scholarly journals Evidence that the Fc region of autologous rabbit IgG isolated before and after hyperimmunization is structurally different: recognition by rheumatoid factor and monoclonal antibodies

2008 ◽  
Vol 81 (2) ◽  
pp. 286-292 ◽  
Author(s):  
J. S. MURRAY ◽  
J. C. BROWN
Keyword(s):  
Monoclonal Antibodies ◽  
Rheumatoid Factor ◽  
Rabbit Igg ◽  
Before And After

Prostate-specific antigen in serum occurs predominantly in complex with alpha 1-antichymotrypsin

1991 ◽  
Vol 37 (9) ◽  
pp. 1618-1625 ◽  
Author(s):  
H Lilja ◽  
A Christensson ◽  
U Dahlén ◽  
M T Matikainen ◽  
O Nilsson ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Monoclonal Antibodies ◽  
Serum Concentration ◽  
Prostate Specific Antigen ◽  
Proteinase Inhibitors ◽  
Specific Antigen ◽  
Serine Proteinase ◽  
Gel Chromatography ◽  
Extracellular Proteinase ◽  
Rabbit Igg

Abstract Immunologic measurements of the serum concentration of prostate-specific antigen (PSA), an abundant prostatic-secreted serine proteinase, are frequently used to monitor patients with prostate cancer, though it has not been ascertained whether this immunoreactivity represents a PSA zymogen, the active proteinase, or PSA complexed to extracellular proteinase inhibitors. To characterize the PSA immunoreactivity in serum, we used monoclonal antibodies produced against PSA and a polyclonal rabbit IgG against alpha 1-antichymotrypsin in the design of three noncompetitive PSA assays: assay T, which detected PSA both when present as the active proteinase and when complexed to alpha 1-antichymotrypsin; assay F, which recognized the active proteinase but most poorly detected PSA complexed to alpha 1-antichymotrypsin; and assay C, which was specific for PSA complexed to alpha 1-antichymotrypsin. We used the three assays to measure PSA immunoreactivity in 64 patients' sera and in the effluent after gel chromatography of sera from four patients. This identified an 80- to 90-kDa complex between PSA and alpha 1-antichymotrypsin as the predominant fraction of the PSA immunoreactivity in blood plasma; an immunoreactive 25- to 40-kDa compound was the minor fraction.

scholarly journals Human cholesteryl ester transfer protein measured by enzyme-linked immunosorbent assay with two monoclonal antibodies against rabbit cholesteryl ester transfer protein: plasma cholesteryl ester transfer protein and lipoproteins among Japanese hypercholesterolemic patients

1998 ◽  
Vol 44 (7) ◽  
pp. 1466-1473 ◽  
Author(s):  
Kanna Sasai ◽  
Kuniko Okumura-Noji ◽  
Takeshi Hibino ◽  
Reiko Ikeuchi ◽  
Nagahiko Sakuma ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cholesteryl Ester ◽  
Cholesteryl Ester Transfer Protein ◽  
Ldl Cholesterol ◽  
Hdl Cholesterol ◽  
Enzyme Linked Immunosorbent Assay ◽  
Transfer Protein ◽  
Plasma Cholesteryl Ester ◽  
Luminal Stenosis ◽  
Before And After

Abstract Plasma cholesteryl ester transfer protein (CETP) concentrations were measured in Japanese subjects by an ELISA with two different monoclonal antibodies that were raised against rabbit CETP and cross-reacted against human CETP. Among 63 patients who consecutively underwent coronary angiography, the plasma CETP of 37 patients with luminal stenosis ≥50% in their coronary arteries was not significantly different from that of the 26 patients with luminal stenosis <50%. No other lipoprotein-related measurement except HDL-cholesterol differentiated the two groups. Among 40 hypercholesterolemic patients, no lipoprotein-related measurement other than LDL-cholesterol was found to positive correlate with the CETP. Before and after the treatment of 23 patients with simvastatin 5 mg a day for 4 weeks, plasma CETP markedly decreased in those whose pretreatment CETP was ≥3 mg/L; no change was observed for those with lower pretreatment CETP. In the former group, negative correlation between CETP and HDL-cholesterol was demonstrated only in the posttreatment plasma.

Improved agarose electrophoretic method for separating alkaline phosphatase isoenzymes in serum.

1988 ◽  
Vol 34 (9) ◽  
pp. 1857-1862 ◽  
Author(s):  
V O Van Hoof ◽  
L G Lepoutre ◽  
M F Hoylaerts ◽  
R Chevigné ◽  
M E De Broe
Keyword(s):  
Alkaline Phosphatase ◽  
Monoclonal Antibodies ◽  
Polyclonal Antibody ◽  
High Molecular Mass ◽  
High Reproducibility ◽  
Neuraminidase Treatment ◽  
Electrophoretic Method ◽  
Electrophoretic Mobilities ◽  
Before And After ◽  
Alkaline Phosphatase Isoenzymes

Abstract A modified agarose electrophoretic system for the separation of alkaline phosphatase (ALP, EC 3.1.3.1) isoenzymes is described. Bone, liver, high-molecular-mass, and intestinal ALP are separated with high reproducibility. The sensitivity of the agarose system is superior to cellulose acetate in detecting high-Mr ALP. Correlation is good between bone ALP fractions scanned before and after treatment with neuraminidase. Immunoglobulin-bound ALPs, the ALP-lipoprotein-X complex, and the additional ALP fraction observed in transient hyperphosphatasemia in children are detected by their peculiar electrophoretic mobility in the proposed system. Approximately 25% of the samples contained an additional fraction of intestinal-type ALP, as evidenced by neuraminidase treatment and use of polyclonal and monoclonal antibodies. Because the electrophoretic mobilities of this "intestinal variant" and of some immunoglobulin-bound ALP fractions are identical to those of bone and intestinal ALP, respectively, treatment of the samples with a polyclonal antibody that reacts with intestinal ALP is advised.

scholarly journals COMPLEMENT FIXATION BY A TWO-COMPONENT ANTIBODY SYSTEM: IMMUNOGLOBULIN G AND IMMUNOGLOBULIN M ANTI-GLOBULIN (RHEUMATOID FACTOR)

1970 ◽  
Vol 132 (4) ◽  
pp. 673-693 ◽  
Author(s):  
Frank R. Schmid ◽  
Ivan M. Roitt ◽  
Maria J. Rocha
Keyword(s):  
Rheumatoid Factor ◽  
Complement Fixation ◽  
Direct Interaction ◽  
Fluid Phase ◽  
Kinetic Studies ◽  
Immunoglobulin M ◽  
Inhibitory Potency ◽  
Cell Agglutination ◽  
Igm Rheumatoid Factor ◽  
Rabbit Igg

Complement-mediated lysis of sheep erythrocytes coated with optimal concentrations of rabbit IgG hemolysin was inhibited by euglobulin fractions from the sera of patients with seropositive rheumatoid arthritis. That this was due to direct interaction with the IgG coat on the red cell rather than a nonspecific reaction with complement in the fluid phase was confirmed by controls using cells coated with IgM hemolysin. The inhibitory activity was recovered in purified IgM rheumatoid factor preparations and could be absorbed out with insoluble aggregated human IgG. The inhibitory potency of the rheumatoid factors correlated well with their sheep cell agglutination titers. Inhibition was not the result of physical aggregation of the erythrocytes by rheumatoid factor. Kinetic studies were consistent with the view that rheumatoid factor displaces C1q from its binding to IgG. Paradoxically, at suboptimal sensitizing concentrations of IgG hemolysin, rheumatoid factor enhances the fixation of complement. These results can be interpreted on the basis of the blockage of complement fixation by IgG and its replacement by a relatively weak direct fixation by the IgM rheumatoid factor. Thus, the interaction of RF with IgG generates only a limited ability to fix complement which, when contrasted with the fixation at suboptimal concentrations of IgG hemolysin alone, appears as net enhancement; when this is contrasted with fixation occurring with optimal concentrations of IgG, it appears as net inhibition.

Characterization of Antibodies Direct against the Idiotypic VK3 Chain of HCV-Related Type-II Mixed Cryoglobulinemia and B-Cell Proliferations

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 4988-4988
Author(s):  
Valli De Re ◽  
Maria Paola Simula ◽  
Alessandro Pavan ◽  
Dolores Marin ◽  
Laura Caggiari ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
B Cells ◽  
Western Blot ◽  
B Cell ◽  
Rheumatoid Factor ◽  
Light Chain ◽  
B Cell Lymphoma ◽  
Type Ii ◽  
Cell Proliferations

Abstract Autoimmune type-II cryoglobulinemia (MC) is sustained by clonal/oligoclonal B-cell populations such the disease may be considered an “indolent B-cell lymphoma (NHL) “ and may favor overt NHL development. HCV-antigen driven mechanism induces B-cell proliferations. Clonal B-cells demonstrate a restricted used of variable genes to construct the B-cell receptor (BCR) and a homology between BCR functional regions and autoimmune rheumatoid factor (RF) activity. We underline the BCR unique repertoire with frequent rheumatoid factor activity also in other autoimmune disorders associated to NHL development as Sjogren’s syndrome and rheumatoid arthritis. All together these BCRs are characterized by their high degree of idiotypic (Id) cross reactivity. Particularly the K chain V3-20/15 is frequently found in subject with positive HCV antibody. Id is a clonamarker expressedby B cells, thus is an ideal target for immunotherapy. The evidence of few Id presented in the NHL subgroup above reported constitute the rational for the development of antibodies and recombinant proteins that use shared Id among different NHL. Five monoclonal antibodies have been produced in our laboratory toward the VK3-20 region of a subject HCV+ with NHL. Epitopes recognized has been performed using epitope excision approach. A fine determination of the antibodies activities toward specific amino acids, possibly common to different individuals, are in progress. Monoclonal antibodies reactivity has been tested in vitro in ELISA, western blot and cytofluorimetry. Apoptosis and SyK/ERK phosphorylation pathways induced following BCR cross-linking of antiId murine IgG will be performed. All the antibodies were reactive in Elisa against the VK3-Ig light chain. Two of these antibodies showed a reactivity against the light chain of cryoprecipitated immunocomplexes from several patients in western blot, and by cytofluorimter they recognised two lymphoma B-cell lines.

Platelet Agglutinating Protein p37 Causes Platelet Agglutination through its Binding to Membrane Glycoprotein IV

1991 ◽  
Vol 65 (01) ◽  
pp. 102-106 ◽  
Author(s):  
Eric C-Y Lian ◽  
Farooq A Siddiqui ◽  
G A Jamieson ◽  
Narendra N Tandon
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Receptor Site ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Thrombocytopenic Purpura ◽  
Normal Platelet ◽  
Reducing Conditions ◽  
Rabbit Igg

SummaryA 37 kDa platelet agglutinating protein (PAP p37) has previously been shown to be present in a subset of patients with thrombotic thrombocytopenic purpura and has been purified from their plasma. Using solubilized platelet membrane proteins from normal donors, it was shown by Western blotting that r2sI-p37 bound to a membrane protein of 97 kDa (red/unred). Furthernore, the same protein was identified by reverse immunoblotting in which purified p37 was electrophoresed, transferred to the nitrocellulose sheet and incubated with solubilized normal platelet membrane proteins. The complex formed between p37 and the membrane protein was identified by autoradiography using polyclonal and monoclonal (OKM5) anti- GPIV antibodies, but was not detected by polyclonal antibody to GPIIIa. Similar studies with purified platelet GPIV under both reducing and non-reducing conditions demonstrated the binding of 125I-p37. Polyclonal and monoclonal antibodies to GPIV completely inhibited the platelet agglutination induced by TTP plasma containing p37, however, normal rabbit IgG, rabbit anti- GPIIIa IgG, and murine monoclonal anti-GPIIb/IIIa (10E5) antibodies had no effect. These data indicate that platelet GPIV is the receptor site for PAP p37.

scholarly journals Interaction of rheumatoid factor and Entamoeba histolytica

1989 ◽  
Vol 31 (4) ◽  
pp. 207-212
Author(s):  
P.G. Kremsner ◽  
W. Graninger
Keyword(s):  
Human Serum ◽  
Rheumatoid Factor ◽  
Entamoeba Histolytica ◽  
Normal Human Serum ◽  
Cytotoxicity Test ◽  
Marked Inhibition ◽  
Rabbit Igg ◽  
Lysis Rate ◽  
Normal Human

The amoebae's cytotoxicity test and the amoebae's lysis test were used to show possible interactions between rheumatoid factor (RF) and Entamoeba histolytica. Amoebae's cytotoxic activity (ACA) was inhibited by affinity chromatography purified antiamoebae rabbit IgG (RIgG). Enhanced inhibition could be demonstrated with RIgG plus RF. But the same marked inhibition of ACA could be seen when replacing RF by heat inactivated normal human serum as a control. About 50% amoebae's lysis occurred when amoebae were brought together with native normal human serum (NNHS) as a source of complement. Amoebae's lysis increased to 60% when incubated with NHS plus human antiamoebae antibodies. No further augmentation could be obtained by the addition of RF. Using RIgG instead of human antibodies the lysis rate did not increase. Incubation of amoebae, NNHS, RIgG and RF even reduced amoebae's lysis. RF neither has an effect on ACA nor on complement mediated AL in vitro.

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