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PubMed1996

High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin.

Binding of laurate (n-dodecanoate) to genetic variants of albumin or its proprotein and to normal albumin isolated from the same heterozygous carriers was studied by a kinetic dialysis technique at physiological pH. The first stoichiometric association constant for binding to proalbumin Lille (Arg-2-->His) and albumin (Alb) Roma (Glu321-->Lys) was increased to 126% and 136% respectively compared with that for binding to normal albumin, whereas the constant for Alb Maku (Lys541-->Glu) was decreased to 80%. In contrast, normal laurate-binding properties were found for as many as nine other albumin variants with single amino acid substitutions. Because the net charges of all these mutants were different from that of normal albumin, the results suggest that the examples of modified laurate binding are not caused by long-range electrostatic effects. Rather, the three positions mentioned are located close to different binding sites for the fatty acid anion. The most pronounced effect was observed for the glycosylated Alb Casebrook, the binding constant of which was decreased to 20%. Binding to the glycosylated Alb Redhill was also decreased, but to a smaller extent (68%). These decreases in binding are caused by partial or total blocking of the high-affinity site by the oligosaccharides, by the negative charges of the oligosaccharides, and/or by conformational changes induced by these bulky moieties. Laurate binding to two chain-termination mutants (Alb Catania and Alb Venezia) was normal, indicating that the C-terminus of albumin is not important for binding. By using different preparations of normal albumin as controls in the binding experiments, it was also possible to compare the effect of various methods for isolation and defatting on laurate binding.

Amino Acid Sequence↗
PubMed2001

Prokinetic agents increase plasma albumin in hypoalbuminemic chronic dialysis patients with delayed gastric emptying.

Hypoalbuminemia is a surrogate of malnutrition in patients with end-stage renal disease undergoing chronic dialysis and commonly improves with prescription of adequate nutrition and dialysis. Nevertheless, some patients remain hypoalbuminemic for poorly understood reasons. We tested the hypotheses that chronic dialysis patients who remain hypoalbuminemic despite prescription of adequate nutrition and dialysis (1) have delayed gastric emptying, and (2) that prokinetic agents will increase plasma albumin (P(alb)) levels in patients with delayed gastric emptying. We retrospectively identified 99 of 343 hemodialysis and peritoneal dialysis patients with hypoalbuminuria (P(alb) < 3.5 mg/dL) and studied those who did not (hypoalbuminemic, n =15) and did (normoalbuminemic, n = 15) increase their P(alb) levels over the subsequent 6 months and met inclusion and exclusion criteria. Gastrointestinal symptom scores determined by an administered questionnaire were not different in hypoalbuminemic and normoalbuminemic patients. Conversely, the half-time (T(1/2)) for radionuclide gastric emptying was longer in hypoalbuminemic than normoalbuminemic patients (74.5 +/- 7.4 versus 46.7 +/- 4.6 minutes; P < 0.004). Hypoalbuminemic patients were prescribed prokinetics and followed prospectively for 6 months, during which time gastric T(1/2) decreased to 53.9 +/- 3.3 minutes (P < 0.01 versus initial) and P(alb) increased from 3.1 +/- 0.2 to 3.5 +/- 0.2 mg/dL (P < 0.004). The net increase in P(alb) level correlated with the net decrease in gastric T(1/2) (r(2) = 0.4; P < 0.04) by linear regression. The data show that some persistently hypoalbuminemic chronic dialysis patients have poor gastric emptying and increase their P(alb) levels in response to prokinetic agents.

Cisapride↗
PubMed2002

Changes in urinary excretion of six biochemical parameters in normotensive pregnancy and preeclampsia.

We evaluated renal functions by urinary biochemical parameters in normotensive pregnancy and preeclampsia. The parameters are expected to be altered resulting from different abnormalities of renal glomeruli and tubules. We chose N-acetyl-beta-d-glucosaminidase (NAG), beta2-microglobulin (beta2MG), total protein (TP), albumin (Alb), urea nitrogen (UN), uric acid (UA), and creatinine (Cr). Urinary excretion of these biochemical parameter concentrations (relative to Cr) was measured simultaneously in first morning fasting urine samples from 27 healthy nonpregnant women (group 1), 32 women with normotensive pregnancies (group 2), and 26 women with preeclampsia (group 3). The average gestational age at entry was 36 weeks. Serum UN and serum UA also were measured. All the ratios were significantly higher in group 2 than in group 1. The NAG-to-Cr, TP-to-Cr, and Alb-to-Cr ratios were significantly higher in group 3 than in group 2. In contrast, the UN-to-Cr and UA-to-Cr ratios were significantly lower in group 3 than in group 2. The percent increase in the beta2MG-to-Cr ratio in group 2 relative to that in group 1 was the highest, followed by percent increases in the NAG-to-Cr, TP-to-Cr, Alb-to-Cr, UA-to-Cr, and UN-to-Cr ratios. In contrast, the percent increase in the Alb-to-Cr ratio in group 3 relative to that in group 2 was the highest, followed by percent increases in the TP-to-Cr, NAG-to-Cr, beta2MG-to-Cr, UA-to-Cr, and UN-to-Cr ratios. The percent increases in the NAG-to-Cr and beta2MG-to-Cr ratios rose markedly in normotensive pregnancy, whereas percent increases of the Alb-to-Cr and TP-to-Cr ratios were far greater in preeclampsia than in normotensive pregnancy. Renal tubular damage and reabsorption dysfunction may be impaired markedly even in normotensive pregnancy, and further deterioration in reabsorption dysfunction may be slight in preeclampsia. Renal glomerular permeability of TP and Alb may be enhanced in normotensive pregnancy and markedly enhanced in preeclampsia.

Adult↗
PubMed1988

Increase in albumin, IgG, and IgM blood-nerve barrier indices in human diabetic neuropathy.

The albumin (Alb), IgG, and IgM concentrations in the endoneurium of fascicular sural nerve biopsy samples were evaluated in controls (n = 9 or 10), diabetic patients without neuropathy (n = 6), and diabetic patients with polyneuropathy (n = 17 or 18). These values were significantly increased in diabetic patients with and without neuropathy when expressed both per endoneurial dry weight or endoneurial total protein compared to biopsy samples from healthy controls. When these concentrations, expressed per endoneurial total protein, were related to plasma concentrations similarly expressed, the resulting blood-nerve barrier (BNB) indices were significantly increased for Alb (6.1 times; P less than 0.00001), IgG (4.9 times; P = 0.00037), and IgM (2.7 times; P = 0.015). The diabetic patients without neuropathy (defined as having an index of pathology of greater than 0.65; a measure of the severity of the pathological abnormality based on morphological criteria) also had significant increases in two of these BNB indices that were intermediate between the diabetic neuropathy patients and controls (Alb, 3.9 times controls; P = 0.00002: IgG, 4.6 times controls; P = 0.00016: IgM, 1.8 times controls; not significant). No correlations were observed between the endoneurial concentrations of these plasma proteins or the BNB indices and the index of pathology, suggesting that these increases in endoneurial plasma proteins precede the pathologic alterations. The increased values for the diabetics in the absence of pathological abnormalities may prove useful in predicting neuropathic complications. The ratio of the IgG-BNB index to the Alb-BNB index was decreased 19%, and the ratio of the IgM-BNB index to the Alb-BNB index was decreased 56% in diabetic neuropathy patients compared to controls. Although the IgG and IgM concentrations are increased in the diabetic endoneurium, the Alb increase is greater and a mechanism other than size indiscriminate extravasation of plasma proteins, therefore, is suggested. Morphometric assessment of the endoneurial compartments, which would be expected to contain these plasma proteins, suggests that they are not altered in diabetic neuropathy; hence, it is hypothesized that the observed increase in endoneurial concentration of these plasma proteins results from altered transport through the endothelial or perineurial barrier, which supports an underlying vascular mechanism in the development of diabetic polyneuropathy.

Adult↗
PubMed2002

STAT3 contributes to the mitogenic response of hepatocytes during liver regeneration.

STAT3 is rapidly induced during liver regeneration in an interleukin 6 (IL-6)-dependent fashion, and IL-6 is required for normal liver regeneration. We wanted to know whether STAT3 was also required for liver regeneration but disruption of the STAT3 gene during embryonic stages causes lethality. Therefore, an albumin promoter-driven Cre-loxP recombination system was used to create a STAT3 deletion in the adult mouse liver to study the role of STAT3 in liver regeneration. After partial hepatectomy, there was virtually no STAT3 RNA or protein induction in Alb(+) STAT3(fl/fl) livers. STAT3 DNA binding activity was also absent in Alb(+) STAT3(fl/fl) livers. Unlike in control livers, STAT1 was activated in STAT3 conditional-mutant livers posthepatectomy. Hepatocyte DNA synthesis at 40 h posthepatectomy in Alb(+) STAT3(fl/fl) livers was reduced to approximately one-third of the control. Alb(+) STAT3(fl/fl) livers had abnormalities in immediate-early gene activation that largely correlated with but were not identical to those seen in IL-6-/- livers. G(1) phase cyclins including cyclins D1 and E had lower expression levels in Alb(+) STAT3(fl/fl) livers, indicating an abnormal G(1) to S phase transition. Therefore, STAT3 accounts for part of the DNA synthetic response of the hepatocytes during liver regeneration, which cannot be compensated for by induction of STAT1. Normal activation of the MAPK pathway in Alb(+) STAT3(fl/fl) livers reinforces the fact that at least part of the effect of IL-6 on hepatocyte proliferation is not mediated by STAT3. This study provides the first in vivo evidence that STAT3 promotes cell cycle progression and cell proliferation under physiological growth conditions.

Animals↗
PubMed1993

Measurement of adducts of benzoquinone with hemoglobin and albumin.

Benzoquinones (BQ) are genotoxic species that stem from metabolism of phenolic compounds. We have developed a method for measuring adducts of 1,2- and 1,4-benzoquinone (1,2-BQ and 1,4-BQ) with cysteine residues of hemoglobin (Hb) and albumin (Alb). The method employs a reductive catalyst (Raney nickel) to selectively cleave sulfur-bound adducts so that they may be extracted with an organic solvent, derivatized with heptafluorobutyrylimidazole and measured by GC-ECD or GC-MS. Reactions of 1,4-BQ (0-300 microM) with whole blood of both F344 rats and humans resulted in linear formation of adducts with Hb and Alb. Adducts of 1,2-BQ with human Alb were formed by activation of catechol (0-300 microM) in situ with horseradish peroxidase. The mean half lives in vitro of 1,4-BQ in blood from humans and rats were 3.5 and 0.68 h, respectively. Second-order rate constants for reaction of 1,4-BQ with Hb and Alb in whole blood were estimated to be 18 and 76 l/mol/h for humans and 180 and 74 l/mol/h for rats respectively. Interestingly, the following high background levels of 1,2-BQ and 1,4-BQ adducts were observed in the proteins: 1,2-BQ-human Hb = 1.5 nmol/g, rat Hb = 25.1 nmol/g; human Alb = 8.0 nmol/g; 1,4-BQ-human Hb = 27.2 nmol/g, rat Hb = 11.5 nmol/g; human Alb = 20.5 nmol/g. These large background levels of BQ adducts suggest that significant exposure to BQ precursors occurs from dietary and/or endogenous sources. Given current evidence regarding the genotoxicity of BQ, such exposures and their health consequences should be investigated.

Animals↗
PubMed2004

Long-term exposure to elevated levels of circulating TIMP-1 but not mammary TIMP-1 suppresses growth of mammary carcinomas in transgenic mice.

Tissue inhibitor of metalloproteinases-1 (TIMP-1) regulates matrix metalloproteinase activity, acts as a growth stimulator and inhibits apoptosis. We developed transgenic mice to evaluate the relevance of circulating versus mammary TIMP-1 in mammary carcinogenesis. The transgene was placed under the control of the albumin (Alb) promoter for the production of large amounts of TIMP-1 in the liver and release into the systemic circulation to achieve chronically elevated blood levels. The initial 7,12-dimethylbenz[a]anthracene (DMBA) mammary carcinogenesis study showed greatly decreased tumor incidence in heterozygous Alb-TIMP-1 mice (25%), compared with their wild-type (wt) littermates (83.3%). Metastatic mammary carcinomas were induced in the Alb-TIMP-1 mice through breeding with mice expressing the polyomavirus Middle T antigen (MT) under the control of the mouse mammary tumor virus-long terminal repeat (MMTV-LTR). Both the mammary tumor burden and the incidence of lung metastases were lower in the Alb-TIMP-1/MMTV-MT mice than their MMTV-MT littermates. Analysis of the Alb-TIMP-1/MMTV-MT tumors showed evidence of decreased proliferative activity and inhibition of apoptosis, whereas microvascular density was not affected. Transgenic expression of TIMP-1 in mammary epithelial cells was accomplished by using MMTV-LTR. In contrast to the Alb-TIMP-1 mice, there was insignificant difference in the growth of both DMBA- and MT-induced mammary tumors between heterozygous MMTV-TIMP-1 mice and their wt littermates. The MT-induced mammary tumors of the MMTV-TIMP-1 mice were separated into 'low' and 'high' TIMP-1 expressing groups. The 'high' TIMP-1 expressing tumors exhibited significantly higher proliferative activity than the tumors of the MMTV-MT only mice, whereas the number of apoptotic cells and microvascular density were not different. The findings of this study show that circulating TIMP-1, but not mammary-derived TIMP-1, has growth suppressive effects on DMBA and MT-induced mammary carcinomas.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed2003

Determinants of aflatoxin exposure in young children from Benin and Togo, West Africa: the critical role of weaning.

BACKGROUND: Dietary exposure to high levels of the fungal toxin, aflatoxin, occurs in West Africa, where long-term crop storage facilitates fungal growth. METHODS: We conducted a cross-sectional study in Benin and Togo to investigate aflatoxin exposure in children around the time of weaning and correlated these data with food consumption, socioeconomic status, agro-ecological zone of residence, and anthropometric measures. Blood samples from 479 children (age 9 months to 5 years) from 16 villages in four agro-ecological zones were assayed for aflatoxin-albumin adducts (AF-alb) as a measure of recent past (2-3 months) exposure. RESULTS: Aflatoxin-albumin adducts were detected in 475/479 (99%) children (geometric mean 32.8 pg/mg, 95% CI: 25.3-42.5). Adduct levels varied markedly across agro-ecological zones with mean levels being approximately four times higher in the central than in the northern region. The AF-alb level increased with age up to 3 years, and within the 1-3 year age group was significantly (P = 0.0001) related to weaning status; weaned children had approximately twofold higher mean AF-alb adduct levels (38 pg AF-lysine equivalents per mg of albumin [pg/mg]) than those receiving a mixture of breast milk and solid foods after adjustment for age, sex, agro-ecological zone, and socioeconomic status. A higher frequency of maize consumption, but not groundnut consumption, by the child in the preceding week was correlated with higher AF-alb adduct level. We previously reported that the prevalence of stunted growth (height for age Z-score HAZ) and being underweight (weight for age Z-score WAZ) were 33% and 29% respectively by World Health Organziation criteria. Children in these two categories had 30-40% higher mean AF-alb levels than the remainder of the children and strong dose- response relationships were observed between AF-alb levels and the extent of stunting and being underweight. CONCLUSIONS: Exposure to this common toxic contaminant of West African food increases markedly following weaning and exposure early in life is associated with reduced growth. These observations reinforce the need for aflatoxin exposure intervention strategies within high-risk countries, possibly targeted specifically at foods used in the post-weaning period.

Aflatoxins↗
PubMed2001

Conversion between bromcresol green- and bromcresol purple-measured albumin in renal disease.

BACKGROUND: Albumin measured by a bromcresol purple dye-binding assay (Alb(BCP)) agrees more closely with the gold standard of immunonephelometry than does bromcresol green (Alb(BCG)) measurement. Both tests are in current clinical use. A method for converting between the two would be useful. METHODS: We measured albumin by bromcresol green and bromcresol purple in 535 patients, 155 of whom had renal disease. We randomly divided data from the patients with renal disease into two equal-sized sets, and used one set to derive, and the remaining set to validate, a regression equation relating the two values. RESULTS: The relationship Alb(BCG)=5.5+Alb(BCP) performed very well in both the renal patient validation set and in the data from 380 unselected in-patients and out-patients. Intraclass correlations for agreement between measured Alb(BCG) and predicted Alb(BCG) was 0.98 in both analyses. CONCLUSIONS: The ability to convert between these measurements will be of use in clinical situations where the absolute value of the serum albumin is important, when data from laboratories using different methodologies must be combined, and in the application of the Modification of Diet in Renal Disease formula to estimate glomerular filtration rate in patients whose albumin has been measured by bromcresol purple.

Bromcresol Green↗
PubMed2004

Increased glomerular albumin permeability in old spontaneously hypertensive rats.

BACKGROUND: Severe long-standing hypertension is associated with an increased urinary protein excretion. METHODS: To investigate the mechanisms of this proteinuria, we measured the glomerular clearances and calculated the glomerular sieving coefficients (theta) for neutral albumin (theta(o-alb)) and for native albumin (theta(alb)) in spontaneously hypertensive rats (SHR) at the ages of 3, 9 and 14 months, in comparison with age-matched normal control Wistar rats (NCR). The hypothesis was that increases in the glomerular permeability of both negatively charged and neutral albumin would indicate a preferential size-selective dysfunction of the glomerular capillary wall (GCW), while an increased permeability to negatively charged albumin, as compared with neutral albumin, predominantly would indicate a charge-selectivity dysfunction of the GCW. A tissue (renal) uptake technique together with urinary sampling was used to assess theta. The glomerular filtration rate was assessed using the plasma to urine clearance of (51)Cr-EDTA. RESULTS: The theta(alb) in SHR increased 2.6 times at 14 months of age as compared with at 3 months, while there was no significant change of theta(alb) in NCR with age. Furthermore, the increased theta(alb) in old SHR correlated significantly with an increase in theta(o-alb) (r = 0.86, P<0.001), suggesting that albuminuria in old SHR primarily results from an increased number of rather unselective ('large') pores in the glomerular filter. CONCLUSIONS: In old age, but not at a young age, hypertensive rats develop proteinuria as a result of dysfunction of the glomerular capillary filter, affecting primarily its size-selectivity. The changes are functionally compatible with the appearance in the glomerular barrier of an increased number of more unselective pores.

Age Factors↗
PubMed1986

Fluid resuscitation after an otherwise fatal hemorrhage: II. Colloid solutions.

We developed a fixed-volume porcine hemorrhage model that simulates the rapid exsanguination of combat or civilian trauma victims. In this study we compared the ability of colloid resuscitation solutions to prevent death after an otherwise lethal hemorrhage in 100 swine. The shed blood was replaced in a 1:1 ratio with either autologous whole blood (WB), untyped swine fresh frozen plasma (FFP), typed FFP, 5% human serum albumin (ALB), or normal saline (NS). Survival rate analysis indicated that WB was significantly better than FFP (untyped), ALB, or NS but not better than typed FFP. The 24-hour survival rates were: WB = 90%, typed FFP = 79%, untyped FFP = 56%, ALB = 57%, and NS = 25%. All deaths in the untyped FFP group suddenly occurred during or within 15 minutes after treatment in a recovering animal. Deaths in the ALB group steadily occurred for up to 2 1/2 hours after treatment. Analysis of hemodynamic, arterial blood gas, and acid-base data indicated that WB and FFP provided a better acid-buffering capacity in surviving animals than NS or ALB. We conclude that compatible FFP is a better resuscitation agent than ALB after an otherwise fatal hemorrhage because FFP is a better acid buffer.

Acid-Base Equilibrium↗
PubMed2002

Proteinuria after injection of human focal segmental glomerulosclerosis factor.

BACKGROUND: Recurrent focal segmental glomerulosclerosis (FSGS) is heralded by proteinuria that may remit after treatment with plasmapheresis or immunoadsorption. Study of recurrent FSGS has been hampered by lack of an animal model that exhibits a pattern of proteinuria that mimics human disease. We have obtained a component of FSGS patient plasma (FSGS factor) that increases glomerular albumin permeability (P(alb)) in vitro and causes transient proteinuria in vivo. METHODS: Plasma fractions containing FSGS factor and comparable plasma fractions from normal donors were injected into normal male Sprague-Dawley rats. Urinary protein, albumin, and creatinine were measured at various time points. Additionally, plasma samples from test animals were collected after injection and tested for FS activity defined by increased P(alb). Finally, glomeruli were isolated from animals after injection and P(alb) of these glomeruli tested. RESULTS: Proteinuria and albuminuria were increased by 24 hr after injection with FSGS factor, and returned to baseline by 48 hr after injection. Injection with the same fraction of normal plasma had no effect on urinary protein. FSGS factor increased urinary protein in a dose-dependent manner. Serum collected from rats 15 or 60 min after injection with FSGS factor increased P(alb) of glomeruli in vitro, whereas serum collected 3 or more hours after injection had no effect. Glomeruli isolated from rats receiving injections with FSGS factor had increased in vitro P(alb) compared with glomeruli from rats injected with a fraction from normal plasma. CONCLUSIONS: We have demonstrated that a single injection of FSGS factor increases P(alb) and, causes transient albuminuria and proteinuria in rats. FS activity in the plasma of recipient rats is also transient. This is the first detailed description of the time course and dose-dependence of proteinuria caused by FSGS factor in an animal model.

Animals↗
PubMed2004

Lipopolysaccharide is a cofactor for malondialdehyde-acetaldehyde adduct-mediated cytokine/chemokine release by rat sinusoidal liver endothelial and Kupffer cells.

BACKGROUND: The nonparenchymal cells of the liver have been suggested to play a significant role in the inflammatory processes observed in the development and/or progression of alcoholic liver disease. Our laboratories have shown that malondialdehyde-acetaldehyde (MAA)-modified proteins can induce immune responses, cytokine/chemokine secretion, and antigen processing and presentation by liver sinusoidal endothelial cells (SECs). Another molecule that has been shown to induce similar types of responses in Kupffer cells (KCs) is lipopolysaccharide (LPS). Because these materials induce similar responses, it was the purpose of this study to investigate the relationship between LPS and MAA-modified proteins in the development of proinflammatory responses by SECs and KCs. METHODS: For these studies, SECs and KCs were isolated from chow-fed, pair-fed, and ethanol-fed rats. Cells were stimulated with media alone, bovine serum albumin (Alb), or MAA-modified Alb (MAA-Alb) in the presence or absence of LPS 1 ng/ml, and the supernatants were assayed by enzyme-linked immunosorbent assay for tumor necrosis factor alpha, macrophage chemotactic protein 1, and macrophage inhibitory protein. RESULTS: All three cytokines/chemokines were 3 to 5 times higher when SECs or KCs were stimulated by MAA-Alb in the presence of LPS, in contrast to cells stimulated with Alb or media in the presence of LPS. Chronic ethanol consumption (6 weeks) had variable effects on the secretion of these cytokines/chemokines but in general did not alter the increased secretion in response to MAA-Alb in the presence of LPS. CONCLUSIONS: These studies strongly suggest that the sensitization of SECs and KCs by LPS plays a significant role in the development and/or progression of alcoholic liver disease, and the subsequent activation by MAA-modified proteins may be a mechanism by which proinflammatory processes are initiated.

Animals↗
PubMed1990

D-penicillamine and D-penicillamine-protein disulphide in plasma and synovial fluid of patients with rheumatoid arthritis.

1. The plasma pharmacokinetics of D-penicillamine (D-pen) and D-penicillamine-albumin disulphide (D-pen-alb) were examined over a dosage interval in six patients with rheumatoid arthritis. In two of these, 24 h synovial fluid profiles of D-pen and D-pen-alb were also obtained. 2. D-pen was undetectable in plasma at the beginning of the study. The peak concentration (5.4 +/- 1.2 microM) occurred at between 45 min and 2 h and the mean elimination half-life was 0.6 h. D-pen-alb, however, was present at a mean plasma concentration of 19.1 microM prior to dosage, peaked at 26.2 microM and was eliminated with a half-life of 40 h. 3. D-pen concentrations in synovial fluid rose more slowly and peaked lower than in plasma. D-pen-alb was present in synovial fluid of the patients at 50.1% and 83.6%, respectively, of the simultaneous plasma concentration prior to dosage. Concentrations varied during the study interval, corresponding to changes in plasma concentrations. 4. These results demonstrate that D-pen forms stable conjugates with protein in treated patients. The presence of D-pen-alb in relatively high concentrations throughout the dosage interval contrasts with the low concentrations and rapid elimination of D-pen. Both D-pen and D-pen-alb were also shown to be present at the putative site of drug action (the inflamed synovial joint) in concentrations lower than those in plasma.

Adult↗
PubMedDate not supplied

Albumin localization in the testis of adult golden hamsters by use of immunohistochemistry.

There is an increasing interest in different biochemical roles of albumin (Alb) in respect to testicular function. For this reason, Alb was localized by the peroxidase-antiperoxidase technique in the testis of adult golden hamsters. A strong Alb immunoreactivity occurred in the interstitial space and on the surface of Leydig cells. A few Sertoli cells showed a strong Alb response under the appearance of so-called leakages traversing Sertoli-Sertoli cell junctions. Spermatogonia reacted strongly, while spermatids and sperms showed rather a mild, or moderate response. Spermatocytes remained unstained. When similar maturation stages of seminiferous tubules were compared, the number of reacting cells varied strikingly. Our results support the assumption that Alb or a protein with an Alb-like immunoreactivity exerts diverse functions of the testis.

Albumins↗
PubMed1995

Influence of acute inflammation on iron and nutritional status indexes in older inpatients.

OBJECTIVE: To investigate the relations between acute inflammation, as shown by high C-reactive protein (CRP) serum levels, and laboratory indexes of iron and nutritional status and to ascertain whether the presence of acute inflammation affects the diagnostic reliability of these indexes. DESIGN: Cross-sectional study. SETTING: Geriatric ward for rehabilitation. PARTICIPANTS: A total of 163 patients, 77 men and 86 women aged 60 years or older. MEASUREMENTS: CRP values > 1 mg/dL were considered to indicate the presence of acute inflammation. Iron status was explored by measuring erythrocyte mean cell volume (MCV), hemoglobin (Hb), serum iron (Fe), TIBC, percent transferrin saturation (% TS) and ferritin (SF). Nutritional status was determined by albumin (Alb) and prealbumin (pre-Alb) serum levels. MAIN RESULTS: In the whole series, CRP correlated significantly with all iron status variables except erythrocyte MCV (directly with SF, inversely with the others) and correlated inversely with Alb and pre-Alb. Mean values of iron status variables were significantly different in patients with inflammation and those without: SF was higher and the other variables lower. Patients with low % TS (< 16%) showed a pattern consistent with iron deficiency. Compared to the group with normal values, they had more severe anemia, lower MCV, Fe, and SF, and higher TIBC; mean Alb, pre-Alb, and CRP values were not significantly different. The prevalence of inflammation was 50% (39.5% in the group with normal % TS). A similar pattern was observed in patients with microcytosis (MCV < 84 fL) associated with low % TS; dividing this subgroup according to SF values (low, < 30 micrograms/L) did not provide more information because patients with acute inflammation were excluded. CONCLUSIONS: Patients with acute inflammation present altered iron status indexes that resemble those observed in the anemia of chronic disease. Fe, TIBC and SF lose diagnostic value. The concomitant presence of microcytosis and low % TS, and to a lesser extent the presence of one of these alterations, is suggestive of iron deficiency associated with inflammation and may warrant gastrointestinal tract investigations and ferrous salt treatment. Protein-calorie malnutrition seems to enhance the effects of inflammation on iron status indexes.

Acute Disease↗
PubMed2001

Distribution spaces for hyaluronan and albumin in rat tail tendons.

A low concentration of hyaluronan (HA) in lymph compared with tissue suggests a large bound fraction. To investigate the distribution and mobility of HA and serum albumin (Alb), we eluted the rat tail tendon with a series of l5 successive centrifugations, each preceded by the addition of 0.15 M NaCl (15% of initial wet wt). The eluate concentration fell exponentially versus the accumulated eluate, allowing estimation of the maximal elutable amount (E(HA) and E(Alb)). Alb elution was practically complete from a space of approximately 28% of wet wt at all centrifugation rates. Twenty percent of HA was elutable at 500 rpm, apparently from the same space as Alb, increasing to 40% at >4,000 rpm. This pattern was not significantly influenced by using 2 M NaCl or by the addition of plasma or metabolic inhibitors. Without prehydration and centrifugation at high revolutions per minute, both Alb and HA concentrations fell rapidly toward zero, presumably in part reflecting mobilization of HA- and Alb-free fluid from the collagen intrafibrillar space (3). We conclude that with prehydration the fibrils swell, increasing the intramolecular spaces to become "penetrable" to HA and allowing removal of HA-containing fluid when the fibrils are compressed by the next centrifugation at high revolutions per minute, increasing E(HA) from 23 to 45%. Chemical binding presumably explains the unelutable 55% of tendon HA. Intrafibrillar HA may act to stabilize the fibrillar volume.

Animals↗
PubMed1996

Serum albumin for estimating creatinine clearance in the elderly with muscle atrophy.

The present study was conducted to develop a special formula to predict creatinine clearance (CCr, ml/min) in the elderly with chronic muscle atrophy using serum albumin (Alb, g/dl). We obtained 90 data sets including actual body weight (BW, kg), urinary creatinine excretion (UCr, mg/24 h), serum creatinine (SCr, mg/dl), and Alb from 90 inpatients aged 60-92 years. Regression equations were determined between the dependent variable of UCr/BW and the explanatory variable of Alb as follows: For males Ucr/BW = 2.695 Alb + 4.665 For females Ucr/BW = 1.827 Alb + 4.146. Then, the new predictive formula was derived from the equations: For males CCr = (19Alb + 32)BW/(100 x SCr) For females CCr = (13Alb + 29)BW/(100 x SCr). Evaluations for the predictive error (predicted CCr- measured CCr) showed that the new formula could provide more accurate and less biased estimates of CCr than the Cockcroft and Gault formula could, even in patients with renal insufficiency and in those with Alb < or = 2.8 g/dl.

Aged↗