Variations in leucine transfer ribonucleic acid in mouse plasma cell tumors producing kappa-type immunoglobin light chains

Biochemistry ◽  
1969 ◽  
Vol 8 (4) ◽  
pp. 1684-1692 ◽  
Author(s):  
J. Frederic Mushinski ◽  
Michael Potter
Keyword(s):  
Plasma Cell ◽  
Ribonucleic Acid ◽  
Light Chains ◽  
Mouse Plasma

scholarly journals Biosynthesis of the carbohydrate portions of immunoglobulin M

1971 ◽  
Vol 125 (1) ◽  
pp. 235-240 ◽  
Author(s):  
R. M. E. Parkhouse ◽  
Fritz Melchers
Keyword(s):  
Plasma Cell ◽  
Early Stage ◽  
Tumour Cells ◽  
Immunoglobulin M ◽  
Cell Tumour ◽  
Light Chains ◽  
Free Light Chains ◽  
Mouse Plasma

Incorporations of radioactive mannose, galactose and fucose into MOPC 104E mouse plasma-cell tumour suspensions suggest a stepwise addition of carbohydrate residues to immunoglobulin M (IgM) during the process of secretion. Mannose and glucosamine residues are added at an early stage, whereas galactose and fucose are added just before, or at the time that, IgM leaves the cell. Free light chains secreted in excess by the same tumour cells incubated with mannose, galactose or fucose contained barely detectable amounts of radioactivity.

scholarly journals THE INTRACELLULAR DISTRIBUTION OF GAMMA GLOBULIN IN A MOUSE PLASMA CELL TUMOR (X5563) AS REVEALED BY FLUORESCENCE AND ELECTRON MICROSCOPY

1962 ◽  
Vol 116 (4) ◽  
pp. 423-432 ◽  
Author(s):  
Richard A. Rifkind ◽  
Elliott F. Osserman ◽  
Konrad C. Hsu ◽  
Councilman Morgan
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Cell ◽  
Secretory Protein ◽  
Cell Tumor ◽  
Secretory Process ◽  
Cytoplasmic Matrix ◽  
Mouse Plasma ◽  
Plasma Cell Tumor ◽  
Antibody Staining ◽  
Fluorescence And Electron Microscopy

Ferritin- and fluorescein-conjugated antibody staining has been applied to a study of a mouse plasma cell tumor. The presence of myeloma globulin within cisternae of the endoplasmic reticulum was observed at a stage of the secretory process when the remainder of the cytoplasm was essentially free of labeled globulin. The distribution of ferritin suggested a functional heterogeneity among units of the endoplasmic reticulum. Apparently, progressive accumulation of globulin results in distension of the endoplasmic reticulum and, occasionally, in the appearance of considerable quantities of this secretory protein in the extracisternal cytoplasmic matrix. Participation of the Golgi apparatus in the packaging and release of small quantitites of globulin seems likely. In addition, however, fragmentation of the peripheral cytoplasm with rupture of distended ergastoplasmic vesicles appeared to be another pathway whereby globulin is secreted.

scholarly journals Phenotypic analysis of human myeloma cell lines

Blood ◽  
1989 ◽  
Vol 73 (2) ◽  
pp. 566-572
Author(s):  
C Duperray ◽  
B Klein ◽  
BG Durie ◽  
X Zhang ◽  
M Jourdan ◽  
...  
Keyword(s):  
B Cell ◽  
Cell Lines ◽  
Plasma Cell ◽  
Plasma Cells ◽  
Myeloma Cell ◽  
Light Chains ◽  
Cell Phenotype ◽  
Phenotypic Analysis ◽  
Barr Virus ◽  
Human Myeloma Cell

Multiple myeloma (MM) is a B-cell malignancy characterized by the accumulation, primarily in bone marrow, of a clone of plasma cells. The nature of the stem cells feeding the tumoral compartment is still unknown. To investigate this special point, we have studied the phenotypes of nine well-known human myeloma cell lines (HMCLs) and compared them with those of normal lymphoblastoid cell lines (LCLs). Twenty-four clusters of differentiation involved in B lymphopoiesis were investigated using a panel of 65 monoclonal antibodies (MoAbs). For each cluster, the percentage of positive cells and the antigen density were determined, giving rise to a “quantitative phenotype”. We thus classified the HMCLs into two different groups: those with cytoplasmic mu chains (c mu+) and those without (c mu-). In the first (c mu+) group, comprising seven cell lines, the HMCLs had a phenotype of pre-B/B cells close to that of Burkitt's lymphoma cell lines. They expressed low densities of surface mu chains, without detectable cytoplasmic or surface light chains. Three of them were infected with the Epstein Barr virus (EBV). These c mu+ HMCLs bore most of the B-cell antigens except CD23. They expressed the CALLA antigen (CD10) and lacked the plasma-cell antigen PCA1. In contrast, LCLs expressed surface light chains, high densities of CD23, low densities of PCA1 antigen, and no CD10 antigen. The c mu- HMCLs had a plasma-cell phenotype, lacking most of the B-cell antigens and expressing high densities of PCA1 antigen.(ABSTRACT TRUNCATED AT 250 WORDS)

kappa/lambda index for confirming urinary free light chain in amyloidosis AL and other plasma cell dyscrasias

1991 ◽  
Vol 37 (6) ◽  
pp. 1122-1126 ◽  
Author(s):  
Stanley S Levinson
Keyword(s):  
Plasma Cell ◽  
Electrophoretic Pattern ◽  
Light Chains ◽  
Plasma Cell Dyscrasia ◽  
Serum Samples ◽  
Kappa Chain ◽  
Immunofixation Electrophoresis ◽  
Patient Groups ◽  
Bone Marrow Analysis ◽  
Serum And Urine

Abstract Primary systemic amyloidosis (AL), a disease involving the deposition of immunoglobulin light chains in tissue, is caused by a plasma cell dyscrasia. In the case of amyloidosis reported here, no monoclonal component was seen upon routine protein electrophoresis of serum or urine nor was a bone marrow analysis positive for AL. Immunofixation electrophoresis did not show a typical paraprotein band but did show, in the gamma region, two large diffuse bands and a lower concentration of oligoclonal-type bands, all of which stained for free lambda but not for free kappa chain. The ratio of kappa to lambda chains in urine was 0.178, much less than the ratio in serum (1.3). Six other urine samples from a group of patients with documented Bence Jones proteinuria also exhibited kappa/lambda ratios that differed manyfold from the ratios in their corresponding serum samples. On the other hand, the kappa/lambda ratios from seven controls (seven patients with generalized proteinuria unrelated to plasma cell dyscrasia) were similar in serum and urine. This difference between the kappa/lambda ratios from serum and urine can be expressed as a kappa/lambda index. The index was significantly different (P less than 0.01) between the two patient groups compared here, and was useful in confirming the presence of Bence Jones protein in this case with a difficult-to-interpret electrophoretic pattern. Although the kappa/lambda ratio has been widely used for confirmation and identification of monoclonal components in serum, its use in clinical laboratories has not been widely extended to urine. Comparison of serum and urine kappa/lambda ratios as a kappa/lambda index may help reduce the need for more complex immunoelectrophoresis techniques in identifying free light chains in urine.

Quantification by Ultrafiltration and Immunofixation Electrophoresis Testing for Monoclonal Serum Free Light Chains

2020 ◽  
Vol 51 (6) ◽  
pp. 592-600 ◽  
Author(s):  
Gurmukh Singh ◽  
Roni Bollag
Keyword(s):  
Plasma Cell ◽  
Light Chain ◽  
Limit Of Detection ◽  
Light Chains ◽  
Total Serum ◽  
Reliable Estimate ◽  
Free Light Chains ◽  
Serum Free ◽  
Immunofixation Electrophoresis ◽  
Serum Free Light Chains

Abstract Objective Measurement of monoclonal immunoglobulins is a reliable estimate of the plasma cell tumor mass. About 15% of plasma cell myelomas secrete light chains only. The concentration of serum free light chains is insufficient evidence of the monoclonal light chain burden. A sensitive quantitative estimate of serum free monoclonal light chains could be useful for monitoring patients with light chain myeloma. We describe such an assay that does not require mass-spectrometry equipment or expertise. Methods Serum specimens from patients with known light chain myelomas and controls were subjected to ultrafiltration through a membrane with pore size of 50 kDa. The filtrate was concentrated and tested by immunofixation electrophoresis. The relative area under the monoclonal peak, compared to that of the total involved light chain composition, was estimated by densitometric scanning of immunofixation gels. The proportion of the area occupied by the monoclonal peak in representative densitometric scans was used to arrive at the total serum concentration of the monoclonal serum free light chains. Results Using an ultracentrifugation and concentration process, monoclonal serum free light chains were detectable, along with polyclonal light chains, in all 10 patients with active light chain myelomas. Monoclonal light chains were identified in serum specimens that did not reveal monoclonal light chains by conventional immunofixation electrophoresis. The limit of detection by this method was 1.0 mg/L of monoclonal serum free light chains. Conclusion The method described here is simple enough to be implemented in academic medical center clinical laboratories and does not require special reagents, equipment, or expertise. Even though urine examination is the preferred method for the diagnosis of light chain plasma cell myelomas, measurement of the concentration of serum free light chains provides a convenient, albeit inadequate, way to monitor the course of disease. The method described here allows effective electrophoretic differentiation of monoclonal serum free light chain from polyclonal serum free light chains and provides a quantitation of the monoclonal serum free light chains in monitoring light chain monoclonal gammopathies.

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