta-Agonists↗
PubMed1999

Salsalate and salicylate binding to and their displacement of thyroxine from thyroxine-binding globulin, transthyrin, and albumin.

Salsalate and its metabolite salicylate are inhibitors of thyroid hormone binding to serum transport proteins and reduce serum total thyroxine (T4) and triiodothyronine (T3) in vivo. The present study is the first to examine and compare salsalate and salicylate binding to human thyroxine-binding globulin (TBG), transthyretin (TTR), albumin (ALB), and whole human serum, and displacement by salsalate and salicylate of T4 from isolated TBG, TTR, ALB. Salsalate and salicylate binding were studied by ultrafiltration at salsalate concentrations of 0.24-1.16 mM (62-300 microg/mL) and salicylate concentrations of 0.0375-2.25 mM (6.0-360 microg/mL). T4 displacement by salsalate and salicylate from TBG, TTR, and ALB was studied by equilibrium dialysis at salsalate concentrations of 0 to 1.52 mM (0-393 microg/mL) and salicylate concentrations of 0 to 60 mM (0-9600 microg/mL). In normal human serum, 95% of salsalate and 76% of salicylate were protein-bound. In the presence of isolated ALB, 89% of salsalate and 64% of salicylate were ALB-bound. Both salsalate and salicylate inhibited T4 binding to all 3 major T4 binding proteins. Both displaced proportionately more T4 from TBG compared with TTR and ALB. The principal site to which both salsalate and salicylate in serum is bound (ALB) is different from the principal site from which they displace T4 (TBG). Salsalate potency in displacing T4 from TBG and ALB was approximately 100-fold greater than salicylate potency.

Binding, Competitive↗
PubMed2006

Preoperative carcinoembryonic antigen and albumin in predicting survival in patients with colon and rectal carcinomas.

OBJECTIVE: To examine the relationship between postoperative outcomes of colorectal carcinoma patients and preoperative serum carcinoembryonic antigen (CEA) and albumin (ALB) levels and evaluate if these levels can accurately predict outcomes and/or be factor indicating adjuvant chemotherapy. BACKGROUND: CEA is a marker for colorectal carcinoma and its level usually increases before a distant metastasis is detected. Also, a low level of serum ALB is usually found in metastatic colorectal carcinoma patients. STUDY: A retrospective cohort study of patients with colorectal carcinomas who were treated with curative surgery in Songklanagarind Hospital between 1998 and 2002. RESULTS: One hundred seventy patients were identified with a median survival of 1131 days (range 71 to 2293 d) and with an overall 5-year survival rate of 54%. Patients were stratified using CEA at 5 ng/mL and an ALB level at 3.5 g/dL into 4 groups: (1) low CEA, high ALB; (2) low CEA, low ALB; (3) high CEA, high ALB; and (4) high CEA, low ALB. The 5-year survival rates for groups 1 to 4 were 66%, 63%, 46%, and 34%, respectively. There was statistically significant difference in 5-year survival between the well-differentiated tumor with low CEA and the poorly differentiated tumor with high CEA (P=0.0115). The high CEA patients who had the well-differentiated tumor had longer survival than those with a poorly differentiated tumor (P=0.0412). CONCLUSIONS: A preoperative CEA level greater than or equal to 5 ng/mL and ALB level less than 3.5 g/dL predict a poor survival chance for colorectal carcinoma patients. In high CEA patients, tumor differentiated is an independent factor affecting survival.

Adult↗
PubMed2002

Early antioxidant therapy with Tempol during hemorrhagic shock increases survival in rats.

BACKGROUND: Hemorrhagic shock (HS) is associated with the generation of reactive oxygen species, which may contribute to delayed multiple organ system failure and death. Previous studies have shown that the antioxidant Tempol improved physiologic variables, although not necessarily outcome, in septic shock and HS. We hypothesized that the combination of free Tempol with polynitroxylated albumin (PNA)-bound Tempol (which prolongs half-life and decreases toxicity) improves outcome after HS in rats. METHODS: In study 1, HS was induced by blood withdrawal of 3 mL/100 g over 15 minutes. Mean arterial pressure was maintained at 40 mm Hg with either infusion of normal saline or withdrawal of blood from 20 to 90 minutes. Resuscitation (90-270 minutes) was with infusion of shed blood. Observation was to 72 hours. At HS 45 min, albumin (ALB) (n = 10) or PNA + Tempol (n = 10) was infused slowly (1 mL/100 g/h) until 120 minutes. Study 2 was the same as study 1 (n = 6 per group), but terminated at 150 minutes. Study 3 was the same as study 1, but started with ALB or PNA + Tempol (n = 7 per group) at 20 minutes. The primary outcome variable in studies 1 and 3 was survival, whereas the primary outcome variables in study 2 were antioxidant reserve (ability of the serum or tissue homogenate to scavenge peroxyl radicals produced by 2,2'-azobis [2-aminodipropane]-dihydrochloride) in serum and small intestine, and low-molecular-weight thiols in tissues (liver, small intestine, and kidney). RESULTS: In study 1, 72-hour survival was 1 of 10 (ALB group) versus 2 of 10 (PNA + Tempol group). At 90 minutes, pH was lower in the ALB group versus the PNA + Tempol group (p = 0.02) and remained low. Arterial lactate increased to 8.9 +/- 3.2 (mean +/- SD) versus 6.5 +/- 1.8 mmol/L (p = 0.04) and base excess was -9.6 +/- 4.3 versus -5.2 +/- 3.2 mmol/L (p = 0.01) (ALB vs. PNA + Tempol groups, respectively). In study 2, antioxidant reserve in serum was lower in the ALB group versus the PNA + Tempol group (p = 0.002). There were no differences between groups in antioxidant reserve in the small intestine or low-molecular-weight thiols in liver, kidney, and small intestine. In study 3, 72-hour survival was zero of seven (ALB group) versus five of seven (PNA + Tempol group) (p = 0.02). Heart rate and systolic blood pressure during late HS were higher in the ALB group in studies 1 and 3 (p < 0.05). CONCLUSION: When infused early in HS, PNA + Tempol can increase survival. When given late, it significantly improves acid-base and serum antioxidant status, without an effect on survival. Additional studies will be required to determine whether early resuscitation with PNA + Tempol attenuates reactive oxygen species-mediated injury as the mechanism for preventing the progression toward multiple organ failure and death after HS. The results suggest that antioxidant therapy with Tempol deserves further study as a potential adjunct in the initial resuscitation from HS.

Acid-Base Equilibrium↗