scholarly journals Studies on J-chain biosynthesis in tumours producing immunoglobulins in NZB mice

1976 ◽  
Vol 156 (3) ◽  
pp. 681-684 ◽  
Author(s):  
H Kaji
Keyword(s):  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
J Chain ◽  
Myeloma Proteins ◽  
Mouse Myeloma

Investigation of biosynthesis of J chain in plasmacytomas induced in NZB mice revealed that this protein was not only synthesized in the cells that produce polymer immunoglobulin A but also in those that produce immunoglobulin G monomer. It was also found that protein similar to J chain of BALB/c-mice was associated with polymer immunoglobulin A but not with immunoglobulin G of NZB mouse myeloma proteins.

scholarly journals Biosynthesis of immunoglobulin A (IgA). Secretion and addition of carbohydrate to monomer and polymer forms of a mouse myeloma protein

1973 ◽  
Vol 136 (3) ◽  
pp. 589-596 ◽  
Author(s):  
E. Della Corte ◽  
R. M. E. Parkhouse
Keyword(s):  
Plasma Cell ◽  
Molecular Species ◽  
Specific Antibody ◽  
Early Stage ◽  
Immunoglobulin A ◽  
Carbohydrate Composition ◽  
Myeloma Protein ◽  
J Chain ◽  
Co Precipitation ◽  
Mouse Myeloma

Cell suspensions of mouse plasma-cell tumour MOPC 315 secreting predominantly IgA (immunoglobulin A) monomer and dimer were incubated with radioactive leucine, mannose, galactose and fucose for various periods of time. The amounts of secreted and intracellular immunoglobulins were measured by co-precipitation with specific antibody, and the molecular species present were assessed by electrophoresis in polyacrylamide gels. Analysis of the secreted myeloma protein demonstrated that monomer and dimer IgA molecules are identical with respect to carbohydrate composition and rate of secretion. Within the cell, the myeloma protein is almost entirely accounted for by monomer units which either leave the cell as such or are polymerized with the addition of J chain close to the time of secretion. The results support the concept of a stepwise addition of carbohydrate residues to IgA immunoglobulin during the process of secretion. Similar patterns of carbohydrate assembly were found for the monomer or dimer molecules. Mannose residues are added at an early stage, whereas fucose is added close to the time of secretion. Galactose is also added early, but some may also be incorporated at a later stage. Control of IgA polymerization is considered unlikely to reflect regulation at the level of carbohydrate addition, and it is suggested that the critical controlling factor is the J chain.

scholarly journals Resonance Raman-spectroscopic studies of the hapten features involved in the binding of 2,4-dinitrophenyl haptens by the mouse myeloma proteins MOPC 315 and MOPC 460

1978 ◽  
Vol 175 (2) ◽  
pp. 727-735 ◽  
Author(s):  
K Kumar ◽  
D J Phelps ◽  
P R Carey ◽  
N M Young
Keyword(s):  
Binding Sites ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Immunoglobulin A ◽  
Spectroscopic Studies ◽  
Side Chain ◽  
Raman Spectroscopic ◽  
Myeloma Proteins ◽  
Resonance Raman Spectra ◽  
Mouse Myeloma

The binding of four dinitrophenyl haptens to the mouse myeloma proteins MOPC 315 IgA (immunoglobulin A) and MOPC 460IgA was studied by resonance Raman spectroscopy. Isotopic substitution with 15N and 2H was used to assign features in the resonance Raman spectra of the free haptens. Changes in each of these features on binding to the proteins could then be attributed to interactions of the proteins' binding sites with either the p-NO2 or the o-NO2/amine regions of the haptens. The interactions between a given hapten and MOPC 315 IgA are often quite distinct from those between the same hapten and MOPC 460 IgA. Moreover, for both antibodies the nature of the R side chain in a Dnp-NHR (Dnp, 2,4-dinitrophenyl) compound appears to modify the interactions between the Dnp chromophore and the protein. Thus, with the haptens studied, there is no unique set of contacts between the Dnp group and the binding site. The contacts expected between epsilon-2,4-dinitrophenyl-L-lysine and the site on MOPC 315 IgA, on the basis of a recent model for this site [Dwek, Wain-Hobson, Dower, Gettins, Sutton, Perkins & Givol (1977) Nature (London) 266, 31–37] were not detected. However, the contacts between this hapten and the site on MOPC 460 IgA were closer to those predicted by the model for MOPC 315 IgA.

scholarly journals Evaluation of the INOVA Diagnostics Enzyme-Linked Immunosorbent Assay Kits for Measuring Serum Immunoglobulin G (IgG) and IgA to Deamidated Gliadin Peptides

2006 ◽  
Vol 13 (1) ◽  
pp. 150-151 ◽  
Author(s):  
Harry E. Prince
Keyword(s):  
Celiac Disease ◽  
Immunosorbent Assay ◽  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
Serum Immunoglobulin ◽  
Enzyme Linked Immunosorbent Assay ◽  
Gliadin Antibodies ◽  
Gliadin Peptides ◽  
Disease Specific ◽  
Inova Diagnostics

ABSTRACT New assays for antibodies to deamidated gliadin peptides (DGP) expressing celiac disease-specific epitopes were evaluated using 154 sera previously tested for endomysial immunoglobulin A (IgA) (EMA), transglutaminase IgA (TGA), and conventional gliadin antibodies. DGP antibody results showed 97% concordance with EMA and TGA results. Of 56 sera negative for EMA and TGA but positive for conventional gliadin antibodies, 54 (96%) were negative for DGP antibodies.

Commensal bacteria coated by secretory immunoglobulin A and immunoglobulin G in the gastrointestinal tract of pigs and calves

2012 ◽  
Vol 83 (12) ◽  
pp. 799-804 ◽  
Author(s):  
Takeshi TSURUTA ◽  
Ryo INOUE ◽  
Takamitsu TSUKAHARA ◽  
Mitsunori NAKAMOTO ◽  
Hiroshi HARA ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
Commensal Bacteria ◽  
Secretory Immunoglobulin A ◽  
Secretory Immunoglobulin

scholarly journals The subunit and polypeptide-chain structure of rabbit secretory immunoglobulin A. Isolation of a proteolytic fragment suitable for sequence studies on the variable region of α-chain

1977 ◽  
Vol 167 (1) ◽  
pp. 245-253 ◽  
Author(s):  
A P Johnstone ◽  
L E Mole
Keyword(s):  
Immunoglobulin G ◽  
Polypeptide Chain ◽  
Immunoglobulin A ◽  
Variable Region ◽  
Chain Structure ◽  
Secretory Immunoglobulin A ◽  
Primary Sequence ◽  
Relative Resistance ◽  
Proteolytic Fragment ◽  
Secretory Immunoglobulin

A method was developed for the preparation of a proteolytic fragment of rabbit secretory immunoglobulin A (sIgA) which contains the variable region of the alpha-chain; this fragment is suitable for primary-sequence studies. The serologically defined subclasses of sIgA are shown to correlate partially with the nature of the binding of a constituent chain of sIgA, called secretory piece. Data are also presented on the relative resistance of sIgA to enzymic and reductive cleavage, compared with immunoglobulin G.

scholarly journals Six catalytic activities and cytotoxicity of immunoglobulin G and secretory immunoglobulin A from human milk

2021 ◽  
Author(s):  
Georgy A. Nevinsky ◽  
Ol'ga D. Zakharova ◽  
Ivan Yu. Kompaneets ◽  
Anna M. Timofeeva ◽  
Pavel S. Dmitrenok ◽  
...  
Keyword(s):  
Human Milk ◽  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Catalytic Activities ◽  
Secretory Immunoglobulin

scholarly journals Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin

2020 ◽  
Author(s):  
Yuxin Wang ◽  
Guopeng Wang ◽  
Yaxin Li ◽  
Hao Shen ◽  
Huarui Chu ◽  
...  
Keyword(s):  
Specific Interaction ◽  
Immunoglobulin A ◽  
Underlying Mechanism ◽  
Secretory Component ◽  
Secretory Immunoglobulin A ◽  
Immunoglobulin Receptor ◽  
J Chain ◽  
Cryo Electron Microscopy ◽  
Structural Insights ◽  
Secretory Immunoglobulin

AbstractSecretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. SIgA possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. The underlying mechanism of how the J-chain and pIgR/SC facilitates the assembly and secretion of SIgA remains to be understood. During the infection of Streptococcus pneumoniae, a pneumococcal adhesin SpsA hijacks SIgA and unliganded pIgR/SC to evade host defense and gain entry to human cells. How SpsA specifically targets SIgA and pIgR/SC also remains unclear. Here we report a cryo-electron microscopy structure of the Fc region of human IgA1 (Fcα) in complex with J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present the structure of Fcα-J-SC in complex with SpsA, which uncovers the specific interaction between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on the pathogenesis of S. pneumoniae.

Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levan

1972 ◽  
Vol 9 (5) ◽  
pp. 535-544 ◽  
Author(s):  
Arne Lundblad ◽  
Richard Steller ◽  
Elvin A Kabat ◽  
Judith W Hirst ◽  
Martin G Weigert ◽  
...  
Keyword(s):  
Myeloma Proteins ◽  
Mouse Myeloma

Major Immunoglobulin Ratios in Carcinoma of the Head and Neck

1978 ◽  
Vol 87 (3) ◽  
pp. 412-415 ◽  
Author(s):  
Arnold E. Katz ◽  
John O. Nysather ◽  
Lee A. Harker
Keyword(s):  
Head And Neck ◽  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
Elevated Serum ◽  
Immunoglobulin M ◽  
Serum Immunoglobulin ◽  
Control Groups ◽  
Immunoglobulin Production ◽  
Patients With Cancer ◽  
Serum Iga

— Serum immunoglobulin A (IgA), immunoglobulin G (IgG), and immunoglobulin M (IgM) levels were determined on 245 patients with carcinoma of the head and neck and on 92 controls. Ratios of these levels were calculated for each subject. The patients with cancer demonstrated elevated serum IgA levels ( P <.0001) and elevated IgA/IgM and IgA/IgG ratios ( P <.05). No differences were noted when the IgM/IgG ratios were compared between the cancer and the control groups. These observations are offered as evidence that previously reported elevations of serum IgA levels in patients with carcinoma of the head and neck are not merely an index of nonspecific increased immunoglobulin production in these patients.

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