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Fulltext A rare occurrence of plasma cell myeloma with biclonal gammopathy

Mardziah, M., Nurasyikin, Y., Rafeah, T., Dian, N., Yousuf, R., Suria, A.A.

Medicine & Health, 2017;12(1):103-108.
MyJurnal

Plasma cell myeloma is known to cause expansion of a single clone of munoglobulin (Ig) which results in the secretion of a unique homogeneous monoclonal protein (M component). However, there are cases which reported that it can also cause production of two different clones of these monoclonal proteins. Although it is relatively very rare as the prevalence is only 2% of all plasma cell myeloma cases, the clinical features are said to be similar to monoclonal gammopathy. It is suggested that these biclonal gammopathy results from either one monoclonal cell clone in monoclonal gammopathy or two different monoclonal cell clones. Whichever the mechanism of the disease be, the response to treatment seems to be similar as compared to the monoclonal cases although some reports shows chemoresistant. Here, we report a rare case of plasma cell myeloma with IgG (lambda) and IgA (lambda) type of biclonal gammopathy, the clinical presentation, the haematological and biochemical markers as well as the response to the treatment.
Keywords: biclonal gammopathy, M protein, plasma cell myeloma

Matched MeSH terms: Myeloma Proteins
Fulltext Performance comparison of EasyFix G26 and HYDRASYS 2 SCAN for the detection of serum monoclonal proteins

Amin Nordin FD, Mohd Khalid MKN, Abdul Aziz SM, Mohamad Bakri NA, Ahmad Ridzuan SN, Abdul Jalil J, et al.

J Clin Lab Anal, 2020 Jun;34(6):e23254.
PMID: 32141626 DOI: 10.1002/jcla.23254

BACKGROUND: Serum protein electrophoresis (SPE) is a widely used laboratory technique to diagnose patients with multiple myeloma (MM) and other disorders related to serum protein. In patients with MM, abnormal monoclonal protein can be detected by SPE and further characterized using immunofixation electrophoresis (IFE). There are several semi-automated agarose gel-based systems available commercially for SPE and IFE. In this study, we sought to evaluate the analytical performance of fully automated EasyFix G26 (EFG26) and semi-automated HYDRASYS 2 SCAN (H2SCAN) for both SPE and IFE.
METHODS: Both instruments were operated according to manufacturer's instructions. Samples used include a commercially available normal control serum (NCS) and patients' specimens. The following were evaluated: precision and comparison studies for SPE, and reproducibility and comparison studies for IFE. Statistical analyses were performed using Microsoft Excel.
RESULTS: For SPE repeatability study, our results showed that EFG26 has higher coefficient of variation (%CV) compared with H2SCAN for both samples except for monoclonal component with %CV of 0.97% and 1.18%, respectively. Similar results were obtained for SPE reproducibility study except for alpha-1 (4.16%) and beta (3.13%) fractions for NCS, and beta fractions (5.36%) for monoclonal sample. Subsequently, reproducibility for IFE was 100% for both instruments. Values for correlation coefficients between both instruments ranged from 0.91 to 0.98 for the five classic bands.
CONCLUSION: Both instruments demonstrated good analytical performance characterized by high precision, reproducibility and correlation.

Matched MeSH terms: Myeloma Proteins/analysis
Fulltext Monoclonal gammopathy with systemic amyloidosis: an evaluation of diagnostic elements

Subashini, C. T., George, E., Nor Aini, U.

Malaysian Journal of Medicine and Health Sciences, 2011;7(1):51-55.
MyJurnal

Monoclonal gammopathies result from an overproduction of a single abnormal clone of plasma cell
or B lymphocyte that produce an immunologically homogenous immunoglobulin (Ig) commonly referred to as paraprotein or monoclonal (M) protein. The circulating M-protein may consist of an intact immunoglobulin, the light chain only, or (rarely) the heavy chain only. The heavy chain is from one of the five immunoglobulin classes G, A, M, D or E, while the light chain is either kappa (κ) or lambda (λ) in type. Accurate detection and quantitation of monoclonal immunoglobulins is important for the diagnosis and management of monoclonal gammopathies. We report a case of a 71 year old lady with a history of chronic gastritis and recurrent lower respiratory tract infection whereby no specific diagnosis was made until a computed tomography (CT) guided lung biopsy and orogastroduodenoscopy (OGDS) 5 years later from the onset of initial symptoms revealed pulmonary and gastric amyloidosis, respectively.

Matched MeSH terms: Myeloma Proteins
Light chain multiple myeloma: an evaluation of its biochemical investigations

Zahari Sham SY, C Thambiah S, Samsudin IN, Lim SM

Malays J Pathol, 2017 Dec;39(3):311-315.
PMID: 29279596 MyJurnal

Multiple myeloma is a type of plasma cell dyscrasia, characterised by presence of paraprotein or monoclonal (M)-protein in serum or urine. The M-protein may consist of an intact immunoglobulin, the heavy chain only or the light chain only. The latter, designated as light chain multiple myeloma (LCMM) makes up almost 20% of myelomas. Clinical manifestation is often heralded by hypercalcaemia, renal impairment, normocytic normochromic anaemia and bone lesions, reflecting end-organ damage, collectively known as the acronym CRAB. In particular, free light chain nephrotoxicity accounts for the high prevalence of renal impairment seen in LCMM. This case illustrates a typical presentation of LCMM with focal discussion on its initial and diagnostic, as well as prognostic biochemical investigations.

Matched MeSH terms: Myeloma Proteins/immunology*
Interaction of Artocarpus lectins with human IgA does not involve asparagine-linked oligosaccharide of the immunoglobulin

Hashim OH, Kobayashi K, Taniguchi N

Biochem. Int., 1992 Jul;27(3):423-9.
PMID: 1417879

In view of the controversy with respect to the interaction of jacalin with human IgA2, a study was undertaken to assess the reactivity of the Artocarpus heterophyllus lectin, as well as the lectin from Artocarpus integer (lectin C), with subclasses of human immunoglobulin A by ELISA. Our data is consistent with the view that Artocarpus lectins have no affinity for the IgA2 immunoglobulins. In further support of the findings, we have established that N-linked oligosaccharide moieties of IgA have no significant bearing in the lectin-immunoglobulin binding. Interaction was also not affected in the presence of 1% (w/v) BSA.

Matched MeSH terms: Myeloma Proteins/metabolism