Discovery of a gamma heavy chain disease in a patient followed-up for a lymphoplasma cell proliferative disorder

2016 ◽  
Vol 74 (3) ◽  
pp. 338-340
Author(s):  
Camille Humeau ◽  
Hélène Monjanel ◽  
François Schellenberg
Keyword(s):  
Heavy Chain ◽  
Heavy Chain Disease

Heavy chain disease

1972 ◽  
Vol 129 (5) ◽  
pp. 836a-837
Author(s):  
B. H. Novis
Keyword(s):  
Heavy Chain ◽  
Heavy Chain Disease

scholarly journals Gamma heavy chain disease: clinical aspects and characterization of a deleted, noncovalently linked gamma1 heavy chain dimer (BAZ)

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 495-505 ◽  
Author(s):  
GB Faguet ◽  
BP Barton ◽  
LL Smith ◽  
FA Garver
Keyword(s):  
Heavy Chain ◽  
Plasma Cells ◽  
Clinical Feature ◽  
Clinical Aspects ◽  
Submaxillary Glands ◽  
Underlying Malignancy ◽  
V Region ◽  
Allotypic Marker ◽  
Heavy Chain Disease

Abstract This report describes the clinical and immunoglobulin features of a patient with gamma heavy chain disease (HCD), who presented with a clinical picture suggestive of an underlying malignancy rather than the usual picture of lymphoma or granulomatous disease. A unique clinical feature was the nearly total replacement of the submaxillary glands by plasma cells. The patient's serum and urine contained a paraprotein, gammaHCD protein BAZ, which belongs to the gamma1 subclass and forms noncovalently linked dimers with a molecular weight of approximately 60,000 daltons. This mutant protein exhibited a deletion which encompassed most of the variable (V) region, the first constant domain (CH 1), and the hinge region. In addition, preliminary structural analyses demonstrated the replacement of alanine by glycine in position 431 of the carboxyterminal octadecapeptide. This substitution may possibly represent another allotypic marker on IgG1 proteins.

Heavy-Chain Disease

1968 ◽  
Vol 278 (22) ◽  
pp. 1195-1201 ◽  
Author(s):  
Leonard L. Ellman ◽  
Kurt J. Bloch
Keyword(s):  
Heavy Chain ◽  
Heavy Chain Disease

A 59-Year-Old Woman With Immunotactoid Glomerulopathy, Heavy-Chain Disease, and Non-Hodgkin Lymphoma

2004 ◽  
Vol 128 (6) ◽  
pp. 689-692
Author(s):  
Erica Jacobson ◽  
Gregory Sharp ◽  
Jeffrey Rimmer ◽  
Bruce MacPherson
Keyword(s):  
Hodgkin Lymphoma ◽  
Heavy Chain ◽  
Average Diameter ◽  
World Health ◽  
Heavy Chains ◽  
Non Hodgkin Lymphoma ◽  
Immunotactoid Glomerulopathy ◽  
History Of ◽  
Health Organization ◽  
Heavy Chain Disease

Abstract Immunotactoid glomerulopathy is one of several renal disorders characterized by the extracellular deposition of nonamyloid fibrillary deposits. There is considerable debate as to whether immunotactoid glomerulopathy should be distinguished from fibrillary glomerulonephritis, a closely related entity. Currently, the distinction is based on fibril size and arrangement. We report the case of a 59-year-old woman in whom a diagnosis of immunotactoid glomerulopathy was made after a 2-year history of proteinuria. Electron microscopy of her renal biopsy showed randomly arranged microtubular subepithelial and mesangial deposits, which measured 34 nm in average diameter. She was later discovered to have circulating immunoglobulin G heavy chains without associated light chains (γ-heavy-chain disease) and, subsequently, non-Hodgkin lymphoma, follicular lymphoma, grade I (World Health Organization classification). Approximately 100 cases of γ-heavy-chain disease have been reported in the literature since it was originally described by Franklin in 1964. However, while there are 10 reports in the literature of heavy-chain disease with fibrillary deposits in the kidney, none fit the criteria for immunotactoid glomerulopathy.

Composite Nodular Lymphocyte-Predominance Hodgkin Disease and γ-Heavy-Chain Disease

2001 ◽  
Vol 125 (6) ◽  
pp. 803-807
Author(s):  
S. David Hudnall ◽  
Jack B. Alperin ◽  
John R. Petersen
Keyword(s):  
Bone Marrow ◽  
Lymph Node ◽  
B Cell ◽  
Heavy Chain ◽  
Monoclonal Gammopathy ◽  
Hodgkin Disease ◽  
Graves Disease ◽  
Unique Case ◽  
History Of ◽  
Heavy Chain Disease

Abstract The association of Hodgkin disease with monoclonal gammopathy has rarely been reported. We present a case of a 48-year-old woman with a history of autoimmune hemolytic anemia and Graves disease who presented with hepatosplenomegaly and a γ-heavy-chain paraprotein. Histopathology of lymph node and bone marrow revealed nodular lymphocyte-predominance Hodgkin disease, while examination of the spleen revealed plasmacytosis consistent with γ-heavy-chain disease. Following splenectomy, the patient has remained in complete remission for both conditions with no further treatment. To our knowledge, this is the first report of a patient with both γ-heavy-chain disease and nodular lymphocyte-predominance Hodgkin disease. Given recent data indicating the B-cell nature of this form of Hodgkin disease, the authors propose that in this unique case there may be a clonal relationship between these 2 concurrent B-cell lymphoproliferative processes.

scholarly journals Gamma heavy chain disease: rapid, sustained response to cyclophosphamide and prednisone

Blood ◽  
1975 ◽  
Vol 46 (1) ◽  
pp. 1-9 ◽  
Author(s):  
RM Lyons ◽  
H Chaplin ◽  
TW Tillack ◽  
PW Majerus
Keyword(s):  
Molecular Weight ◽  
Heavy Chain ◽  
Keratoconjunctivitis Sicca ◽  
Coombs Test ◽  
Serum Complement ◽  
Covalent Linkage ◽  
Covalently Linked ◽  
Polypeptide Chains ◽  
Heavy Chain Disease ◽  
Low Serum

Abstract A patient, CAL, with gamma heavy chain disease is presented who has had a complete remission lasting over 2 yr with combination chemotherapy consisting of pulsatile cyclophosphamide and prednisone. The patient exhibited many features of an atuoimmune process including a vasculitis, low serum complement levels, a positive antiglobulin (Coombs) test, Raynaud's phenomenon, and keratoconjunctivitis sicca. The CAL paraprotein was found to have several previously undescribed characteristics. It reacted with antisera to Fd, Fab, and Fab', suggesting that most of the Fd portion of the molecule was intace. CAL protein consists of two polypeptide chains of molecular weight 49,000 covalently linked to form a dimer of 95,000 molecular weight. The covalent linkage suggests that the hinge region of this gamma heavy chain is intact.

A New Case of Gamma Heavy Chain Disease: Clinical, Immunochemical and Structural Characterization

Vox Sanguinis ◽  
1979 ◽  
Vol 37 (2) ◽  
pp. 89-95
Author(s):  
A.O. Carbonara ◽  
W. Paolino ◽  
F. Malavasi ◽  
A. Levis ◽  
A. Stramignoni ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Structural Characterization ◽  
Heavy Chain Disease

Heavy chain disease

2002 ◽  
Vol 3 (3) ◽  
pp. 247-254 ◽  
Author(s):  
Thomas E. Witzig ◽  
Dietlind L. Wahner- Roedler
Keyword(s):  
Heavy Chain ◽  
Heavy Chain Disease
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