The FLC dimer with lambda type may false-migrate to the position of "albumin" band by urine protein electrophoresis on Sebia agarose gel-based detection system.


Journal

Journal of clinical laboratory analysis
ISSN: 1098-2825
Titre abrégé: J Clin Lab Anal
Pays: United States
ID NLM: 8801384

Informations de publication

Date de publication:
Feb 2019
Historique:
received: 15 06 2018
revised: 21 07 2018
accepted: 01 08 2018
pubmed: 29 8 2018
medline: 12 3 2019
entrez: 29 8 2018
Statut: ppublish

Résumé

Monoclonal free light chains (FLC) commonly exist in monomeric or dimeric forms but rarely as larger molecules. Little is known about whether polymeric molecules can affect urine protein electrophoresis (UPE) results. Urine samples were collected from 72 multiple myeloma (MM) patients with Bence Jones protein (BJP). Urine protein and immunofixation electrophoresis were analyzed on Sebia SDS "agarose" gel electrophoresis system (SDS-AGE), and immunoglobulin free light chains were measured on the BNII nephelometric assay. A type of disulfide-bound FLC dimer shows a pattern shift to the position of the "albumin" band in urine protein electrophoresis in multiple myeloma (MM) patients according to the Sebia agarose gel-based detection system, which was validated by immunofixation, SDS-PAGE, and mass spectrometric methods. Similar cases were found in 21 (29.17%) of 72 MM patients with BJP, and 19 (90.5%) of 21 patients were the lambda type. These results indicate that BJP with lambda type has a strong tendency to abnormally migrate, which may increase the risk of misinterpretation of protein electrophoresis in clinics. Thus, when the urine protein electrophoresis is inconsistent with the result by nephelometric method, urine protein electrophoresis needs to be repeated on the deduced condition to confirm the essence of the originally identified "albumin."

Sections du résumé

BACKGROUND BACKGROUND
Monoclonal free light chains (FLC) commonly exist in monomeric or dimeric forms but rarely as larger molecules. Little is known about whether polymeric molecules can affect urine protein electrophoresis (UPE) results.
METHODS METHODS
Urine samples were collected from 72 multiple myeloma (MM) patients with Bence Jones protein (BJP). Urine protein and immunofixation electrophoresis were analyzed on Sebia SDS "agarose" gel electrophoresis system (SDS-AGE), and immunoglobulin free light chains were measured on the BNII nephelometric assay.
RESULTS RESULTS
A type of disulfide-bound FLC dimer shows a pattern shift to the position of the "albumin" band in urine protein electrophoresis in multiple myeloma (MM) patients according to the Sebia agarose gel-based detection system, which was validated by immunofixation, SDS-PAGE, and mass spectrometric methods. Similar cases were found in 21 (29.17%) of 72 MM patients with BJP, and 19 (90.5%) of 21 patients were the lambda type.
CONCLUSIONS CONCLUSIONS
These results indicate that BJP with lambda type has a strong tendency to abnormally migrate, which may increase the risk of misinterpretation of protein electrophoresis in clinics. Thus, when the urine protein electrophoresis is inconsistent with the result by nephelometric method, urine protein electrophoresis needs to be repeated on the deduced condition to confirm the essence of the originally identified "albumin."

Identifiants

pubmed: 30152095
doi: 10.1002/jcla.22658
pmc: PMC6818555
doi:

Substances chimiques

Disulfides 0
Immunoglobulin Light Chains 0
Bence Jones Protein 9006-99-9

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e22658

Informations de copyright

© 2018 Wiley Periodicals, Inc.

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Auteurs

Changqiang Chen (C)

Department of Clinical Laboratory, Ruijin Hospital North, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Peizhan Chen (P)

Translational Medicine Research Center, Ruijin Hospital North, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Xuqian Fang (X)

Department of Pathology, Ruijin Hospital North, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

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Classifications MeSH