False-Positive Titers of Thyroid Autoantibodies in Patients Undergoing Hemodialysis?

1991 ◽  
Vol 37 (12) ◽  
pp. 2153-2154 ◽  
Author(s):  
Ljerka Lukinac ◽  
Zvonko Kusic ◽  
Petar Kes

Abstract Concentrations of thyroid-related hormones in serum of patients with chronic renal failure are known to be abnormal (1, 2). In our study on thyroid-function testing of patients undergoing hemodialysis, we determined, in addition to concentrations of free and total triiodothyronine, free and total thyroxin, “reverse” triiodothyronine, and thyroxin-binding globulin, the titers of thyroglobulin and microsomal autoantibodies (TGA and TMA, respectively). The study was provoked by the appearance of an uncommon agglutination pattern in the control wells of some samples from patients with chronic renal failure during the standard procedures of detecting TGA and TMA with hemagglutination methods (Thymune-T and Thymune-M assays from Welcome, London, U.K.). For these samples we were not certain whether positive titers for TGA and (or) TMA represented false-positive or true-positive values. Therefore, we assayed the absorbed serum samples and samples after addition of excess nonspecific immunoglobulin. Furthermore, we wanted to determine the difference in TGA and TMA titers of serum samples before and after hemodialysis.

Author(s):  
D R James ◽  
C P Price

We describe evidence that serum samples from patients with chronic renal failure possess a constituent that interferes with the measurement of uric acid when using a method employing uricase with peroxidase-assisted detection of the hydrogen peroxide generated. The interference is also reflected in reduced recovery of both hydrogen and sarcosine when added to serum from patients with chronic renal failure. The interferent may be protein in nature or protein bound, as the poor recovery of hydrogen peroxide is seen in patients' serum before and after haemodialysis.


PEDIATRICS ◽  
1982 ◽  
Vol 70 (5) ◽  
pp. 742-750 ◽  
Author(s):  
Anthony C. Hsu ◽  
Sang Whay Kooh ◽  
Donald Fraser ◽  
William A. Cumming ◽  
Victor L. Fornasier

The incidence, age at onset, and progression of the biochemical, radiographic, and histologic characteristics of renal osteodystrophy were studied in 50 children in whom chronic renal failure had been recently diagnosed. During a ten-year observation period, 19 patients progressed to end-stage renal failure and radiographic signs of renal osteodystrophy developed in 15 of these (79%). Renal osteodystrophy developed in all nine patients whose chronic renal failure was diagnosed before 3 years of age and in six of the ten children with later onset of failure. The mean interval from diagnosis of renal failure to development of osteodystrophy was 1.4 years. Radiographically, growth zone lesions predominated in the younger children, whereas cortical erosions were more prevalent in the older children. Histologic examination, performed in 38 patients, showed both defective mineralization and excessive resorption and was a more sensitive diagnostic index than radiography. Noticeable deformities developed in one third of the patients with osteodystrophy, despite medical treatment including vitamin D2 therapy. Deformities were particularly frequent and Severe in patients whose renal failure developed in infancy. In all 13 patients whose growth patterns were studied before and after osteodystrophy developed, the onset of bone lesions was associated with a deterioration of growth, indicating that osteodystrophy plays a major role in causing the growth retardation commonly observed in children with chronic renal failure.


1981 ◽  
Author(s):  
M Bern ◽  
J Green

Sulfinpyrazone can reduce the incidence of thrombosis of A-V shunts in chronic renal failure. The drug is also reported to prevent acute deaths from coronary artery disease. This study was to determine mechanisms for these protective effects.Patients on chronic hemodialysis served as the study models. Six patients on dialysis three times per week for 6 or more months received sulfinpyrazone 200 mgm t.i.d. p.o. for 14 days. Blood samples were obtained before dialysis was begun before and after the 14 days of drug therapy.Results are shown as mean ± standard error of mean.AT III levels rose significantly by functional and immune assays. Functional levels (by von Kaulla technique) rose 24.5 ± 3.1 sec. to 47.3 + 5.5 sec. (P>.005) Plasma protein AT III (by radial immunodiffusion) rose 31.2 ± 2.17 mg/dl to 37.9 ± 2.1 mgm/dl. (P>.01) Platelet factor 4 (by Abbot radioimmunology assay) fell from 46.4 + 13.6 ngm/ml to 9.5 ± 1.1 ngm/ml.(P>.005) The concentration of thrombin-anti-thrombin complex (by R. Rosenberg, Harvard Medical School, Boston) rose from 4.2 ± .09 to 8.4 ± 1.0 (P>.005)Thus it appears that sulfinpyrazone elevates antithrombin concentration and function while simultaneously suppressing platelet release. These two effects may or may not be mutually dependent. The clinical efficacy of sulfinpyrazone may relate in part to the elevation of antithrombin III, probably by inhibiting its consumption, while also inhibiting platelet function.


1997 ◽  
Vol 43 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Patrick C D’Haese ◽  
Glen F Van Landeghem ◽  
Ludwig V Lamberts ◽  
Vera A Bekaert ◽  
Iris Schrooten ◽  
...  

Abstract To study the possible accumulation of Sr in chronic renal failure patients, methods were developed for the determination of the element in serum, urine, bone, and soft tissues by using Zeeman atomic absorption spectrometry. Serum samples were diluted 1:4 with a Triton X-100–HNO3 mixture, whereas urine samples were diluted 1:20 with HNO3. Bone samples were digested with concentrated HNO3 in stoppered polytetrafluoroethylene (Teflon®) tubes, whereas soft tissues were dissolved in a tetramethylammonium hydroxide solution in water. For serum and urine we used matrix-matched calibration curves, whereas bone and tissue samples were measured against aqueous calibrators. Atomization was performed from the wall of pyrolytically coated graphite tubes for all of the matrices under study. Both inter- and intraassay CVs were <6% (n = 12, n = 10, respectively), and the recovery of added analyte was close to 100% for all of the biological matrices under study. Detection limits were 1.2 μg/L (serum), 0.3 μg/L (urine), 0.4 μg/g (bone), and 2.2 ng/g (soft tissues), whereas the sensitivity determined by the slope of the calibration curve, i.e., the amount of Sr producing a 0.0044 integrated absorbance change in signal, was 2.4 pg, 2.4 pg, 3.9 pg, and 2.6 pg for these matrices respectively. We conclude that the present methods are precise and accurate and easily applicable for both routine use and research investigations. They will allow us to study the metabolism of the element in chronic renal failure patients and shed some light on the association that was recently noted between increased bone Sr concentrations and the development of osteomalacia in these individuals.


2019 ◽  
Vol 18 (10) ◽  
pp. 2121-2137 ◽  
Author(s):  
Joshua W. Jeffs ◽  
Nilojan Jehanathan ◽  
Stephanie M. F. Thibert ◽  
Shadi Ferdosi ◽  
Linda Pham ◽  
...  

Exposure of blood plasma/serum (P/S) to thawed conditions (> −30 °C) can produce biomolecular changes that skew measurements of biomarkers within archived patient samples, potentially rendering them unfit for molecular analysis. Because freeze-thaw histories are often poorly documented, objective methods for assessing molecular fitness before analysis are needed. We report a 10-μl, dilute-and-shoot, intact-protein mass spectrometric assay of albumin proteoforms called “ΔS-Cys-Albumin” that quantifies cumulative exposure of archived P/S samples to thawed conditions. The relative abundance of S-cysteinylated (oxidized) albumin in P/S increases inexorably but to a maximum value under 100% when samples are exposed to temperatures > −30 °C. The difference in the relative abundance of S-cysteinylated albumin (S-Cys-Alb) before and after an intentional incubation period that drives this proteoform to its maximum level is denoted as ΔS-Cys-Albumin. ΔS-Cys-Albumin in fully expired samples is zero. The range (mean ± 95% CI) observed for ΔS-Cys-Albumin in fresh cardiac patient P/S (n = 97) was, for plasma 12–29% (20.9 ± 0.75%) and for serum 10–24% (15.5 ± 0.64%). The multireaction rate law that governs S-Cys-Alb formation in P/S was determined and shown to predict the rate of formation of S-Cys-Alb in plasma and serum samples—a step that enables back-calculation of the time at which unknown P/S specimens have been exposed to room temperature. A blind challenge demonstrated that ΔS-Cys-Albumin can detect exposure of groups (n = 6 each) of P/S samples to 23 °C for 2 h, 4 °C for 16 h, or −20 °C for 24 h—and exposure of individual specimens for modestly increased times. An unplanned case study of nominally pristine serum samples collected under NIH-sponsorship demonstrated that empirical evidence is required to ensure accurate knowledge of archived P/S biospecimen storage history.


1981 ◽  
Author(s):  
Y Endo ◽  
M Mamiya ◽  
K Takahashi ◽  

We have reported that jS-thromboglobulin (β-TG) and platelet factor 4 (PF4) increased in chronic renal failure. The purpose of the current study is to reveal a correlation between plasma β-TG (Amersham Corp. England) and renal function, a correlation between plasma β-TG and PF. (Abbott Lab., USA) and the effect of hemodialysis on patients with chronic renal failure.Significantly increased levels of plasma β-TG (76.8±25.5 ng/ml, p<0.01) were observed in 24 patients with chronic renal failure (BUN>20mg/dl), compared to normal subjects (13.2±5.6ng/ml). The increase in β-TG was highly correlated with BUN (r=0.651, p<0.01), creatinine (r=0.778, p<0.01) and creatinine clearance (r=-0.723, p<0.01). Although plasma PF4 (normal 5.0±2.0ng/ml) increased also, no statistical significance could be found. Statistical correlation between β-TG and PF4 was not found in these patients. This reason is thought to Be due to the difference of molecular weight (PF. 8000MW, β-TG 36000MW) and half-life (PF4 30min,β-TG 100min) The high levels of β-TG (89.4±3.4ng/ml) showed a further increase (109.4±5.8ng/dl, p<0.01) after dialysis. This is thought to be due to hemoconcentration, because of no adhesion of platelet to cellulose membrane but about 20% elevation in mean of other blood factors such as RBC, WBC, platelet, fibrinogen etc. The PF4 levels (before, 7.7±1.3ng/ml) which increased at 15min (55.2±19.6ng/ml, p<0.01) and 1 hr (23.7±8.4ng/ml, p< 0.01) are thought to be due to the influence of heparin infusion. The change in PF4. was not accompanied by the change in β-TG. During hemodialysis the decrease of other platelet functions such as adhesiveness, aggregation induced by ADP, collagen and PF3remained unchanged.


2013 ◽  
Vol 62 (18) ◽  
pp. C170
Author(s):  
Abdulkadir Yıldız ◽  
Abdurrahman Akyuz ◽  
Murat Yuksel ◽  
Mustafa Oylumlu ◽  
Mehmet Zihni Bilik ◽  
...  

1994 ◽  
Vol 40 (8) ◽  
pp. 1544-1548 ◽  
Author(s):  
N C France ◽  
P T Holland ◽  
M R Wallace

Abstract We tested the possibility that the buffering agents in dialysis bath fluid might contribute to increased endogenous oxalate production in dialyzed patients. Using stable isotope dilution mass spectrometry, we obtained oxalate production rates and pool sizes directly for 10 patients in chronic renal failure, 5 of whom were undergoing continuous ambulatory peritoneal dialysis (lactate-buffered fluid). All peritoneal dialysis patients had either increased oxalate production rates or expanded oxalate pools when compared with undialyzed patients in renal failure. From a further four patients receiving maintenance hemodialysis we took blood samples immediately before and after three consecutive dialysis sessions in which the bath-fluid buffering agent (bicarbonate or acetate) was alternated; we analyzed these samples for oxalate and key precursors by capillary gas chromatography. Plasma glycine and serine concentrations remained within the physiological range. Glycolate and oxalate concentrations decreased, but the oxalate remained above normal after dialysis. All changes were independent of the bath-fluid buffering agent. We suggest that dialysis might stimulate the formation of oxalate by removing product inhibition of a late catabolic step.


1988 ◽  
Vol 35 (6) ◽  
pp. 865-876 ◽  
Author(s):  
SHINICHI SAKURAI ◽  
YOSHIHITO HARA ◽  
SHIRO MIURA ◽  
MICHIYUKI URABE ◽  
KENICHI INOUE ◽  
...  

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