Immunoglobulin D Research Articles

Purification of glycopeptides of human ceruloplasmin and immunoglobulin D by high-pressure liquid chromatography

To facilitate structural studies of glycoproteins, reverse-phase high-pressure liquid chromatography (HPLC) methods have been developed for preparative isolation of glycopeptides and have been applied to human ceruloplasmin as an example of glycopeptides containing glucosamine (GlcN) and to human immunoglobulin D (IgD) for glycopeptides containing galactosamine (GalN). The use of RP-P columns and of trifluoroacetic acid and heptafluorobutyric acid as counterions was investigated. Various elution systems (both isocratic and programmed gradient) were used with n-propanol to assess the relative hydrophilicity of the peptides. The procedure developed for the GlcN glycopeptides of ceruloplasmin enabled purification of nine major chymotryptic peptides (ranging in size from 15 to 29 residues) and also of many minor peaks. These were characterized by amino acid and endgroup analysis, and the complete sequence of five was determined. These represent three different sites of GlcN attachment in the amino-terminal half of the ceruloplasmin chain. The procedures developed have enabled isolation of glycopeptides from ceruloplasmin having a single GlcN oligosaccharide attached; the latter are valuable for study of the structure and function of the carbohydrate groups. Separation of GalN glycopeptides from IgD was more difficult because of the high content of GalN in the hinge. Purification and sequence analysis was aided by partial removal of sugar by treatment with HF and by other methods. Four (or five) GalN oligosaccharides are attached to serine or threonine residues in the IgD hinge region, and all but one are in close proximity in the repeating sequence Ala-Thr-Thr-Ala-Pro-Ala-Thr-Thr.

Human B cell differentiation. II. Pokeweed mitogen-responsive B cells belong to a surface immunoglobulin D-negative subpopulation.

Surface immunoglobulin D (IgD)-positive lymphocytes precoated with monoclonal anti-delta antibody were selectively removed from blood mononuclear cell preparations by "panning" and by fluorescence-activated cell sorter. The depletion of sIgD+ cells did not significantly affect plasma cell responses to pokeweed mitogen PWM). PWM-responsive B cells lacking sIgD and mouse erythrocyte receptors preferentially sedimented in lower density fractions of a discontinuous Percoll gradient, and sIgD-negative B cells were found to have a larger mean diameter than IgD-positive cells. We conclude that PWM-responsive B cells represent a distinct subpopulation of relatively large cells that have ceased to express receptors for mouse erythrocytes and surface IgD.

A search for association between IgD concentrations and immunoglobulin allotypes in 936 sera from a genetic isolate in Newfoundland.

Immunoglobulin allotype (Gm) data has been analysed agaonst immunoglobulin D (IgD) concentrations in a population study in Newfoundland. There was no significant difference between the distribution of IgD concentrations in people homozygous for the alleles G1m(f) and G3m(b) when compared with people homozygous for the alleles G1m(a) and G3m(g). These findings, involving 573 homozygous individuals as opposed to ninety-eight in an earlier study on a New York population, do not confirm the earlier findings. Thus a genetic influence on IgD concentration by Gm genes or genes closely linked to them is not universally demonstrable by typing for these four markers and by using the Mancini technique for mearusing IgD concentration.

Structure and biological functions of human IgD. IV. Ontogeny of human serum immunoglobulin D(IgD) as related to IgG, IgA and IgM.

The ontogeny of serum IgG, IgA, IgM and IgD in 312 members of a southern United States population was studied. Circulating IgD was found in all adolescents and in 97% of the adults tested. IgD levels increased until adult life. Females had statistically significantly higher levels of Igtd than did the males of their respective age groups. The children investigated showed an accelerated development of adult levels of all immunoglobulins, particularly IgG, IgM and IgD. These departures from previously reported norms emphasize the importance of regional variability and demonstrate the necessity for characterizing local patterns of humoral immunologic development. Our total lack of knowledge concerning the biological function of IgD could be corrected if more laboratories would measure IgD as part of their routine immunoglobulin screening programs.

The conformation of human immunoglobulin D

1. Introduction Human immunoglobulin D (IgD) is present in low concentrations in normal human serum, usually less than 1% of the total immunoglobulin population [l] . Little is known of the physiological role of this immunoglobulin class since IgD molecules appear to lack the structural requirements for many effector functions, such as skin sensitisation and complement activation [2]. There have also been few reports of antibody activity associated with IgD. However, recent work suggests that IgD may be particularly active as a lymphocyte membrane antigen receptor [3]. Chemically-derived data, such as the lack of convincing homology of the ‘hinge’ region with other human immunoglobulin heavy chain sequences [4], the comparatively low proline content [5] , the distinctive susceptibility to proteolysis and high carbohydrate content [6], all suggest a unique structure of IgD within the general immunoglobulin structural pattern of two heavy and two light poly- peptide chains. We have studied two isolated IgD myeloma proteins using circular dichroism (CD) and isoelectric focusing (IEF) in order to try to clarify any unusual structural features of the molecule that could be responsible for the distinctive physiological behaviour of this immuno- globulin class. Neither the IEF pattern nor the CD spectra of IgD have been reported previously. 2. Materials and methods Serum from tyo patients (A and B) suffering from multiple myeloma (IiD) were generous gifts from 310 Dr I. C. M. MacLennan and Dr 0. Cromwell, respectively. Following precipitation with 19.3% ammonium sulphate containing 4%

IgD on cell membranes of human lymphoid cell lines with multiple immunoglobulin classes.

IMMUNOGLOBULIN D (IgD) is present in minute amounts in the serum and the biological role of this immunoglobulin class is unknown1. The finding that a high proportion of lymphocytes bear IgD on their surface membrane2 has triggered renewed interest in this molecule.

IgD myeloma with amyloid arthropathy

A case of Immunoglobulin D (IgD) myeloma with amyloid arthropathy is described. The patient presented with bilateral symmetrical enlargement of multiple joints with subcutaneous nodules; the clinical picture suggested the diagnosis of rheumatoid arthritis. At necropsy, however, the joint swelling and nodules were proved to be amyloid deposition.

Extramedullary plasmacytomas following successful radiotherapy of Hodgkin's disease: Clinical and immunologic aspects

A patient with multiple extramedullary plasmacytomas is described, with particular attention to the protein abnormalities. A lambda type Bence Jones protein and elevated serum levels of immunoglobulin D (IgD) were demonstrated as well as the in vitro biosynthesis of the lambda light chain by the plasma cells from a subcutaneous plasmacytoma. It seems probable that the particular clone of cells studied in vitro retained only the ability to manufacture the lambda type light chain.

Plasma Cell Leukemia With IgD Paraprotein

Immunoglobulin D (IgD) has been recently established as a new fourth member of the immunoglobulin family. It was discovered by Rowe and Fahey¹in 1965 in a patient with multiple myeloma and later it was found to be present in the serum of normal human subjects. Its biological functions and roles in the immune mechanisms are still unknown. D-myelomas are quite rare. Only a few reports have appeared in the literature.^2-7 In the present communication a patient with plasma cell leukemia with IgD paraprotein will be described. This is, to our knowledge, the first reported case. <h3>Materials and Methods</h3> Routine hematological examinations were performed according to Dacie and Lewis.⁸Electrophoresis of serum and urine were done on paper, cellulose acetate, and starch gel according to techniques described by Kohn⁹and Smithies.¹⁰Immunoelectrophoresis and immunodiffusion of serum and urine were performed according to Scheidegger,¹¹and

Quantitative determination of serum immunoglobulin D in gammopathy.

Serum immunoglobulin D (IgD) level was determined in 10 normal subjects, 5 cases of IgD-myeloma and 23 cases of various autoimmune diseases by the antibody-agar plate method using the antiserum against the heavy chain of IgD, which had been prepared in a rabbit immunized with an IgD-myeloma protein. The serum IgD level was below 0.05mg/ml in normal subjects and above 10mg/ml in IgD-myeloma cases. In one case, IgD levels were serially followed; the level dropped to 1.0mg/ml by administration of cyclophosphamide. More than a half of cases of various autoimmune diseases showed the serum IgD levels of above 0.05mg/ml. The highest level in this autoimmune disease group was 0.14mg/ml in a case of aortitis. All of the 4 cases of aortitis studied showed IgD levels of above 0.05mg/ml. Whether serum IgD elevation in autoimmune diseases is an expression of general elevation of immunoglobulins or represents the elevation of antibodies specific for these diseases awaits further studies.

Metabolism of human immunoglobulin D (IgD).

Metabolism of human immunoglobulin D (IgD).

Serum immunoglobulin levels in cystic fibrosis.

CYSTIC fibrosis provides an opportunity to study the immunoglobulin response of children, adolescents, and young adults who have chronic pulmonary bacterial infection, yet who seem to be resistant to secondary acute bacterial complications such as septicemia and meningitis. Until recently, three main classes of human serum immunoglobulins have been recognized: IgG (Immunoglobulin G, γG, or 7S γ2-globulin), IgA (Immunoglobulin-A, γ A, γ1A, or β2A-globulin), IgM (Immunoglobulin-M, γM, γ1M, β2M, or 19S γ1-macroglobulin). Antibody activity has been associated with each of these classes. A fourth class, IgD (Immunoglobulin-D), has been added to this list;1however, its function has yet to be elucidated. Although hypergammaglobulinemia has been well described in cystic fibrosis,2quantitative documentation of the immunoglobulin classes affected has not been recorded. The present study was undertaken to determine which immunoglobulin classes are involved in the serologic response to chronic pulmonary infection in cystic fibrosis. Since IgA is the