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PubMed1979

A new case of gamma-3 heavy chain disease. Biochemical and immunological investigations.

A new gamma 3 heavy chain disease (gamma 3-HCD) protein (Emm) is described. A molecular weight of 70,000-80,000 daltons was estimated. Antigenic analysis showed that protein Emm lacks light chains and the CH1 domain of heavy chains, whereas the antigenic determinants of the gamma 3 Fc fragment (CH2 and CH3 domains) as well as those of the gamma 3 hinge region were present. Since the anomalous protein was temporarily present in serum Emm, a transient triggering of a cell clone which produces the gamma 3-HCD protein is suggested.

Chemical Phenomena↗
PubMed2000

Electrophoretic characterization of a gamma-1-heavy chain disease.

This report describes a new case of gamma-1-heavy chain disease found in a woman with malignant lymphoproliferative disease. The patient's serum and urine containing gamma-1-heavy chains were analyzed using different electrophoretic approaches, especially two-dimensional electrophoresis and immunoblotting analysis. In a serum sample, five sets of gamma-1-heavy chain spots differing in molecular weight with acidic pI values and one set of more basic gamma-1-heavy chain spots were found. The major group of spots exhibited molecular weight in the range from 29 to 39 kDa. Examination of urine sample proved the presence of the more basic set of gamma-1-heavy chain spots and two acidic groups, including 29 to 39 kDa set.

Aged↗
PubMed1994

Primary Sjögren's syndrome and gamma heavy chain disease.

We describe a patient who has primary Sjögren's syndrome associated with asymptomatic gamma heavy chain disease and a tubulointerstitial nephritis. Sjögren's syndrome is known to be complicated by lymphoproliferative disorders and tubulointerstitial nephritis but gamma heavy chain disease is rare (approximately 100 cases described). There is one previously reported case of gamma heavy chain disease associated with primary Sjögren's syndrome and 2 cases associated with secondary Sjögren's syndrome. Our patient and the 3 other patients described in the literature did not have evidence of an underlying lymphoproliferative disorder.

Aged↗
PubMed1978

The structural heterogeneity among degraded gamma heavy chain disease proteins.

The amino terminal sequence of seven newly studied and three previously reported gamma Heavy Chain disease proteins show that they begin at several sites ranging from position 215--234 in the hinge region. The presence of more than one species of molecule in several of the sera and the susceptibility of this region to proteolytic cleavage, taken together with the finding of a blocked Heavy Chain disease protein in the serum of one and the cells of another patient support the concept that these molecules are the result of proteolytic cleavage of typical Heavy Chain disease proteins.

Amino Acid Sequence↗
PubMed1998

A case of mu heavy-chain disease associated with hyperglobulinemia, anemia, and a positive Coombs test.

We report here for the first time a patient with mu heavy-chain disease (HCD), hyperimmunoglobulinemia, and a positive direct antiglobulin test (DAT, Coombs test). The heavy-chain diseases involve the proliferation of lymphoplasma cells of B cell origin and are characterized by the production of incomplete heavy chains devoid of light chains. The association of mu heavy-chain disease with either hyperglobulinemia or a positive DAT has not been reported in the literature to date. In this patient, immunofixation of serum proteins with monospecific antisera to alpha-, gamma-, mu,- or delta-chains and to kappa- and lambda-chains revealed a precipitation band with antibody to IgM, but not with kappa and lambda light-chain antibodies, indicating mu heavy-chain disease. Hyperglobulinemia was present, which is very uncommon for HCD. A DAT of the patient's red blood cells (RBC) was found to be strongly positive for anti-IgG but negative for anti-IgM, -IgA, -C3c, and -C3d. However, when the eluate from the patient's red blood cells was investigated with nephelometry, it was found to contain antigens reactive with anti-y as well with anti-mu-antiserum. When a DAT was performed with a randomly chosen test cell incubated with the eluate, the antibody-containing eluate was shown to react with anti-IgG as well as with anti-IgM-antiserum. In summary, the eluate from the patient's RBCs contained IgG and an immunoglobulin structure reactive with anti-IgM in an RBC agglutination assay as well as with anti-mu antiserum in a nephelometric investigation. Whether this IgM on the patient's erythrocytes is penta- or oligomeric, complete IgM, or the heavy chain cannot be concluded from these observations.

Aged↗
PubMed1977

Gamma heavy chain disease--presenting as pancytopenia and splenomegaly.

A patient with gamma heavy chain disease (Franklin's disease) was discovered during evaluation for pancytopenia and splenomegaly. Lymphadenopathy, palatal edema, and infiltration of the bone marrow palatal edema, and infiltration of the bone marrow with abnormal cells were all absent. Serum and urine protein electrophoresis demonstrated a monoclonal protein migrating in the beta region. Immunoelectrophoresis showed that it reacted with antibodies against the Fc fragment of IgG heavy chains (gamma chains) but not with antibodies against kappa and lambda but not with antibodies against kappa and lambda light chains of Fab fragments. In the first year after detection of the disease, the patient had acute cholecystitis and disseminated herpes zoster. Sixteen months after diagnosis he died of overwhelming pneumonia caused by Pseudomonas aeruginosa and lebsiella neumoniae. A striking feature of his illness was his asymptomatic presentation, with pancytophenia and splenomegaly the only indication of this disease.

Cholecystitis↗
PubMed1997

A case of mu-heavy chain disease: combined features of mu-chain disease and macroglobulinemia.

A case of mu-heavy chain disease (HCD) is described. The patient, a 40-year-old man, presented with an intracranial tumor. The bone marrow of this patient showed infiltration with both plasma cells and lymphocytes. The majority of plasma cells were vacuolated and the result of immunoelectrophoresis of serum protein revealed an arc with anti-IgM antiserum and an additional rapid migrating arc of different mobility with anti-kappa antiserum. The urine contained a kappa-type Bence Jones protein. An enzyme-linked antibody study showed that the majority of plasma cells in bone marrow contained both mu and kappa antigenic determinants in their cytoplasm. On Sephadex G-200 gel filtration, the monoclonal IgM-kappa protein and the mu-chain fragment were detected in the serum, suggesting the combined features of mu-HCD and macroglobulinemia. The molecular weight of the mu-chain fragment was approximately 45,000 daltons. The intracranial tumor completely disappeared after irradiation therapy. However, he died 1 year later after development of a huge abdominal tumor.

Adult↗
PubMed1986

A pre-translational defect in a case of human mu heavy chain disease.

A patient (BW) was studied with Mu heavy chain disease (mu HCD) in whom a leukemic B-cell clone secreted a shortened monoclonal mu chain without associated light chain. The cells did, however, produce a normal-sized kappa light chain that was detected as urinary Bence-Jones protein. The cytoplasmic and secreted monomeric mu chain had an approximate mol. wt of 58,000. Radiochemical sequence analysis of the biosynthetically labelled mu chain revealed a protein that lacked the entire variable region. The sequence initiated at amino acid position 5 within the first constant region domain (CH1) of C mu. The primary in vitro translation product, the cytoplasmic and secreted proteins were all similarly truncated, thereby excluding extensive postsynthetic degradation. The mu RNA, that directed the synthesis of the truncated mu protein, was about 350 bp smaller than the normal mu RNA. Furthermore, by primer extension analysis it was possible to localize this deletion in the mu RNA to a region 5' of CH1. Thus, a defect at the level of Ig gene structure/assembly that deletes coding information or results in aberrant RNA processing must be responsible for the truncated mu HCD protein BW.

Amino Acid Sequence↗
PubMed1994

First report of fludarabine in gamma-heavy chain disease.

We describe a case of gamma-heavy chain disease presenting with lymphadenopathy, splenomegaly, lytic lesions and bone marrow infiltration. Chemotherapy with epirubicin, chlorambucil and prednisolone produced a partial remission which lasted 5 months. The patient was then treated with fludarabine. After six courses of fludarabine a good partial remission was achieved which converted to complete remission with disappearance of the monoclonal IgG3 in the ensuing 12 months without further therapy. This response has, so far, been sustained for 2 1/2 years after stopping treatment.

Aged↗
PubMed1980

Primary structure of human gamma 3 immunoglobulin deletion mutant: gamma 3 heavy-chain disease protein Wis.

The complete sequence of a gamma 3 heavy-chain disease (HCD) protein Wis is presented. The molecule is a dimer of a 289-residue chain linked by 12 disulfide bonds. Protein Wis has an unusual amino terminus, followed by a deletion of most of the VH domain. After a small stretch homologous to the VC joining region, there is a second deletion which ends at the beginning of the quadruplicated hinge. Two carbohydrate groups are linked to Asn-6 and -140. the molecule has an extra interchain disulfide bridge at position 7 in addition to the 11 normally present in the quadruplicated hinge. The previously noted homology to the gamma 1 heavy chain is striking; from positions 224 to 234, protein Wis resembles gamma 1 Nei [Ponstingl, H., & Hilschmann, N. (1976) Hoppe-Seyler's Z. Physiol. Chem. 357, 1571--1604] except for a serine which replaces Asn at position 227. The results, taken together with studies of other immunoglobulin heavy-chain deletion mutants, support the suggestion that the different domains and interdomain regions of human H chains are coded for by different gene segments and that the deleted proteins reflect alterations in the recombination of different genes and/or the splicing of heterogeneous nuclear messenger ribonucleic acid (hn mRNA).

Amino Acid Sequence↗
PubMed1992

Mu-heavy chain disease: presentation as a benign monoclonal gammopathy.

mu-Heavy chain disease (HCD) is a rare monoclonal lymphoid disorder characterized by the failure to assemble a complete IgM immunoglobulin. The mu-heavy chains analyzed to date revealed absence of the variable region and a shortened constant domain. We report the first case of mu-HCD presenting as a benign monoclonal gammopathy. The literature on the 27 reported mu-HCD cases is reviewed, and important clinical and laboratory findings are discussed. The ages of the patients ranged from 15 to 80 years (median, 57.5 years). Twenty-two of 27 patients had an associated lymphoplasma cell proliferative disorder. A monoclonal spike on routine serum protein electrophoresis was found in only 8 of 19 patients. Fourteen of 22 patients had Bence Jones proteinuria, but mu-HCD protein was reported in the urine of only two patients. The survival ranged from less than 1 month to 11 years (median, 24 months).

Heavy Chain Disease↗
PubMed1989

Gamma heavy chain "disease": heterogeneity of the clinicopathologic features. Report of 16 cases and review of the literature.

This review underscores the diversity of the clinical manifestations and hematopathological features of gamma heavy chain disease based on the detailed report of 16 patients evaluated in our chemical department, the analysis of 12 cases diagnosed in our laboratory, and the study of 81 cases previously reported. This condition is defined by the presence in the serum of immunoglobulin molecules composed of deleted gamma heavy chains devoid of light chains. The production by the monoclonal B cells of these peculiar proteins appears to result from multiple defects (deletions, insertions, and mutations) in both heavy and light chain genes leading to abnormal mRNA splicing. Gamma heavy chain disease is currently underdiagnosed. The diagnosis established by immunoelectrophoresis using specific antisera combined, in some instances, with the immunoselection procedure, can easily be missed on serum electrophoretic patterns: a narrow abnormal band suggestive of a monoclonal component was found in only 10 of our 28 cases. The amount of heavy chain disease protein in urine ranges from trace to 20 g/day and is usually moderate. Gamma heavy chain disease most often presents as a lymphoproliferative disorder featured by lymphadenopathies, splenomegaly, and constitutional symptoms. Extra-hematopoietic tumor localizations, such as cutaneous or subcutaneous involvement or thyroid tumor, may occur. Autoimmune disorders, notably rheumatoid arthritis and autoimmune hemolytic anemia or thrombocytopenic purpura, are frequent (26% of cases). There is no specific histological pattern. The most frequent is a pleomorphic malignant lymphoplasmacytic proliferation mainly seen in bone marrow and lymph nodes. Some cases present with a predominantly plasmacytic proliferation or chronic lymphocytic leukemia. Other patients are affected with non-Hodgkin lymphoma of various morphologic types. Immunocytologic studies showed that a gamma heavy chain disease protein may occur in the context of a double monoclonal lymphoproliferative process or in various B or T cell malignancies that are not directly involved in the production of the abnormal immunoglobulin. In some patients, the histologic appearance of the enlarged lymphoid organs showed only a moderate lymphoplasmacytic infiltration of uncertain malignancy. More important, some patients showed no evidence of an underlying lymphoproliferative disorder after several years of follow-up. The clinical course of gamma heavy chain disease varies from an asymptomatic state to a rapidly progressive malignancy. The choice of therapy should entirely rely on the underlying clinicopathologic features, without taking into account the presence of the abnormal protein.(ABSTRACT TRUNCATED AT 400 WORDS)

Adult↗
PubMed1985

Gamma heavy chain disease: report of a case associated with trisomy of chromosome 7.

A case of gamma heavy chain disease is reported in a 52-year-old white male who presented with fever and generalized lymphadenopathy. A lymph node biopsy showed malignant lymphoma. A partial transient response was obtained with cyclophosphamide, vincristine, prednisone, and doxorubicin. He died 3 months after diagnosis from disease progression and infectious complications. Chromosome analysis of cells from an involved lymph node showed the presence of trisomy 7. Chromosome abnormalities have been reported in three of ten previously published cases of gamma heavy chain disease. Trisomy of chromosome #7 has not previously been reported.

Chromosome Aberrations↗
PubMed1975

IgA heavy chain disease. A case detected in the western hemisphere.

IgA heavy chain disease (alpha chain disease) was detected in a 46 year old South American (Colombian) of mixed Spanish and Indian (Mestizo) descent. The clinical course was characterized by severe malabsorption, initially thought to be a variant of tropical sprue. Jejunal mucosal biopsy revealed marked villous atrophy with heavy infiltration of the lamina propria by a single monotonous cell type which, by light microscopy, had the appearance of either a large, abnormal plasma cell or a small histiocyte. Electron microscopy of the biopsy specimen demonstrated the presence of abnormal plasma cells, lymphatic distention and abnormalities of surface epithelial cells. At autopsy a 6 by 3 cm mass was found in the right para-aortic area along with many firm 2 cm mesenteric and para-aortic lymph nodes. Histologic examination revealed the presence of a monotonous cell type similar to that found in the jejunal mucosal biopsy specimen.

Abdomen↗
PubMed1980

A gamma l heavy-chain disease protein *EST) lacking the entire VH and CHl domains.

A gamma l heavy-chain disease protein (EST) is described which lacks the entire VH and CHl domains and starts with the normal sequence of gamma l H-chains corresponding to the beginning of the hinger region (position 216). Although degradation cannot be excluded with certainty, it is probable that this protein is synthesized as an internally deleted gamma heavy-chain disease protein. Presumably a DNA recombination has occurred resulting in the deletion of the genes of coding for the VH and CHl domains with splicing of the precursor RNA to the sequence coding for the hinge region.

Amino Acid Sequence↗
PubMed1984

Alpha heavy-chain disease presenting as goiter.

A patient with alpha heavy-chain disease (alpha HCD) originally had presented with a goiter from an extramedullary plasmacytoma. Alpha HCD was diagnosed by both standard laboratory procedures and high-resolution two-dimensional gel electrophoresis. The fragment of the alpha chain had a molecular weight of 38,000 and consisted of seven major charge forms, with an isoelectric point range of 5.2-5.6. Since alpha HCD usually involves the gastrointestinal tract, the thyroidal involvement in this case is unusual.

Adult↗