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Article ; Online: FLC polymerization: Another hurdle towards standardization of FLC measurements.

Kaplan, Batia / Jacobs, Joannes F M

Clinica chimica acta; international journal of clinical chemistry

2021 Volume 515, Page(s) 42–43

Abstract: In the November issue of this journal, Caponi et al. convincingly show that free light chain (FLC) lambda measurements are influenced by the FLC-polymerization status. With liquid chromatography using a size-exclusion column they separated monoclonal FLC ...

Abstract	In the November issue of this journal, Caponi et al. convincingly show that free light chain (FLC) lambda measurements are influenced by the FLC-polymerization status. With liquid chromatography using a size-exclusion column they separated monoclonal FLC dimers from monomers. FLC analysis of these different fractions clearly indicated that Freelite (The Binding Site) reacted better with FLC dimers than with FLC monomers. In contrast, N Latex FLC (Siemens) recognizes mainly FLC monomers and has poor reactivity with the FLC dimers. This important finding may be one of the leading factors to explain discrepancies in FLC-quantification using Freelite versus other immunochemical assays such as N-Latex FLC.
MeSH term(s)	Humans ; Immunoglobulin Light Chains ; Immunoglobulin kappa-Chains ; Immunoglobulin lambda-Chains ; Latex ; Polymerization ; Reference Standards
Chemical Substances	Immunoglobulin Light Chains ; Immunoglobulin kappa-Chains ; Immunoglobulin lambda-Chains ; Latex
Language	English
Publishing date	2021-01-01
Publishing country	Netherlands
Document type	Letter
ZDB-ID	80228-1
ISSN	1873-3492 ; 0009-8981
ISSN (online)	1873-3492
ISSN	0009-8981
DOI	10.1016/j.cca.2020.12.030
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Article: Amyloid Typing in Cardiac Amyloidosis Using Western Blotting.

Kaplan, Batia / Goldis, Rivka / Ziv, Tamar / Dori, Amir / Magen, Hila / Simon, Amos J / Volkov, Alexander / Maor, Elad / Arad, Michael

The Israel Medical Association journal : IMAJ

2024 Volume 26, Issue 3, Page(s) 149–156

Abstract: Background: Cardiac amyloidosis (CA) is characterized by the extracellular deposition of misfolded protein in the heart. Precise identification of the amyloid type is often challenging, but critical, since the treatment and prognosis depend on the ... ...

Abstract	Background: Cardiac amyloidosis (CA) is characterized by the extracellular deposition of misfolded protein in the heart. Precise identification of the amyloid type is often challenging, but critical, since the treatment and prognosis depend on the disease form and the type of deposited amyloid. Coexistence of clinical conditions such as old age, monoclonal gammopathy, chronic inflammation, or peripheral neuropathy in a patient with cardiomyopathy creates a differential diagnosis between the major types of CA: amyloidosis light chains (AL), amyloidosis transthyretin (ATTR) and amyloidosis A (AA). Objectives: To demonstrate the utility of the Western blotting (WB)-based amyloid typing method in patients diagnosed with cardiac amyloidosis where the type of amyloid was not obvious based on the clinical context. Methods: Congo red positive endomyocardial biopsy specimens were studied in patients where the type of amyloid was uncertain. Amyloid proteins were extracted and identified by WB. Mass spectrometry (MS) of the electrophoretically resolved protein-in-gel bands was used for confirmation of WB data. Results: WB analysis allowed differentiation between AL, AA, and ATTR in cardiac biopsies based on specific immunoreactivity of the electrophoretically separated proteins and their characteristic molecular weight. The obtained results were confirmed by MS. Conclusions: WB-based amyloid typing method is cheaper and more readily available than the complex and expensive gold standard techniques such as MS analysis or immunoelectron microscopy. Notably, it is more sensitive and specific than the commonly used immunohistochemical techniques and may provide an accessible diagnostic service to patients with amyloidosis in Israel.
MeSH term(s)	Humans ; Amyloidosis/diagnosis ; Amyloid/analysis ; Amyloid/metabolism ; Amyloidogenic Proteins ; Cardiomyopathies/diagnosis ; Blotting, Western ; Amyloid Neuropathies, Familial/pathology ; Prealbumin
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; Prealbumin
Language	English
Publishing date	2024-03-16
Publishing country	Israel
Document type	Journal Article
ZDB-ID	2008291-5
ISSN	1565-1088 ; 0021-2180
ISSN	1565-1088 ; 0021-2180
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Article: Multiple Myeloma with Systemic Amyloidosis: Serum Free Light Chain Dimerization Analysis in the Diagnosis of an Equivocal Case of Plasma Cell Dyscrasia.

Duek, Adrian / Kaplan, Batia / Segman, Yafit / Leiba, Merav

The Israel Medical Association journal : IMAJ

2021 Volume 23, Issue 7, Page(s) 459–461

MeSH term(s)	Amyloidosis/blood ; Amyloidosis/diagnosis ; Amyloidosis/physiopathology ; Bone Marrow Examination/methods ; Cardiomyopathies/diagnosis ; Cardiomyopathies/etiology ; Dexamethasone/administration & dosage ; Humans ; Immunoassay/methods ; Immunoglobulin Light Chains/blood ; Immunologic Factors/administration & dosage ; Lenalidomide/administration & dosage ; Male ; Middle Aged ; Multiple Myeloma/blood ; Multiple Myeloma/diagnosis ; Multiple Myeloma/physiopathology ; Nephelometry and Turbidimetry/methods ; Paraproteinemias/diagnosis ; Pelvic Bones/diagnostic imaging ; Pelvic Bones/pathology ; Protein Multimerization ; Tomography, X-Ray Computed/methods ; Treatment Outcome
Chemical Substances	Immunoglobulin Light Chains ; Immunologic Factors ; Dexamethasone (7S5I7G3JQL) ; Lenalidomide (F0P408N6V4)
Language	English
Publishing date	2021-07-12
Publishing country	Israel
Document type	Case Reports ; Journal Article
ZDB-ID	2008291-5
ISSN	1565-1088 ; 0021-2180
ISSN	1565-1088 ; 0021-2180
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Article ; Online: Personalized Disease Monitoring in Pediatric Onset Multiple Sclerosis Using the Saliva Free Light Chain Test.

Ganelin-Cohen, Esther / Tartakovsky, Evgeny / Klepfish, Ely / Golderman, Sizilia / Rozenberg, Ayal / Kaplan, Batia

Frontiers in immunology

2022 Volume 13, Page(s) 821499

Abstract: Background: Development of new safe methods of monitoring disease activity in the pediatric onset multiple sclerosis (POMS) is a challenging task, especially when trying to refrain from frequent MRI usage. In our recent study, the : Objectives: To ... ...

Abstract	Background: Development of new safe methods of monitoring disease activity in the pediatric onset multiple sclerosis (POMS) is a challenging task, especially when trying to refrain from frequent MRI usage. In our recent study, the Objectives: To assess utility of saliva FLC measurements for monitoring disease activity in POMS. Methods: We used semiquantitative Western blot analysis to detect immunoreactive FLC monomers and dimers and to calculate the intensity of their bands. Statistical tests included Firth logistic regression analysis suitable for small sample sizes, and Spearman's non-parametric correlation. Results: In Conclusions: Our results show the potential of the non-invasive saliva FLC test, as a new tool for monitoring the disease activity in POMS.
MeSH term(s)	Adult ; Biomarkers ; Child ; Humans ; Immunoglobulin Light Chains ; Immunoglobulin kappa-Chains ; Multiple Sclerosis/diagnosis ; Multiple Sclerosis/drug therapy ; Saliva
Chemical Substances	Biomarkers ; Immunoglobulin Light Chains ; Immunoglobulin kappa-Chains
Language	English
Publishing date	2022-04-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.821499
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Article ; Online: Diagnostic Challenges and Solutions in Systemic Amyloidosis.

Goldis, Rivka / Kaplan, Batia / Kukuy, Olga Lesya / Arad, Michael / Magen, Hila / Shavit-Stein, Efrat / Dori, Amir / Livneh, Avi

International journal of molecular sciences

2023 Volume 24, Issue 5

Abstract: Amyloidosis refers to a clinically heterogeneous group of disorders characterized by the extracellular deposition of amyloid proteins in various tissues of the body. To date, 42 different amyloid proteins that originate from normal precursor proteins and ...

Abstract	Amyloidosis refers to a clinically heterogeneous group of disorders characterized by the extracellular deposition of amyloid proteins in various tissues of the body. To date, 42 different amyloid proteins that originate from normal precursor proteins and are associated with distinct clinical forms of amyloidosis have been described. Identification of the amyloid type is essential in clinical practice, since prognosis and treatment regimens both vary according to the particular amyloid disease. However, typing of amyloid protein is often challenging, especially in the two most common forms of amyloidosis, i.e., the immunoglobulin light chain amyloidosis and transthyretin amyloidosis. Diagnostic methodology is based on tissue examinations as well as on noninvasive techniques including serological and imaging studies. Tissue examinations vary depending on the tissue preparation mode, i.e., whether it is fresh-frozen or fixed, and they can be carried out by ample methodologies including immunohistochemistry, immunofluorescence, immunoelectron microscopy, Western blotting, and proteomic analysis. In this review, we summarize current methodological approaches used for the diagnosis of amyloidosis and discusses their utility, advantages, and limitations. Special attention is paid to the simplicity of the procedures and their availability in clinical diagnostic laboratories. Finally, we describe new methods recently developed by our team to overcome limitations existing in the standard assays used in common practice.
MeSH term(s)	Humans ; Immunoglobulin Light-chain Amyloidosis ; Proteomics/methods ; Amyloid/metabolism ; Amyloid Neuropathies, Familial ; Amyloidogenic Proteins
Chemical Substances	Amyloid ; Amyloidogenic Proteins
Language	English
Publishing date	2023-02-28
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24054655
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Article ; Online: Diagnostic Challenges and Solutions in Systemic Amyloidosis

Rivka Goldis / Batia Kaplan / Olga (Lesya) Kukuy / Michael Arad / Hila Magen / Efrat Shavit-Stein / Amir Dori / Avi Livneh

International Journal of Molecular Sciences, Vol 24, Iss 4655, p

2023 Volume 4655

Abstract	Amyloidosis refers to a clinically heterogeneous group of disorders characterized by the extracellular deposition of amyloid proteins in various tissues of the body. To date, 42 different amyloid proteins that originate from normal precursor proteins and are associated with distinct clinical forms of amyloidosis have been described. Identification of the amyloid type is essential in clinical practice, since prognosis and treatment regimens both vary according to the particular amyloid disease. However, typing of amyloid protein is often challenging, especially in the two most common forms of amyloidosis, i.e., the immunoglobulin light chain amyloidosis and transthyretin amyloidosis. Diagnostic methodology is based on tissue examinations as well as on noninvasive techniques including serological and imaging studies. Tissue examinations vary depending on the tissue preparation mode, i.e., whether it is fresh-frozen or fixed, and they can be carried out by ample methodologies including immunohistochemistry, immunofluorescence, immunoelectron microscopy, Western blotting, and proteomic analysis. In this review, we summarize current methodological approaches used for the diagnosis of amyloidosis and discusses their utility, advantages, and limitations. Special attention is paid to the simplicity of the procedures and their availability in clinical diagnostic laboratories. Finally, we describe new methods recently developed by our team to overcome limitations existing in the standard assays used in common practice.
Keywords	amyloidosis ; amyloid typing ; free light chains ; free light chain dimers ; mass spectrometry ; transthyretin ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	610
Language	English
Publishing date	2023-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Diagnostic utility of kappa free light chains in multiple sclerosis.

Kaplan, Batia / Ganelin-Cohen, Esther / Golderman, Sizilia / Livneh, Avi

Expert review of molecular diagnostics

2019 Volume 19, Issue 4, Page(s) 277–279

MeSH term(s)	Humans ; Immunoglobulin Light Chains/cerebrospinal fluid ; Immunoglobulin Light Chains/isolation & purification ; Immunoglobulin kappa-Chains/cerebrospinal fluid ; Immunoglobulin kappa-Chains/isolation & purification ; Multiple Sclerosis/cerebrospinal fluid ; Multiple Sclerosis/diagnosis ; Multiple Sclerosis/pathology ; Nephelometry and Turbidimetry
Chemical Substances	Immunoglobulin Light Chains ; Immunoglobulin kappa-Chains
Language	English
Publishing date	2019-02-27
Publishing country	England
Document type	Journal Article
ZDB-ID	2112530-2
ISSN	1744-8352 ; 1473-7159
ISSN (online)	1744-8352
ISSN	1473-7159
DOI	10.1080/14737159.2019.1586535
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Article ; Online: Amino acid sequence homology of monoclonal serum free light chain dimers and tissue deposited light chains in AL amyloidosis: a pilot study.

Goldis, Rivka / Kaplan, Batia / Arad, Michael / Dispenzieri, Angela / Dasari, Surendra / Kukuy, Olga Lesya / Simon, Amos J / Dori, Amir / Shavit-Stein, Efrat / Ziv, Tamar / Murray, David / Kourelis, Taxiarchis / Gertz, Morie A / Dominissini, Dan / Magen, Hila / Muchtar, Eli

Clinical chemistry and laboratory medicine

2023 Volume 62, Issue 3, Page(s) 464–471

Abstract: Objectives: Diagnosis of light chain amyloidosis (AL) requires demonstration of amyloid deposits in a tissue biopsy followed by appropriate typing. Previous studies demonstrated increased dimerization of monoclonal serum free light chains (FLCs) as a ... ...

Abstract	Objectives: Diagnosis of light chain amyloidosis (AL) requires demonstration of amyloid deposits in a tissue biopsy followed by appropriate typing. Previous studies demonstrated increased dimerization of monoclonal serum free light chains (FLCs) as a pathological feature of AL. To further examine the pathogenicity of FLC, we aimed at testing amino acid sequence homology between circulating and deposited light chains (LCs). Methods: Matched tissue biopsy and serum of 10 AL patients were subjected to tissue proteomic amyloid typing and nephelometric FLC assay, respectively. Serum FLC monomers (M) and dimers (D) were analyzed by Western blotting (WB) and mass spectrometry (MS). Results: WB of serum FLCs showed predominance of either κ or λ type, in agreement with the nephelometric assay data. Abnormal FLC M-D patterns typical of AL amyloidosis were demonstrated in 8 AL-λ patients and in one of two AL-κ patients: increased levels of monoclonal FLC dimers, high D/M ratio values of involved FLCs, and high ratios of involved to uninvolved dimeric FLCs. MS of serum FLC dimers showed predominant constant domain sequences, in concordance with the tissue proteomic amyloid typing. Most importantly, variable domain sequence homology between circulating and deposited LC species was demonstrated, mainly in AL-λ cases. Conclusions: This is the first study to demonstrate homology between circulating FLCs and tissue-deposited LCs in AL-λ amyloidosis. The applied methodology can facilitate studying the pathogenicity of circulating FLC dimers in AL amyloidosis. The study also highlights the potential of FLC monomer and dimer analysis as a non-invasive screening tool for this disease.
MeSH term(s)	Humans ; Pilot Projects ; Sequence Homology, Amino Acid ; Proteomics ; Immunoglobulin Light-chain Amyloidosis/diagnosis ; Immunoglobulin Light Chains ; Amyloidosis/diagnosis ; Amyloidogenic Proteins ; Immunoglobulin lambda-Chains
Chemical Substances	Immunoglobulin Light Chains ; Amyloidogenic Proteins ; Immunoglobulin lambda-Chains
Language	English
Publishing date	2023-09-26
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1418007-8
ISSN	1437-4331 ; 1434-6621 ; 1437-8523
ISSN (online)	1437-4331
ISSN	1434-6621 ; 1437-8523
DOI	10.1515/cclm-2023-0591
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Article ; Online: Cerebrospinal fluid kappa free light chains for the diagnosis of multiple sclerosis: A consensus statement.

Hegen, Harald / Arrambide, Georgina / Gnanapavan, Sharmilee / Kaplan, Batia / Khalil, Michael / Saadeh, Ruba / Teunissen, Charlotte / Tumani, Hayrettin / Villar, Luisa Maria / Willrich, Maria Alice V / Zetterberg, Henrik / Deisenhammer, Florian

Multiple sclerosis (Houndmills, Basingstoke, England)

2022 Volume 29, Issue 2, Page(s) 182–195

Abstract: Cerebrospinal fluid (CSF) analysis is of utmost importance for diagnosis and differential diagnosis of patients with suspected multiple sclerosis (MS). Evidence of intrathecal immunoglobulin G (IgG) synthesis proves the inflammatory nature of the disease, ...

Abstract	Cerebrospinal fluid (CSF) analysis is of utmost importance for diagnosis and differential diagnosis of patients with suspected multiple sclerosis (MS). Evidence of intrathecal immunoglobulin G (IgG) synthesis proves the inflammatory nature of the disease, increases diagnostic certainty and substitutes for dissemination in time according to current diagnostic criteria. The gold standard to determine intrathecal IgG synthesis is the detection of CSF-restricted oligoclonal bands (OCBs). However, advances in laboratory methods brought up κ-free light chains (FLCs) as a new biomarker, which are produced in excess over intact immunoglobulins and accumulate in CSF in the case of central nervous system-derived inflammation. Overwhelming evidence showed a high diagnostic accuracy of intrathecal κ-FLC synthesis in MS with sensitivity and specificity of approximately 90% similar to OCB. κ-FLCs have advantages as its detection is fast, easy, cost-effective, reliable, rater-independent and returning quantitative results which might also improve the value of predicting MS disease activity. An international panel of experts in MS and CSF diagnostics developed a consensus of all participants. Six recommendations are given for establishing standard CSF evaluation in patients suspected of having MS. The panel recommended to include intrathecal κ-FLC synthesis in the next revision of MS diagnostic criteria as an additional tool to measure intrathecal immunoglobulin synthesis.
MeSH term(s)	Humans ; Multiple Sclerosis/diagnosis ; Multiple Sclerosis/cerebrospinal fluid ; Immunoglobulin kappa-Chains/cerebrospinal fluid ; Immunoglobulin G/cerebrospinal fluid ; Biomarkers/cerebrospinal fluid ; Sensitivity and Specificity ; Oligoclonal Bands/cerebrospinal fluid
Chemical Substances	Immunoglobulin kappa-Chains ; Immunoglobulin G ; Biomarkers ; Oligoclonal Bands
Language	English
Publishing date	2022-12-17
Publishing country	England
Document type	Journal Article
ZDB-ID	1290669-4
ISSN	1477-0970 ; 1352-4585
ISSN (online)	1477-0970
ISSN	1352-4585
DOI	10.1177/13524585221134217
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Article ; Online: Cerebrospinal fluid kappa free light chains for the diagnosis of multiple sclerosis: A systematic review and meta-analysis.

Hegen, Harald / Walde, Janette / Berek, Klaus / Arrambide, Georgina / Gnanapavan, Sharmilee / Kaplan, Batia / Khalil, Michael / Saadeh, Ruba / Teunissen, Charlotte / Tumani, Hayrettin / Villar, Luisa M / Willrich, Maria Alice V / Zetterberg, Henrik / Deisenhammer, Florian

Multiple sclerosis (Houndmills, Basingstoke, England)

2022 Volume 29, Issue 2, Page(s) 169–181

Abstract: Background: Intrathecal immunoglobulin-G synthesis is a hallmark of multiple sclerosis (MS), which can be detected by oligoclonal IgG bands (OCB) or by κ-free light chains (κ-FLC) in cerebrospinal fluid.: Objective: To perform a systematic review and ...

Abstract	Background: Intrathecal immunoglobulin-G synthesis is a hallmark of multiple sclerosis (MS), which can be detected by oligoclonal IgG bands (OCB) or by κ-free light chains (κ-FLC) in cerebrospinal fluid. Objective: To perform a systematic review and meta-analysis to evaluate whether κ-FLC index has similar diagnostic value to identify patients with clinically isolated syndrome (CIS) or MS compared to OCB, and to determine κ-FLC index cut-off. Methods: PubMed was searched for studies that assessed diagnostic sensitivity and specificity of κ-FLC index and OCB to discriminate CIS/MS patients from control subjects. Two reviewers following preferred reporting items for systematic reviews and meta-analyses (PRISMA) guidelines performed study eligibility assessment and data extraction. Findings from studies were analyzed with bivariate mixed models. Results: A total of 32 studies were included in the meta-analysis to evaluate diagnostic value of κ-FLC index. Sensitivity and specificity ranged from 52% to 100% (weighted average: 88%) and 69% to 100% (89%) for κ-FLC index and from 37% to 100% (85%) and 74% to 100% (92%) for OCB. Mean difference of sensitivity and specificity between κ-FLC index and OCB was 2 and -4 percentage points. Diagnostic accuracy determined by mixed models revealed no significant difference between κ-FLC index and OCB. A discriminatory cut-off for κ-FLC index was determined at 6.1. Conclusion: The findings indicate that κ-FLC index has similar diagnostic accuracy in MS as OCB.
MeSH term(s)	Humans ; Multiple Sclerosis/diagnosis ; Multiple Sclerosis/cerebrospinal fluid ; Immunoglobulin kappa-Chains/cerebrospinal fluid ; Oligoclonal Bands/cerebrospinal fluid ; Immunoglobulin G/cerebrospinal fluid ; Demyelinating Diseases ; Biomarkers/cerebrospinal fluid
Chemical Substances	Immunoglobulin kappa-Chains ; Oligoclonal Bands ; Immunoglobulin G ; Biomarkers
Language	English
Publishing date	2022-12-01
Publishing country	England
Document type	Meta-Analysis ; Systematic Review ; Journal Article ; Review
ZDB-ID	1290669-4
ISSN	1477-0970 ; 1352-4585
ISSN (online)	1477-0970
ISSN	1352-4585
DOI	10.1177/13524585221134213
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