Urine Protein Electrophoresis and Immunoelectrophoresis Using Unconcentrated or Minimally Concentrated Urine Samples

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1 Immunopathology / Electrophoresis of Unconcentrated Urine Samples Urine Protein Electrophoresis and Immunoelectrophoresis Using Unconcentrated or Minimally Concentrated Urine Samples Anja C. Roden, MD, Karen S. Lockington, MT, Linda J. Tostrud, MT, and Jerry A. Katzmann, PhD Key Words: Protein electrophoresis; Immunoelectrophoresis; Unconcentrated urine; Urine; Immunofixation; Monoclonal gammopathy; M protein DOI: /6K33KTFA7A5VUQ1T Abstract Our objective was to evaluate a gel system that uses unconcentrated urine specimens for protein electrophoresis (PEL) and immunofixation electrophoresis (IFE) in patients with monoclonal gammopathies. For the study, 222 urine specimens were analyzed by our current PEL method (Helena Laboratories, Beaumont, TX) and by a system that recommends use of unconcentrated urine (Sebia, Norcross, GA). M protein concentrations were compared in the 43 cases with a measurable M spike. IFE was performed on 111 of the samples using both methods. There was a 97% concordance for detection of PEL abnormalities. The concordance for IFE was 98%. M protein concentrations by the 2 methods correlated well (r 2 = 0.99; slope, 1.04). Cases with insufficient urine volumes for concentration (PEL, 7; IFE, 20) were analyzed in the Sebia gel system, and in 11 cases (PEL, 2; IFE, 9) an M protein was identified. High-resolution gel electrophoresis of urine using the Sebia system offers similar performance for detection, characterization, and quantification of M proteins when compared with our current gel system. Testing unconcentrated urine specimens will mean fewer sample rejections owing to insufficient sample volume. Analysis of serum and urine samples is important for the diagnosis and monitoring of patients with monoclonal gammopathies. 1 Although agarose gel electrophoresis and capillary zone electrophoresis are the common screening methods for monoclonal proteins (M proteins), immunofixation electrophoresis (IFE) is more sensitive and is required to confirm the presence of a serum M protein and to characterize its heavy chain and light chain type. 1 Furthermore, if urine is assessed, it is recommended that urine be adequately concentrated to increase diagnostic sensitivity. 2 Although most monoclonal gammopathies can be detected, characterized, and monitored with serum assays, some plasma cell proliferative disorders synthesize and secrete monoclonal free light chain or heavy chain fragments. The products of these clonal plasma cells are of relatively small molecular weight and may be readily cleared from blood. To detect and/or monitor these abnormalities, it may be necessary to test urine samples. Monoclonal light chains in patients with diseases such as primary amyloidosis can be detected by serum IFE with a sensitivity of 80% to 85%. Inclusion of urine IFE increases this sensitivity to 90% to 95%. Recent reports of the sensitivity of a diagnostic panel that includes serum protein electrophoresis (PEL), IFE, and free light chain quantitation have indicated that the diagnostic sensitivity of this expanded serum panel is equal to that of serum plus urine tests. 3 Even after serum studies diagnose an M protein, however, urine tests are still required to evaluate the urine total protein and the distribution of the urinary proteins. The Sebia High-Resolution Gel Electrophoresis (HRGE) (Sebia, Norcross, GA), an agarose gel electrophoresis method for unconcentrated urine, has been reported to be a simple Am J Clin Pathol 2008;130: DOI: /6K33KTFA7A5VUQ1T 141

2 Roden et al / Electrophoresis of Unconcentrated Urine Samples and reliable method for quantitation of Bence Jones proteins. 4 Because unconcentrated urine can be used to monitor urine M spikes and because serum free light chain assays can identify many of the monoclonal light chain cases missed by serum IFE, we evaluated the use of unconcentrated urine in the Sebia agarose gel system. To obtain sufficient sensitivity, our clinical laboratory currently concentrates urine specimens from 10- to 200- fold before performing PEL and IFE. The concentration factors depend on the initial urine total protein concentration. Concentrating urine specimens takes from 10 minutes (10-fold) to 45 minutes (200-fold), with many requiring several hours to concentrate. The larger concentration factors require the transfer of the specimen to a new tube once or twice during the process, and labeling errors or sample mixups may be introduced. Furthermore, to achieve a large concentration, a large original sample volume is required, and this required volume is not always available. Low-volume specimens are especially frequent with random samples. If additional sample has to be requested, it prolongs the turnaround time (TAT) of the overall test, and if no additional sample is available, the specimen must be rejected. The introduction of urine PEL and IFE methods that use unconcentrated urine specimens and offer performance similar to that of the current methods would decrease errors, improve TAT, eliminate the cost of concentrators, decrease labor for technicians, and reduce test cancellations owing to insufficient sample volume. In the present study, we assessed the Sebia HRGE for PEL and IFE using unconcentrated urine specimens and compared results with our current methods using concentrated urine specimens and the Helena gel system (Helena Laboratories, Beaumont, TX). The aim of our study was to evaluate a method change in regard to analytic performance. samples were concentrated to achieve a final protein concentration between 1.7 and 8.0 g/dl. Urine specimens were concentrated with Vivaspin 20 concentrators (Vivascience, Littleton, MA). Samples were placed in the concentrators and centrifuged at 20 C until the volume had been appropriately reduced. Concentration factors of 10, 20, 40, 80, 100, or 200 were determined from the original protein concentration ztable 1z. All 222 specimens required concentration. However, some specimens (PEL, 7; IFE, 20) did not have sufficient volume to concentrate and, therefore, could be tested only by the Sebia method. PEL and IFE by Current Methods (Concentrated) PEL and IFE were performed with concentrated urine as described in the previous section. PEL was performed by agarose gel electrophoresis (SPIFE SPE, Helena Laboratories). IFE was done if ordered by the clinician or if an M protein was identified by PEL and it was the first time the patient was being tested. IFE was performed with antisera to γ, α, µ, κ, and λ immunoglobulin chains (SPIFE ImmunoFix-15, Helena Laboratories). The results from PEL and IFE were reported to the patient s medical records. PEL and IFE by Sebia Gel Electrophoresis Unconcentrated or minimally concentrated (10 ) urine samples were used with the Sebia gels. Urine samples with initial protein concentrations of more than 16 mg/dl were not concentrated. If the urine sample had a protein concentration between 0 and 16 mg/dl, the specimen was concentrated 10-fold. For simplicity, unconcentrated and 10-fold concentrated urine specimens are referred to as unconcentrated in this article. PEL was performed on all specimens (Hydragel 15 HR, Sebia). If IFE was performed by the clinical laboratory or if the Sebia PEL revealed an M protein, Sebia IFE (Hydragel 9IF, Sebia) was done. Materials and Methods Specimens All specimens received on 2 consecutive days in February 2007 at the Clinical Immunology Laboratory, Mayo Clinic, Rochester, MN, for urine electrophoresis were included in the study (n = 222). If available and pertinent to the study, medical records were reviewed. The study was approved by the Mayo Institutional Review Board. Specimen Preparation Urine protein concentration was measured by colorimetric dye binding on a Hitachi 911 (Roche Diagnostics, Indianapolis, IN). Before we concentrated any of the urine specimens, an aliquot was reserved for additional electrophoresis. Urine ztable 1z Laboratory Guide for Sample Volume and Concentration Factors Required for Final Concentrations of Approximately 2 to 8.0 g/dl and Final Volumes of 100 to 200 µl Urine Protein Urine Concentration Final Concentration (mg/dl) Volume (ml) Factor Volume (µl) > Am J Clin Pathol 2008;130: DOI: /6K33KTFA7A5VUQ1T

3 Immunopathology / Original Article Quantitation of M Protein To quantitate any M protein peaks detected on the PEL gels, gels were scanned and fractionated by using the Helena Quick Scan 2000 densitometer, Helena Laboratories. The amount of urinary M protein was calculated by multiplying the M protein fraction with the urine protein concentration or the 24-hour urine total protein value. The percentage difference compared with the M spike evaluated on the Sebia gel was calculated, and linear regression analysis was performed. Interpretation of Gels All clinical laboratory PEL and IFE gels were reviewed by 2 technicians and one of the laboratory directors. All Sebia gels were reviewed by the authors. Results generated by the clinical laboratory were compared with results generated on the Sebia system and assessed for concordant monoclonal protein patterns. If one gel system contained a single abnormality and the other gel system had 2 abnormalities, we assumed that these were monomers and dimers and defined them as concordant. Results In an effort to determine whether identification of M proteins by PEL is similar between our current method using concentrated urine specimens and the Sebia urine gels using unconcentrated or 10 concentrated urine specimens, PEL assays were evaluated from 222 specimens. A direct comparison was possible in 215 (96.8%) of 222 specimens. These results are summarized in ztable 2z. Results were concordant in 209 (97.2%) of 215 specimens. The Helena PEL method had 2 false-positive results and 1 false-negative result (98% specificity and 99% sensitivity compared with Helena IFE). The false-negative sample had a protein concentration of 3 mg/dl, and an M protein was detected by IFE. The Sebia gels had no false-positives but had 3 falsenegatives with protein concentrations of 17, 20, and 88 mg/dl (100% specificity and 97% sensitivity compared with Helena IFE). Two of the concordant results contained 1 electrophoretic abnormality on the Sebia gel and 2 on the Helena gel. In 7 (3.2%) of 222 urine specimens, the sample volume was too small to concentrate. These urine specimens were assessed in the Sebia PEL system and 2 (29%) of 7 specimens contained an M protein that was confirmed by IFE. Sebia IFE was performed on 111 samples that had an IFE performed by the clinical laboratory. In 109 (98.2%) of 111 specimens, there was concordance. These results are summarized in ztable 3z. Two samples were discordant, and these 2 false-negative results were among 55 urine specimens with an M protein identified in the Helena system (96% sensitivity compared with Helena IFE). Four of the concordant results had 1 M protein identified in the Sebia gel system and dimers of identical heavy and light chain in the Helena gel. In 20 additional specimens, the available urine sample volume was insufficient for the clinical laboratory to perform IFE. In 9 (45%) of these 20 specimens, we identified an M protein on the Sebia IFE gel system, and 1 specimen showed an equivocal pattern. If a discrete M spike was identified and fractionated on both PEL gels, the gels were scanned to quantitate the M protein. The amount of urinary M protein was calculated as milligrams per 24 hours or as milligrams per deciliter if only a random urine sample was available. In 43 cases, M protein quantification was available from both methods. The percentage difference in M protein concentrations derived from the 2 methods was 104%. A regression analysis was performed and is shown in zfigure 1z. The linear regression of the M spikes derived from the 2 methods had a slope of 1.04 and a correlation coefficient of 99%. ztable 2z Comparison of PEL Interpretation on the Helena Gel System With the Sebia Gel System * Protein, mg/dl Total (n = 100) (n = 32) (n = 38) (n = 18) (n = 21) (n = 6) (n = 215) Concordant PEL (97.2%) Positive Negative Discordant PEL (2.8%) False-negative, unconcentrated False-positive, concentrated False-negative, concentrated IFE, immunofixation electrophoresis; PEL, protein electrophoresis. * True-positive and true-negative results were determined by the Sebia IFE gel method using concentrated urine specimens and Helena IFE gels. Of the 222 sequential urine samples submitted to the laboratory, 7 were rejected owing to insufficient volume to allow sample concentration. Helena Laboratories, Beaumont, TX; Sebia, Norcross, GA. Am J Clin Pathol 2008;130: DOI: /6K33KTFA7A5VUQ1T 143

4 Roden et al / Electrophoresis of Unconcentrated Urine Samples ztable 3z Comparison of IFE Interpretation on the Helena Gel System With the Sebia Gel System * Protein, mg/dl Total (n = 56) (n = 16) (n = 17) (n = 9) (n = 10) (n = 3) (n = 111) Concordant IFE (98.2%) Positive Negative Discordant IFE False-negative, unconcentrated (1.8%) IFE, immunofixation electrophoresis. * Helena Laboratories, Beaumont, TX; Sebia, Norcross, GA. Discussion Urine protein studies are important in the diagnosis and management of monoclonal gammopathies. Because of our patient population with dysproteinemia, our clinical laboratory has a large number of urine PEL assays that also require IFE to be performed. For sufficient sensitivity and specificity, our current methods require the concentration of the urine, a process that can be time-consuming and labor-intensive and has the potential to introduce errors. Therefore, a method that can use unconcentrated or minimally concentrated urine specimens while offering similar sensitivity and specificity would be desirable. Evidence suggests that the Sebia HRGE that uses longer sample application time and slower separation might provide such a method. 1 Early in this study we recognized that most of the lowprotein samples were negative on the Sebia gel if tested neat. Therefore, all specimens with a protein concentration 16 mg/ dl or less were concentrated 10-fold, and only the results Urine M Protein by HRGE (mg/24 h or mg/dl) 5,000 4,000 3,000 2,000 1, ,000 2,000 3,000 4,000 5,000 Urine M Protein by CM (mg/24 h or mg/dl) zfigure 1z Comparison of urinary M protein excretion by protein electrophoresis using the Helena gel system (current method [CM]) vs the Sebia High-Resolution Gel Electrophoresis system (HRGE) (n = 43). y = 1.041x ; R 2 = Helena Laboratories, Beaumont, TX; Sebia, Norcross, GA. from the 10-fold concentrated specimens in this group of specimens were included in the analysis. Our final results, however, suggest that we may have to change our cutoff levels for the 10-fold concentration of urine specimens to 25 mg/dl because of 2 false-negative results in this protein concentration range. We found a 97% concordance in the identification of M protein using concentrated urine specimens vs unconcentrated or minimally concentrated urine specimens. The 6 discordant specimens had relatively low total protein concentrations (between 3 and 88 mg/dl). Concentrating urine 10-fold requires approximately 10 minutes (vs at least 45 minutes for a 200-fold concentration). Furthermore, instead of using a 20-mL concentrator, we would use a less expensive 4-mL concentrator. In addition, 1 round of centrifugation would be sufficient in comparison with at least 2 rounds with the 200-fold concentration. Overall, even if we will need to concentrate urine specimens with a protein concentration of 25 mg/dl or less, it will shorten the TAT and lower the overall costs of the assay. The concordance of IFE between concentrated and unconcentrated urine specimens was also very high (98%). Two unconcentrated samples were false-negatives on the Sebia gels. Both samples had a protein concentration of 16 mg/dl or less but were concentrated 10-fold before use by HRGE. In a few specimens (PEL, 2; IFE, 4), the current method revealed 2 distinct M proteins; however, only 1 band was found with the Sebia method. We defined these cases as concordant. However, we realize that although the identification of an abnormality was concordant, we potentially may not recognize an M protein band. The M protein bands using unconcentrated urine and the Sebia gel system are sometimes broader and fuzzier than on our current gels using concentrated urine. This may result in 2 closely migrating proteins being hidden within a broader electrophoretic band. This is likely due to the slower protein separation and the possibility for increased diffusion. M protein quantitation is an essential feature in the laboratory assessment of monoclonal gammopathies and in the 144 Am J Clin Pathol 2008;130: DOI: /6K33KTFA7A5VUQ1T

5 Immunopathology / Original Article monitoring of disease progression or response to treatment. Therefore, the relationship of the M protein concentrations derived from both methods is important. Our results show a linear regression slope of 1.04 between M protein quantitation by both methods. This nearly identical quantitation means that no crossover studies will be necessary as patients are monitored by changed methods. A significant advantage of the use of the Sebia gel system is the lower sample volume required. In this study, a total of 7 specimens for PEL and 20 specimens for IFE did not have sufficient sample to be concentrated, but the urine volume was enough for analysis by the Sebia gel method. In several of these small-volume specimens (n = 11) we identified an M protein. A small sample volume often results in test cancellation if no additional urine is available. Although overall results between the 2 methods compared well, the introduction of Sebia gels using unconcentrated or 10-fold concentrated urine will require a considerable amount of education and practice in interpreting gel patterns. In this system, M proteins can sometimes have a broader and fuzzier appearance than with our current method. This is likely due to the slower separation of the proteins, a feature intentionally applied to this method to increase the sensitivity. In 3 of 43 specimens, we were unable to quantitate an M peak on the Sebia gel because of a fuzzy band that appeared as a discrete M spike on the Helena gel system. It is interesting that there were also 3 specimens in which we were unable to calculate an M protein concentration from our current gel system because they appeared as fuzzy bands but were discrete M proteins on Sebia gels. Our study demonstrates that the Sebia gel system is similar in detection and quantitation of M proteins when compared with the Helena gel system using concentrated urine specimens. The introduction of this new method in our clinical immunology laboratory will provide a method that potentially reduces transfer errors, allows testing of low-volume urine samples, improves TAT, and reduces costs. From the Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN. Address reprint requests to Dr Katzmann: 200 First St SW, Rochester MN, References 1. International Myeloma Working Group. Criteria for the classification of monoclonal gammopathies, multiple myeloma and related disorders: a report of the International Myeloma Working Group. Br J Haematol. 2003;121: Keren DF. Detection and characterization of monoclonal components in serum and urine. Clin Chem. 1998;44(6 pt 1): Katzmann JA, Dispenzieri A, Kyle RA, et al. Elimination of the need for urine studies in the screening algorithm for monoclonal gammopathies by using serum immunofixation and free light chain assays. Mayo Clin Proc. 2006;81: Salomo M, Gimsing P, Nielsen LB. Simple method for quantification of Bence Jones proteins. Clin Chem. 2002;48: Am J Clin Pathol 2008;130: DOI: /6K33KTFA7A5VUQ1T 145

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