Dyserythropoietc anemia and monoclonal gammopaty.
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Results for “Immunoglobulin lambda-Chains”
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Lymphoid cells of the normal man intestinal mucosa possessing both kappa and lambda light chain specifities.
The presence of lymphoid cells possessing both kappa and lambda specificities has been observed in the intestinal mucosa of normal subjects. The variability in the number of such cells in different sections of the same sample and in different subjects seems to be a characteristic of this cell population and may reflect the high activity of the immune system in the gut.
Antibody-Producing Cells↗
Monoclonal IgG3-kappa and IgG1-lambda proteins with different idiotypic determinants present in a single patient.
Two monoclonal proteins belonging to IgG3-kappa and IgG1-lambda subclasses were detected in a single patient. Immunochemical analysis revealed that the idiotypic determinants of the two proteins were different. Examination of bone marrow by an immunofluorescence technique indicated that these two proteins were produced in different cells, although both kappa and lambda chains were present in a minute proportion of the cells. J chain was present in all cells that produced IgG.
Bone Marrow↗
Structural and biosynthetic studies of a human IgA half molecule.
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Antibody Formation↗
Mediation of cytotoxic functions by classes and subclasses of sheep antibody reactive with cell surface immunoglobulin idiotypic and constant region determinants.
Sheep antibodies, reactive with either the idiotypic or constant region antigenic determinants of the immunoglobulin light chain on guinea-pig L2C leukaemic cells, were separated into IgM and into the two subclasses of IgG, IgG1 and IgG2. Antibody of both IgG subclasses inhibited the migration of L2C cells along plastic surfaces; IgM was only weakly inhibitory. Antibody of class IgM and of subclass IgG1 mediated complement cytotoxicity against the L2C cells whereas only that of subclass IgG2 mediated K-cell cytotoxicity; the effector arms were rabbit complement and sheep peripheral leucocytes, respectively.
Animals↗
Treatment of plasma cell myeloma with cytotoxic agents.
Because cross-resistance between alkylating agents has not been observed, we attempt in a prospective trial to determine the advantages, if any, in administering three alkylating agents sequentially, alternately, or concurrently. A patient with myeloma, showing progressive shortening of M-protein doubling time from 98 to 15 days, developed an acute terminal phase, characterized by fever and pancytopenia. A similar acute terminal phase was observed in 17 of 50 deaths from myeloma. Since alkylating agents are only effective in controlling the chronic phase of myeloma, future improvements will require the discovery of agents that delay, prevent, or are effective in the treatment of the acute phase. Forty-five patients with kappa- and 36 with lambda-light-chain disease showed no differences in frequency of amyloidosis, renal failure, response to treatment, or survival after treatment with alkylating agents.
Acute Disease↗
The characterization of human anti-IgG autoantibodies by liquid isoelectric focussing.
A series of human anti-IgG autoantibodies (AGA) have been analyzed by liquid isoelectric focusing in order to a) determine their isoelectric points (pI) and b) assess their heterogeneity. The 13 AGA examined include five IgM, five IgA, and three three IgG AGA. All demonstrate a single major peak indicative of restricted heterogeneity and each is characterized by an acidic pI. This anodal pI is distinct from other immunoglobulins isolated from the same serum that do not exhibit anti-IgG activity. It is speculated that the acidic pI is the result of acidic amino acid substitutions in the variable regions of immunoglobulin chains. The restricted heterogeneity and distinctive pI of the AGA suggest the selection of structurally similar antibody molecules from the large repertoire available in the human genome.
Alkylation↗
Similar idiotypic specificity for the membrane IgD and IgM of human B lymphocytes.
Certain cases of chronic lymphocytic leukemia possess monoclonal bands in the serum. Idiotypic antibodies to the isolated IgM protein of one such case demonstrated that the leukemic lymphocytes carried the identical specificity on their lymphocytes. Both the lymphocyte IgM and the IgD possessed this same specificity. This was demonstrated best through the use of rhodamine-conjugated Fab fragments of IgM- and IgD-specific antisera which were both capped by the idiotypic antiserum.
Animals↗
IgG half-molecules: clinical and immunologic features in a patient with plasma cell leukemia.
The clinical manifestations and immunologic features of a patient with plasma cell leukemia who produced k, IgG half-molecules are described. His serum contained both 7S myeloma protein and 4.3S half-molecules, whereas his urine contained predominantly half-molecules. The half-molecules were discovered because the serum and urine formed double precipitin lines when analyzed by commercially available IgG radial immunodiffusion plates that contained antibodies to determinants on both the Fab and Fc fragments. Immunoelectrophoresis also revealed double precipition lines with such antisera. In contrast, when antisera specific for the IgG Fc fragment were used, the serum showed only a single line formed by intact IgG, and the urine failed to react, indicating that the half-molecule was antigenically deficient in the Fc fragment. The half-molecule consisted of one covalently linked heavy and light chain, both having about normal molecular weights, suggesting that they did not have a large deletion which could have caused the half-molecule production. Comparison of the clinical manifestations of the patient with those of four other known patients who produced half-molecules suggested that half-molecule formation is not associated with a distinct clinical syndrome.
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GammaG-globulin production and light-chain metabolism in patients with metastatic cancer.
GammaG-Globulin and excess light-chain metabolism were studied in eight subjects with progressive metastatic malignant disease by determining the plasma radioactivity curves following the administration of appropriately labeled substances. In addition to the plasma die-away curves, which required about 3 weeks for full expression for gamma-globulin, but only 3 to 4 days for light-chain, urinary excretion of the label from metabolized protein was determined. The data are compared to similar studies in control individuals. The metabolism of excess light chain was similar to normal in all respects. The total synthesis of gammaG-globulin was increased with a mean value about twice normal. The mean survival time of a circulating immunoglobulin molecule was short, indicating rapid loss from the system. Other aspects of immunoglobulin metabolism were similar to normal with a normal percentage of the labeled protein appearing in the urine, suggesting no abnormality in the utilization pattern but simply an increased rate of turnover. The capability of malnourished patients with cancer to produce large quantities of immunoglobulin is not specific for this disease, since similar patterns may be seen in response to infections in protein-depleted individuals. However, there is the possibility that the cancer itself acts as an inciting agent in these subjects. Furthermore, such sustained protein synthesis may place an additional burden on already compromised host metabolism.
Humans↗
The primary structure of a human lambda II chain.
The human myeloma protein Boh (gamma 2, lambda) was isolated and completely reduced and aminoethylated. The light chain was obtained by chromatography on Sephadex G-100 in 4 M guanidine HC1. The amino-terminal sequence on the blocked light chain could be determined by automatic sequence degradation after PCAase treatment. Twenty-one peptides were isolated from a tryptic digest and 12 peptides from a chymotryptic digest. The sequence determination on these peptides was performed by automatic sequencing methods. The light chain of Boh protein belongs to the lambda II subgroup. Unique substitutions have been found at position 8 (Arg) and position 62 (Tyr). Furthermore, the Boh light chain has six cysteine residues, the additional (sixth) cysteine being adjacent to the invariable intrachain-S-S linking cysteine at position 91. Sequence comparison of lambda II proteins reveals a high degree of homology emphasizing the biologic significance of the hypervariable region sequences;
Amino Acid Sequence↗
Evidence for the absence of noncovalent bonds in the Fcmu region of IgM.
IgM isolated from the sera of five patients with Waldenström's macroglobulinemia was subjected to tryptic digestion at 60 degrees C. The Fc5mu fragments recovered from the digests were reduced by 0.05 M cysteine and alkylated by iodoacetamide, producing large quantities of an Fcmu fragment having a sedimentation velocity (see article) of 2.9S and a molecular weight of 33,500 by sedimentation equilibrium in neutral buffer. Further studies on the Fcmu fragment from one of the proteins demonstrated that it was not dissociated into smaller fragments by 5 M guanidine-HC1, even after reduction with 0.1 M 2-mercaptoethanol in 5 M guanidine at pH 7.5. The number of sulfhydryl groups released by the latter treatment indicated the presence of two intrachain disulfide bonds. These observations provide evidence that this portion of the mu-chain demonstrates minimal noncovalent interactions. Tryptic digestion of the Fcmu fragment at 37 degrees C resulted in the production of several lower molecular weight fractions. The three major fractions demonstrated apparent molecular weights of 21,000, 13,800 and 6800 by sedimentation equilibrium in 5 M guanidine-HC1. The latter fraction (fraction C) had no detectable carbohydrate and consisted of two disulfide-bonded peptides having molecular weights of approximately 3800 and 2200. Studies on the amino acid composition and amino-terminal sequences indicated that fraction C was derived from the Cmu4 homology region and consisted of residues 468 through 546 of the mu-chain with the tryptic peptides encompassing residues 492 through 514 missing.
Amino Acid Sequence↗
[Antibody specificity--immune specificity].
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Antibody Formation↗
[Production of rabbit precipitating antisera to subclasses of human IgG].
Precipitating antisera to human subclasses IgG were obtained by immunization of rabbits by whole molecules IgG2, IgG3, IgG4 and gamma 1-chains derived from IgG1H (Pr). Analysis of the antisera obtained demonstrated that rabbits produced specific antibodies to the antigenic subclass determinants IgG3 well, to IgG2, IgG4--much worse, and failed to produce specific antibodies to subclass IgG1 (in immunization with whole molecules of this protein). Antisera contained antibodies to the antigenic determinants common of IgG, and antibodies to light chains which were removed by immunosorption, for which purpose a sorbent on the basis of BrCN sepharose conjugated with IgG of the three other subclasses and Fab-fragment was used.
Animals↗
IgD myeloma protein with "unreactive" light chain determinants.
Serum from a patient with multiple myeloma showed a monoclonal protein, classified by immunoelectrophoresis as IgD. Immunofixation electrophoresis and immunoelectrophoresis failed to demonstrate a precipitation reaction between the paraprotein and antisera to immunoglobulin light chains. The light chains of the monoclonal protein, immunologically inaccessible in the intact molecule, reacted with anti-lambda chain antisera only after reduction and alkylation of the paraprotein. Moreover, interpretation of the immunoelectrophoretic patterns was hampered by the presence in patient's serum of free lambda chains having about the same mobility as that of the paraprotein.
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[Contribution of new methods of quantitative cytology and immunology to the understanding of lymphoproliferative syndromes].
Seventy one patients with a lymphoid hemopathy, three with agammaglobulinemia and six normal controls were investigated with regard to their blood lymphocyte membrane-associated light chains. Detection and quantitation of antigenic determinants were performed by means of peroxidase-labeled antibodies. Compared to normal controls, values found in chronic lymphocytic leukemia (CLL) were very low (tenfold decrease). The number of antigenic determinants on lymphoid cells from patients with blast crises supervening in CLL, prolymphocytic leukemia, Waldenstrom's macroglobulinemia and Burkitt cell acute leukemia were significantly higher than those seen in patients with CLL. The data obtained in this investigation through quantitative immunocytology constitutes a new parameter for the classification of lymphoid hemopathies and for an approach to their pathogenesis, in particular if the quantity of membrane immunoglobulin correlates with the stage of cell maturation.
Antibodies↗
[Participation of rat immunoglobulin light chains of the kappa and lambda type in formation of antibodies to the polysaccharide of group A streptococcus].
The role of light kappa and lambda chains and also allelic variants of kappa chains of rat immunoglobins in the formation of antibodies to beta-N-acetyl-glucosamine polysaccharides of streptococcus group A of inbred rat strains MSU, WAG, August and hybrids of the first generation (MUS X WAG)F1 and (MSU X August)F1 was studied. From individual sera of immune rats fractions of specific antibodies to beta-N-acetyl-glucosamine were isolated. These antibodies differ in their affinity to antigenes. The retio of molecules with kappa and lambda light chain types was determined for the fraction of specific antibodies. The ratio of molecules kappa and lambda depends on the affinity of antibodies to beta-N-acetyl-glucosamine and on the genotype of the animals studied. Data obtained allow to conclude that differences in the functional activity of lambda chains between strains WAG and August, on one hand, and strain MSU, on the other, do exist. Functional differences releaved between these rat strains were confirmed by analyzing corresponding antibody fractions to beta-N-acetylglucosamine in F1 hybrids. Differences between allelic variants of kappa chains in the formation of antibodies to beta-N-acetylglucosamine of polysaccharides were not found.
Acetylglucosamine↗
Cryoglobulinemia and amyloidosis associated with intestinal lymphoma.
A case of lymphocytic lymphoma of the small intestine was associated with cryoglobulinemia and amyloidosis. The neoplastic lymphoid cell demonstrated surface IgG membrane markers by immunofluorescence and immunoelectron microscopy. The cryoglobulins were characterized as monoclonal IgG3 proteins with lambda light chains. Amyloidosis of the small intestine and regional lymph nodes was found in association with lymphatic infiltration of these organs, suggesting the production of amyloid in situ.
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