The Laboratory Investigation of Paraproteinaemia

Whicher, J T; Calvin, J.; Riciies, P; Warren, Christine

doi:10.1177/000456328702400201

Cited by 56 publications

(33 citation statements)

References 26 publications

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“…There are no strict guidelines as to when an M-spike is too small relative to the underlying polyclonal immunoglobulins to permit accurate measurement by the Unfortunately, while the tangent method works well in the γ region, M-proteins can migrate anywhere in the electrophoretic pattern [51]. When they are occur in the α-, β-or β-γ region, the presence of other serum proteins such as transferrin and C3 alter the shape of the trace where the M-spike would have met polyclonal immunoglobulin and instead the intersection of monoclonal and polyclonal immunoglobulin is hidden under non-immunoglobulin protein.…”

Section: Detection and Measurement Of M-proteins In Serum By Protein mentioning

confidence: 99%

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Challenges of measuring monoclonal proteins in serum

Keren

Schroeder

2016

Clinical Chemistry and Laboratory Medicine (CCLM)

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Abstract:The measurement of monoclonal protein (M-protein) is vital for stratifying risk and following individuals with a variety of monoclonal gammopathies. Direct measurement of the M-protein spike by electrophoresis and immunochemical measurements of specific isotypes or free light chains pairs has provided useful information about the quantity of M-protein. Nonetheless, both traditional electrophoresis and immunochemical methods give poor quantification with M-proteins smaller than 10 g/L (1 g/dL) when in the presence of polyclonal immunoglobulins that co-migrate with the M-protein. In addition, measurements by electrophoresis of M-proteins migrating in the β-and α-regions are contaminated by normal serum proteins in those regions. The most precise electrophoretic method to date for quantification involves exclusion of the polyclonal immunoglobulins by using the tangent skimming method on electropherograms, which provides a 10-fold improvement in precision. So far, however, tangent measurements are limited to γ migrating M-proteins. Another way to improve M-protein measurements is the use of capillary electrophoresis (CE). With CE, one can employ immunosubtraction to select a region of interest in the β region thereby excluding much of the normal proteins from the M-protein measurement. Recent development of an immunochemical method distinguishing heavy/light chain pairs (separately measuring IgGK and IgGL, IgAK and IgAL, and IgMK and IgML) provides measurements that could exclude polyclonal contaminants of the same heavy chain with the uninvolved light chain type. Yet, even heavy/light results contain an immeasurable quantity of polyclonal heavy/ light chains of the involved isotype. Finally, use of liquid chromatography-tandem mass spectrometry (LC-MS/MS) looms on the horizon as a means to provide more consistent and sensitive measurements of M-proteins.

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Section: Detection and Measurement Of M-proteins In Serum By Protein mentioning

confidence: 99%

“…But many reflect the presence of posttranslational modifications and/or polymerization. IgA and IgM M-proteins are particularly prone to polymerize [51].…”

Section: A B Cmentioning

confidence: 99%

Challenges of measuring monoclonal proteins in serum

Keren

Schroeder

2016

Clinical Chemistry and Laboratory Medicine (CCLM)

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“…Separation of serum protein fractions is very important for the diagnosis of many different diseases, including paraproteinaemias, immune deficiency, and various protein abnormalities (Whicher et al 1987). Identifying and quantifying protein fractions and determining the physiologic serum protein electrophoretic patterns enable the identification of animals with altered serum protein pattern, which may reflect responses to changes in homeostasis or disease (Alberghina et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Age-related changes in the concentrations of serum proteins in calves

Nagy

Tóthová

Kováč

2014

Journal of Applied Animal Research

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The objective of this study was to describe the physiological differences in serum protein electrophoretic pattern in calves at different ages and nutrition. One hundred and one clinically healthy calves at the age from 2 weeks till 6 months were included into the study. On the basis of their age and age-related feeding management, the calves were divided into five groups (calves at the age of 2 weeks, 1 month, 2, 3-4, and 5-6 months). Blood samples were taken by direct puncture of v. jugularis. Blood serum was analyzed for total serum protein concentrations, the relative and absolute values of protein fractions (albumin, alpha 1 [α 1 ]-, alpha 2 [α 2 ]-, beta 1 [β 1 ]-, beta 2 [β 2 ]-, and gamma [γ]-globulins) with calculation of albumin:globulin ratios. The results showed a significant effect of age and changes in nutrition on the serum total protein (TP) concentrations and the most of protein fractions. Significantly higher relative concentrations of albumin, α-globulins (predominantly α 2 ), as well as β 1 -globulins were found in younger calves compared with older animals (P < 0.001, P < 0.001, and P < 0.001, respectively). On the other hand, the relative values of β 2 -, γ-globulins, and TPs were significantly lower in younger calves than in older ones (P < 0.05, P < 0.001, and P < 0.001, respectively). Therefore, it is essential to determine the physiological serum protein electrophoretic pattern in different age groups of calves, because these reflect the physiological response of animals to changes in nutrition, growth or development. Our results suggest that the age of animals should be taken into consideration when interpreting the serum protein profile.

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“…The wide range of possible concentrations of monoclonal proteins also makes the inclusion of robust antigen excess checks vital for quantitative assays where monoclonal proteins may be seen. 6 Overall, the results given in immunoassays for monoclonal Igs generally do not provide an accurate quanti¢cation. 7 We assess broad assay reliability by participation in EQA.…”

mentioning

confidence: 99%

Free light chains

Sheldon

2007

Ann Clin Biochem

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The Laboratory Investigation of Paraproteinaemia

Cited by 56 publications

References 26 publications

Challenges of measuring monoclonal proteins in serum

Challenges of measuring monoclonal proteins in serum

Age-related changes in the concentrations of serum proteins in calves

Free light chains

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