Immunohistologic Localization of Gamma-1-Macroglobulins, Beta-2A-Myeloma Proteins, 6.6 S Gamma-Myeloma Proteins and Bence Jones Proteins

Blood ◽  
1963 ◽  
Vol 21 (4) ◽  
pp. 403-423 ◽  
Author(s):  
ALAN SOLOMON ◽  
JOHN L. FAHEY ◽  
RICHARD A. MALMGREN
Keyword(s):  
Cellular Localization ◽  
Indirect Evidence ◽  
Malignant Cell ◽  
Specific Protein ◽  
Lymphoid Cells ◽  
Malignant Cells ◽  
Serum Globulin ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Bence Jones Proteins

Abstract The cellular localization of 6.6 S γ-globulins, β2A-globulins, γ1-macroglobulins and Bence Jones proteins was studied by immunohistochemical procedures in 21 patients with multiple myeloma or macroglobulinemia. Each type of protein was identified by specific immunofluorescence in a variety of morphologic forms of malignant cells. Some cells were typically plasmacytic, some were lymphoid cells and others were immature forms. It was clear that γ, β2A, γ1M, and Bence Jones proteins were not associated exclusively with a single morphologic form of malignant cell. The variety of immunofluorescent positive cells in each patient was more restricted, however, than in a group of patients with a specific protein abnormality. In patients with anomalous proteins, all or almost all of the malignant cells were found to contain the specific anomalous protein. The malignant cells contained either γ-myeloma protein, β2A-myeloma protein or γ1-macroglobulin in patients with these types of anomalous protein. Only one class of globulin was found in individual cells. In patients with Bence Jones proteins as the sole anomalous protein, all the malignant cells appeared to have Bence Jones protein. Where an anomalous serum globulin coexisted with Bence Jones proteins, indirect evidence indicated that the Bence Jones proteins and the larger globulin were formed in the same cells.

scholarly journals CLASSIFICATION OF MYELOMA PROTEINS, BENCE JONES PROTEINS, AND MACROGLOBULINS INTO TWO GROUPS ON THE BASIS OF COMMON ANTIGENIC CHARACTERS

1962 ◽  
Vol 116 (6) ◽  
pp. 859-877 ◽  
Author(s):  
Mart Mannik ◽  
Henry G. Kunkel
Keyword(s):  
Multiple Myeloma ◽  
Antigenic Determinants ◽  
General Category ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Protein Molecules ◽  
Bence Jones Proteins

Antisera to normal 7S γ-globulin and to Bence Jones proteins permit the grouping of myeloma proteins (gamma and beta 2A types), Bence Jones proteins, and the Waldenström type macroglobulins into two fundamental antigenic groups. The antigenic determinants responsible for this grouping are common to all these proteins which fall in the general category of immunoglobulins. Antisera to Bence Jones proteins were particularly useful for this classification since they failed to react with the proteins of the opposite group. These antisera also permit the grouping of normal 7S γ-globulin into two major types. The Bence Jones proteins from individual patients were found to correspond in antigenic group to that of the serum myeloma protein. Studies with antisera to 7S γ-globulin and to Bence Jones proteins indicated that the Bence Jones proteins were antigenically identical to a portion of the corresponding multiple myeloma protein molecules.

scholarly journals COMPARISONS OF BENCE-JONES PROTEINS AND L POLYPEPTIDE CHAINS OF MYELOMA GLOBULINS AFTER HYDROLYSIS WITH TRYPSIN

1963 ◽  
Vol 118 (1) ◽  
pp. 41-53 ◽  
Author(s):  
J. H. Schwartz ◽  
G. M. Edelman
Keyword(s):  
High Voltage ◽  
Two Dimensional ◽  
Bence Jones Protein ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Group I ◽  
Chain Fraction ◽  
Polypeptide Chains ◽  
High Voltage Electrophoresis ◽  
Bence Jones Proteins

L polypeptide chains of myeloma globulin and Bence-Jones protein isolated from the same patient were found to be identical after comparison of their tryptic hydrolysates by two-dimensional high voltage electrophoresis. The patterns of peptides from proteins belonging to antigenic group I differed markedly from those of proteins in antigenic group II. A partially purified H chain fraction was compared with L chains from the same myeloma protein. The tryptic hydrolysates yielded dissimilar patterns of peptides. These data indicate that γ-myeloma proteins contain two kinds of polypeptide chains, Hγ chains and either LI or LII chains. The L chains appear to be identical with those comprising the Bence-Jones protein from the same patient.

scholarly journals GENETIC CHARACTERS OF HUMAN γ-GLOBULINS IN MYELOMA PROTEINS

1962 ◽  
Vol 116 (5) ◽  
pp. 719-738 ◽  
Author(s):  
M. Harboe ◽  
C. K. Osterland ◽  
M. Mannik ◽  
H. G. Kunkel
Keyword(s):  
Plasma Cells ◽  
Protein Product ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Normal Individuals ◽  
Γ Globulins ◽  
Normal Human ◽  
Genetic Characters ◽  
Single Plasma ◽  
Bence Jones Proteins

The genetic factors Gm(a), Gm(b), Gm(x), and Inv(a), Inv(b) described for normal human γ-globulin were all found in different myeloma proteins. A single myeloma protein never contained more than one product of alternate alleles even in heterozygous individuals. However, factors determined by the two different loci were often found in the same myeloma protein. The Gm(a) character of the myeloma protein parallelled that of the normal γ-globulin of the same serum in most cases. In contrast, the Gm(b) character was usually absent in the myeloma protein when it was directly demonstrable in the normal γ-globulin. The myeloma proteins from six Negroes were Gm(a+b-), whereas the normal γ-globulin was Gm(a+b+). This indicates that the effect of gene Gmb is similar in Negroes and whites, even though its relation to gene Gma is different in the two races. Gm factors were found only in the 7S γ-globulin type myelomas and not in other products of plasma cell tumors. Inv characters were, however, present in all four types of proteins studied, namely 7S and 19S γ-globulins, ß2A-globulins, and Bence Jones proteins. In two instances, genetic heterogeneity of the protein products was demonstrated suggesting the proliferation of more than one clone of plasma cells in some multiple myeloma patients. The accumulated evidence obtained in this study strongly suggested that the presence and absence of genetic characters was compatible with the concept that myeloma proteins were closely analogous to individual moieties in the spectrum of normal γ-globulins rather than truly abnormal proteins. Their study offered evidence of a heterogeneity of genetic characters among the normal γ-globulins in a given individual. It also appears probable that in normal individuals single plasma cells have a restricted capacity to express genetic information in their protein product.

Occurrence of Myeloma-Like γ-Globulin in C.S.F of A Four-Month Old Infant with Hydrocephalus

PEDIATRICS ◽  
1964 ◽  
Vol 33 (3) ◽  
pp. 435-440
Author(s):  
G. M. HOCHWALD ◽  
G. J. THORBECKE
Keyword(s):  
Paper Electrophoresis ◽  
Reticulum Cell ◽  
Reticulum Cell Sarcoma ◽  
Myeloma Protein ◽  
Characteristic Appearance ◽  
Myeloma Proteins ◽  
Group I ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Narrow Bands

Myeloma-like immune globulins present themselves as narrow bands upon paper electrophoresis, and usually show a characteristic appearance in immunoelectrophoresis. Two antigenically different groups of myeloma proteins have been described: groups I and II. Recently, 60% of normal γ-globulin, throughout the mobility range of γ-globulin, has been shown to possess the antigen characteristic for group I, and 30% that for group II myeloma. Occurrence of myeloma-like proteins in the serum is not restricted to multiple myeloma. They may also be seen with other tumors, such as reticulum cell sarcoma, and various carcinomas. In addition, Sonnet and Milhaux have reported on the frequent occurrence of myeloma-like ("monoclonal") γ-globulins in the serum of adult Bantus with different diseases. When large amounts of a myeloma protein are present in the serum, it may be found in a much lower concentration in the spinal fluid.

scholarly journals Deficiency of Vitamin B12-Binding Alpha Globulin in Two Brothers

Blood ◽  
1969 ◽  
Vol 33 (1) ◽  
pp. 1-12 ◽  
Author(s):  
RALPH CARMEL ◽  
VICTOR HERBERT
Keyword(s):  
Vitamin B12 ◽  
Binding Protein ◽  
Indirect Evidence ◽  
Serum Globulin ◽  
Peripheral Leukocyte ◽  
Hereditary Defect ◽  
B12 Deficiency ◽  
Destructive Factor ◽  
Low Serum

Abstract Persistent deficiency of serum B12-binding alpha-1 globulin was demonstrated in two brothers, manifesting primarily as low serum B12 levels. Despite the inability of one subject to maintain normal levels of B12 in the blood, as shown by persistently low serum values despite monthly injections of B12, no evidence of metabolic B12 deficiency could be found. Tissue B12-storing ability appeared to be intact. His brother exhibited only minimal hypersegmentation of neutrophil nuclei; otherwise, he too presented a completely normal picture. The normally present alpha globulin B12-binder was virtually absent from saliva and peripheral leukocyte extracts of both subjects. Current indirect evidence favors neutrophils as at least a partial source of the serum globulin.33 The cause of the possibly hereditary defect in the 2 subjects is unknown. Neither excessive B12-binding protein excretion34 nor a destructive factor in their serum or leukocytes was found.

A DISCRETE SIMULATION OF TUMOR GROWTH CONCERNING NUTRIENT INFLUENCE

2004 ◽  
Vol 18 (17n19) ◽  
pp. 2651-2657 ◽  
Author(s):  
L. SUN ◽  
Y. F. CHANG ◽  
X. CAI
Keyword(s):  
Cell Growth ◽  
Tumor Growth ◽  
Potts Model ◽  
Discrete Model ◽  
Malignant Cell ◽  
Healthy Tissue ◽  
Thermodynamic Method ◽  
Malignant Cells ◽  
Discrete Simulation ◽  
Adjustment Factors

We develop a 2-D discrete model to simulate malignant cells growing in healthy tissues using a thermodynamic method on the basis of Potts model. After introducing a malignant seed in a healthy tissue, we use a set of adjustment factors, including the interaction between cells and nutrient, to simulate the growth of malignant cells under different environments. This allows us to investigate the effects of environment on malignant cell growth and the formation of cancer.

An In Vitro Model of Proliferating CLL Cells for Drug Sensitivity Analysis.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2956-2956
Author(s):  
K. Ganeshaguru ◽  
N. I. Folarin ◽  
R. J. Baker ◽  
A. M. Casanova ◽  
A. Bhimjiyani ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Lymph Nodes ◽  
Peripheral Blood ◽  
Drug Sensitivity ◽  
In Vitro Model ◽  
Survivin Expression ◽  
Lymphoid Cells ◽  
Malignant Cells ◽  
Vitro Model

Abstract B-cell chronic lymphocytic leukaemia (CLL) is a heterogeneous disease with a variable clinical course. The disease is characterised by the proliferation in the bone marrow and lymph node of a clonal population of CD5+ve cells that accumulates in the peripheral blood. Therefore, the characteristics of the proliferative compartment are important in determining the kinetics of disease progression in CLL and the sensitivity of the malignant cells to cytotoxic drugs. However, laboratory studies on drug sensitivity of CLL have been performed exclusively on resting circulating peripheral blood cells since it is not feasible to obtain cells from the proliferating pool in sufficient numbers for in vitro analysis. CLL cells can be stimulated to proliferate in vitro using CpG oligonucleotides (ODN) and other factors. The aim of the present study was to generate and validate an in vitro model using malignant cells from the peripheral blood of patients with CLL. The expression pattern of proteins eg., survivin in this model should mimic that in proliferating CLL cells in the bone marrow and lymph nodes. Survivin is a member of the family of inhibitor of apoptosis (IAP) proteins with an additional role in cell cycle progression. Survivin has been shown to be expressed in proliferating bone marrow and lymphoid cells. Cells from patients with CLL were activated for 72h with a combination of ODN (1μM), IL-2 (100u/ml) and CD40L (0.5μg/ml) (ODN*). Activated cells retained their characteristic CLL immunophenotype as determined by the continued expression of CD5, CD19, CD23 and CD25 (n=5). Cell proliferation was confirmed by increased incorporation of 3H-thymidine into DNA in activated cells (n=12). Novel findings in the ODN* activated CLL cells were significant increases in expression of CD38 (n=7, p=0.0001) and of T-cell zeta associated protein (ZAP-70) tyrosine kinase (n=14, p=0.0005). The increased expression of both these proteins in circulating peripheral blood CLL cells has been associated with poor prognosis. All six ODN* activated CLL isolates analysed by western blotting showed increased survivin expression with no constitutive expression in the controls. Drug sensitivity was studied in cells from eight patients using the MTT assay. Activated cells showed significantly greater resistance to chlorambucil (median IC50=164.4±28.18μM) compared to control cells (median IC50=93.63±14.96μM, p=0.044). Figure 1 shows representative IC50 curves. The increased resistance of the activated cells to chlorambucil may be a consequence of the upregulation of survivin. In summary, the in vitro model replicates several key features of authentic proliferating CLL cells found in bone marrow and lymph nodes. It also shows increased resistance to the conventional drug chlorambucil. This model may be of value in evaluating novel drugs and drug combinations which may be more effective in killing the proliferating population that maintain the malignant cell population in CLL. Figure Figure

Breast Implant Related Anaplastic Large Cell Lymphoma ALK- (ALCL ALK-) – Case Report

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 5086-5086 ◽  
Author(s):  
Alejandro Arbelaez ◽  
Laurence Catley ◽  
Louis Pool
Keyword(s):  
Conflicts Of Interest ◽  
Case Reports ◽  
Breast Implant ◽  
Treatment Options ◽  
Fluid Collection ◽  
Case Series ◽  
Breast Implants ◽  
Large Cell ◽  
Lymphoid Cells ◽  
Malignant Cells

Abstract Case presentation A 29 underwent bilateral cosmetic breast augmentation 10 years previously (McGhan Textured Round 400 mL implants). Six months before, she developed slowly progressive right breast pain and inflammatory signs associated with fluid collection around the right breast that was drained. A yellow cloudy fluid was examined and showed atypical large lymphoid cells. The cell block prepared in another institution showed numerous lymphoid cells including large atypical cells with lobated nuclei. PET CT scan was negative, same as bone marrow aspirate and trephine for lymphoma infiltration. Following bilateral removal of the breast implants, further histopathology studies showed no infiltration by lymphoma of the breast capsules or scar tissue. However, right breast peri prosthetic fluid microscopy showed a population of single malignant cells with scanty cytoplasm, numerous mitosis, and nuclei showing single and multiple nucleoli. Some cells showing horseshoe nuclei. The malignant cells were positive for CD30 and LCA and negative for CD20, CD68, AE1-3, and ALK 1. FISH for ALK was not possible (Fig 1) Discussion Primary breast lymphomas are very rare conditions; they represent less than 1% of all NHL and less than 0.7% of all breast malignancies. There have been some cases reported in the medical literature of ALCL ALK- associated with breast implants. All the cases have been described in patients with textured implants, such as in this case and the reason is unknown. There are two main types of ALCL of the breast based on published case reports: a mass and an effusion. Primary breast effusion associated ALCL portends a good prognosis despite the fact that they are ALK-. The development of ALCL proximal to breast implants suggests that they are the result of an immune reaction to the silicone. Whether they represent true malignancy or a localised reactive phenomenon is not entirely clear yet. In previous case series, the condition has been described as indolent. However, given the low incidence of this condition and the limited literature available; it is difficult to know what the best treatment approach is. Following confirmation of the diagnosis, treatment options were discussed with the patient and the preferred option was active treatment with local radiation after removal of breast implants. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Purification, properties and cellular localization of the stereospecific CS2 secondary alkylsulphohydrolase of Comamonas terrigena

1977 ◽  
Vol 167 (3) ◽  
pp. 723-729 ◽  
Author(s):  
G W J Matcham ◽  
K S Dodgson ◽  
J W Fitzgerald
Keyword(s):  
Chain Length ◽  
Cellular Localization ◽  
Indirect Evidence ◽  
Initial Study ◽  
Potassium Salts ◽  
Experimental Conditions ◽  
Alkyl Sulphate ◽  
A Subunit ◽  
A Chain ◽  
Comamonas Terrigena

The availability of homogeneous samples of the potassium salts of L- and D-octan-2-yl sulphate has enabled the separation of the optically stereospecific CS1 and CS2 secondary alkysulphohydrolases from extracts of cells of Comamonas terrigena. The CS2 enzyme was purified to homogeneity, and an initial study was made of its general properties, specificity, cellular localization and relationship to the CS1 enzyme. The CS2 enzyme has a molecular weight of approx. 250000 and a subunit size of approx. 58000, indicating that the molecule is a tetramer. Under the experimental conditions used the enzyme appears to be specific for (+)-secondary alkyl sulphate esters with the sulphate group at C-2 and with a chain length of at least six carbons. Enzyme activity towards racemic C-2 sulphates increases with increasing chain length up to C10, and there is some indirect evidence to suggest that activity declines when that chain length is exceeded. Other indirect evidence confirms that the CS1 enzyme exhibits similar specificity, except that only (-)-isomers can serve as substrates. Both enzymes are present in broth-grown stationary-phase cells of C. terrigena in approximately equal amounts.

An Immunoglobulin Light Chain of Subgroup III1 of λ Type with a Free Sulfhydryl Group

1971 ◽  
Vol 49 (8) ◽  
pp. 900-902 ◽  
Author(s):  
Barbara M. Buchwald
Keyword(s):  
Light Chain ◽  
Sulfhydryl Group ◽  
Variable Region ◽  
Cysteine Residue ◽  
Immunoglobulin Light Chain ◽  
Myeloma Protein ◽  
Free Sulfhydryl Group ◽  
Bence Jones Proteins

A myeloma protein, Du, (γ1)2 (λ)2, is shown to have an extra cysteine residue in the light chain. This light chain is from the same λ variable region subgroup as are two Bence-Jones proteins, X and Bau, which also have an extra cysteine residue. The position of this residue is the same in all three chains.

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