A study of the relationship between albuminuria, proteinuria and urinary reagent strips.

BACKGROUND: The aims of this study were to examine the relationship between proteinuria and albuminuria and to assess the equivalence between the albumin to creatinine ratio (ACR) and the protein to creatinine ratio (PCR) at the cut-offs recommended by the National Institute for Health and Clinical Excellence (NICE) guidance on chronic kidney disease. The sensitivity and specificity of the reagent strips used in our laboratory for the detection of clinical proteinuria was also assessed. METHODS: Urine samples (n = 117) were screened for protein using the Bayer Multistix 10SG and read manually. Urinary total protein and creatinine was measured on the Roche P Modular by the benzethonium chloride and kinetic Jaffe methods, respectively. Urinary albumin was measured by immunoturbidimetry on the Roche Cobas Mira. RESULTS: The relationship between urinary protein and albumin loss was non-linear (P < 0.05). As urinary protein loss increased the percentage of albumin to total protein increased. At the NICE guidance recommended cut-offs for clinical proteinuria (ACR > or =30 mg/mmol and PCR > or =50 mg/mmol) there was one discordant result between ACR and PCR (ACR <30 mg/mmol and PCR >50 mg/mmol). The Bayer Multistix 10SG had a sensitivity and specificity of 97% and 62%, respectively, for the detection of clinical proteinuria compared with ACR. CONCLUSIONS: The proportion of urinary total protein attributable to albumin changes with concentration. There was only one discordant result between ACR and PCR: therefore either ratio may be used for the identification of clinical proteinuria. As a screening test for proteinuria, the Bayer Multistix 10SG had an acceptable sensitivity but poor specificity.

Evaluation of the albumin cobalt binding (ACB) assay for measurement of ischaemia-modified albumin (IMA) on the Beckman Coulter LX-20.

BACKGROUND: In the presence of ischaemia, albumin undergoes changes resulting in the formation of ischaemia-modified albumin (IMA). Increased serum concentrations of IMA have been found in patients with myocardial ischaemia. The purpose of this study was threefold: to evaluate the albumin cobalt binding (ACB) assay for measurement of IMA on the Beckman Coulter LX-20; to establish a reference range for IMA; and to investigate the relationship between IMA and total albumin concentrations. METHODS: The ACB assay was evaluated under the following headings: imprecision, accuracy and reliability. A reference range was established on a population of 81 healthy subjects. RESULTS: The within-batch coefficient of variation (CV) at IMA concentrations of 88, 99 and 120 KU/L were 1.4, 2.0 and 2.5%, respectively. The between-batch CVs at 74, 84 and 123 KU/L were 3.4, 3.3 and 3.0%, respectively. Comparison with the Cobas Mira Plus showed a mean negative bias of 7 KU/L. The 97.5th percentile established on our reference population was 110 KU/L. A significant inverse relationship was found between total serum albumin and IMA concentrations (r = -0.66, P < 0.0001). Correcting the IMA concentrations for total albumin in our reference population, using a formula devised in this study, yielded a range similar to that of uncorrected IMA. CONCLUSIONS: The ACB assay was found to have acceptable precision and performed very satisfactorily on the Beckman Coulter LX-20. A correction to measured IMA concentrations, to take into account total albumin concentrations, may need to be applied for the proper interpretation of IMA results.

Evaluation of three different specimen types (serum, plasma lithium heparin and serum gel separator) for analysis of certain analytes: clinical significance of differences in results and efficiency in use.

BACKGROUND: There is a lack of consensus regarding the most appropriate specimen type for analysis of many biochemistry analytes. The aim of this study was to compare renal and lipid analyte profiles and phenytoin values in plain serum (S), serum gel (G) and plasma (lithium heparin, P) tubes and to investigate the stability of these analytes after prolonged contact with cells or gel at room temperature (RT, 20 degrees C) and as aliquoted and stored at 4 degrees C. METHODS: Primary specimens were centrifuged once, maintained at RT and analysed within 2 h (T(0)) and after 24 h (T(24)) and 48 h (T(48)). For assessment of stability at 4 degrees C, two cell-free aliquots were separated from each of the primary tubes and stored at 4 degrees C and then analysed at T(24) and T(48). Differences in analyte concentrations between tubes at T(0) and following storage (at T(24) and T(48)) were evaluated for both statistical and clinical significance. RESULTS: At T(0) all analytes, except potassium, demonstrated equivalence between serum, gel and plasma tubes. Potassium and creatinine were more stable in gel tubes than in serum/plasma tubes. In contrast, phentytoin was stable in plain serum and plasma up to T(48) at RT, but showed a progressive and clinically significant decrease in concentration in gel tubes at T(24) and T(48) at RT. All analytes except CO(2) were stable up to T(48) when aliquoted and stored at 4 degrees C. CONCLUSIONS: We concluded that the serum gel tube has advantages over plain serum and plasma tubes for measurement of the analytes investigated in this study, with the exception of phenytoin. In practice, the gel tubes demonstrate enhanced analyte stability and reduce the need to aliquot specimens, with greater protection against possible contamination. Further investigation would be required to evaluate a broader range of analytes.

Differential production of adrenal steroids by purified cells of the human adrenal cortex is relative rather than absolute.

OBJECTIVES: The adrenal cortex produces aldosterone, cortisol and androgens in response to ACTH and angiotensin II. To define the differential response of morphologically distinct cells of the adrenal cortex, we examined the phenotypical and functional characteristics of human adrenocortical cells. RESULTS: Tumour growth factor-beta receptor-1 (TGFbeta-R1) and CYP-11 were found to be expressed predominantly in the zona fasciculata, whereas human leukocyte antigen (HLA-DR) and CYP-17 were localised to the zona reticularis. The angiotensin II receptor, AT-1, was found to be predominantly expressed in the zona glomerulosa. Adrenocortical cells, separated by density, yielded two distinct fractions which displayed differential growth patterns. Lipid-rich cells of fraction I expressed TGFbeta-R1 and produced significantly more cortisol relative to androstenedione than unseparated or fraction II cells, whereas lipid-poor cells of fraction II expressed HLA-DR and produced more androstenedione relative to cortisol in the presence of ACTH. Aldosterone production by fraction II was significantly greater than fraction I or unseparated cells. TGFbeta-R1-positive fasciculata-type cells separated into fraction I and HLA-DR-positive cells consistent with reticularis cells separated into fraction II. Aldosterone-producing cells indicative of glomerulosa cells separated into fraction II. CONCLUSIONS: Our findings are consistent with the concept that all adrenocortical cells are capable of producing a range of steroids, but the relative production of cortisol, androgen and aldosterone differs.