scholarly journals Cryoprecipitogogue from normal serum: mechanism for cryoprecipitation of immune complexes.

1981 ◽  
Vol 78 (7) ◽  
pp. 4562-4565 ◽  
Author(s):  
J. A. Hardin
Keyword(s):  
Immune Complexes ◽  
Normal Serum

scholarly journals A broad screen for targets of immune complexes decorating arthritic joints highlights deposition of nucleosomes in rheumatoid arthritis

2009 ◽  
Vol 106 (37) ◽  
pp. 15867-15872 ◽  
Author(s):  
Paul A. Monach ◽  
Wolfgang Hueber ◽  
Benedikt Kessler ◽  
Beren H. Tomooka ◽  
Maya BenBarak ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Extracellular Matrix ◽  
Immune Complexes ◽  
Protein Microarrays ◽  
Normal Serum ◽  
Intracellular Protein ◽  
Cartilage Surface ◽  
Diversity Of Components ◽  
Arthritic Joints ◽  
Proteins And Peptides

Deposits of Ig and complement are abundant in affected joints of patients with rheumatoid arthritis (RA) and in animal models of RA in which antibodies are demonstrably pathogenic. To identify molecular targets of the Igs deposited in arthritic joints, which may activate local inflammation, we used a combination of mass spectrometry (MS) and protein microarrays. Immune complexes were affinity-purified from surgically removed joint tissues of 26 RA and osteoarthritis (OA) patients. Proteins complexed with IgG were identified by proteomic analysis using tandem MS. A striking diversity of components of the extracellular matrix, and some intracellular components, copurified specifically with IgG from RA and OA tissues. A smaller set of autoantigens was observed only in RA eluates. In complementary experiments, IgG fractions purified from joint immune complexes were tested on protein microarrays against a range of candidate autoantigens. These Igs bound a diverse subset of proteins and peptides from synovium and cartilage, different from that bound by normal serum Ig. One type of intracellular protein detected specifically in RA joints (histones H2A/B) was validated by immunohistology and found to be deposited on the cartilage surface of RA but not OA joints. Thus, autoantibodies to many determinants (whether deposited as “neoantigens” or normal constituents of the extracellular matrix) have the potential to contribute to arthritic inflammation.

scholarly journals Normal serum levels of immune complexes in postpolio patients

2014 ◽  
Vol 4 ◽  
pp. 54-57 ◽  
Author(s):  
Eva Melin ◽  
Azita Sohrabian ◽  
Johan Rönnelid ◽  
Kristian Borg
Keyword(s):  
Immune Complexes ◽  
Serum Levels ◽  
Normal Serum

scholarly journals COMPLEMENT-DEPENDENT RELEASE OF IMMUNE COMPLEXES FROM THE LYMPHOCYTE MEMBRANE

1973 ◽  
Vol 138 (3) ◽  
pp. 495-507 ◽  
Author(s):  
Gary W. Miller ◽  
Paul H. Saluk ◽  
Victor Nussenzweig
Keyword(s):  
Cell Membrane ◽  
B Lymphocytes ◽  
Immune Complexes ◽  
Mammalian Species ◽  
Normal Serum ◽  
Soluble Antigen ◽  
Lymphocyte Membrane ◽  
Alternate Pathway ◽  
Extensive Degradation ◽  
Antigen Antibody

Soluble antigen-antibody-complement complexes bound to mouse B lymphocytes are rapidly released from the cell membrane in the presence of normal serum from several mammalian species. The release is not the result of antigen-antibody dissociation or extensive degradation of the complexes. However, the released complexes have been altered because they will no longer bind to fresh lymphocytes. The release is not the result of lymphocyte damage mediated by complement. It is complement-dependent, and is generated either preferentially or exclusively via the alternate pathway, since it occurs in C4-deficient serum, is Mg++ but not Ca++ dependent, and requires C3 proactivator. C3 inactivator is not involved. The release activity of the serum, once generated, is unstable at 37°C. The release of complexes from the lymphocyte membrane by serum provides a convenient assay for the functioning of the alternate pathway in the mouse and in other species.

scholarly journals CHARACTERISTICS OF A NON-COMPLEMENT-DEPENDENT C3-REACTIVE COMPLEX FORMED FROM FACTORS IN NEPHRITIC AND NORMAL SERUM

1970 ◽  
Vol 131 (6) ◽  
pp. 1306-1324 ◽  
Author(s):  
Enrique H. Vallota ◽  
Judith Forristal ◽  
Roger E. Spitzer ◽  
Neil C. Davis ◽  
Clark D. West
Keyword(s):  
Immune Complexes ◽  
Biological Significance ◽  
Normal Serum ◽  
Proliferative Glomerulonephritis ◽  
Temperature Sensitive ◽  
Cobra Venom Factor ◽  
Nephritic Factor ◽  
C3 Nephritic Factor ◽  
Optimum Ph ◽  
Reactive Complex

When serum from a patient with membrano-proliferative glomerulonephritis and normal serum are mixed at 37°C, C3 is rapidly broken down to two more rapidly migrating components. In the mixture, a heat-labile pseudoglobulin, designated as the C3 nephritic factor or C3NeF, reacts with a pseudogolbulin in the normal serum, designated as cofactor, to form a C3 inactivator. By analogy with the cobra venom factor, the C3 inactivator is most likely a complex of the nephritic factor and cofactor. The complex has been designated as the C3 lytic nephritic factor or C3LyNeF. The reaction which results in the Formation of C3LyNeF requires the presence of Mg++, is highly temperature sensitive but occurs very rapidly at 37°C. In 20 min at 37°C, C3LyNeF can break down over 80% of the C3 in a mixture of normal and nephritic serum. The two-step reaction which leads to C3 breakdown has an optimum pH ranging from 6.0 to 9.0. Experiments employing serum depleted of C4 and C2, as well as certain characteristics of the C3NeF system provide evidence that C3 breakdown with nephritic serum is not dependent on complement-inactivating immune complexes or on the action of convertase (C4, 2). Data relating rate of C3 breakdown to the concentrations of C3NeF, C3, and C3LyNeF in the reaction mixture are similar to those for the reaction of enzyme with substrate. The biological significance of C3LyNeF in the production of glomerular inflammation has not been established.

scholarly journals Reevaluation of fibronectin-collagen interactions in tissues: an immunocytochemical and immunochemical study.

1988 ◽  
Vol 36 (6) ◽  
pp. 639-648 ◽  
Author(s):  
A J Cidadão ◽  
S Thorsteinsdóttir ◽  
J F David-Ferreira
Keyword(s):  
Liquid Phase ◽  
Immune Complexes ◽  
Normal Serum ◽  
Dot Blot ◽  
Rat Uterus ◽  
Immunochemical Study ◽  
Liquid Phase Adsorption ◽  
Tail Tendon ◽  
Rat Tail

We studied the distribution of fibronectin (FN) in rat uterus, rat tail tendon, and rooster comb, using LM and EM immunocytochemistry. Special attention was paid to the interaction of FN with collagen (COL). Various labeling protocols and dot-blot experiments were performed to confirm the results. Under conditions of labeling specificity, FN distribution over native COL fibrils was usually sparse, especially when these were organized into thick bundles. No labeling was observed over section surfaces of COL fibrils when postembedding methods were used, which indicates that no FN is present within these fibrils. Under conditions in which exogenous FN could react with tissues, e.g., when preincubation with normal serum for background blocking was performed, artifactual staining appeared over COL. Such a reaction also occurred when anti-FN antiserum completely blocked by liquid-phase adsorption was used. Therefore, the FN present in soluble FN-anti-FN immune complexes must have still been able to react with COL. The artifactual labeling was, in all cases, almost exclusively localized on the section surfaces of COL fibrils. These results suggest that FN has a very low affinity for the surface of native COL fibrils.

A Sensitive On-Grid Immunoelectron Microscopic Procedure for Diagnosis of Rotavirus Infection

1980 ◽  
Vol 38 ◽  
pp. 506-507
Author(s):  
M. F. Miller ◽  
A. R. Rubenstein
Keyword(s):  
Electron Microscopy ◽  
Specific Antibody ◽  
Immune Complexes ◽  
Acute Gastroenteritis ◽  
Plant Viruses ◽  
Aggregation Process ◽  
Microscopic Technique ◽  
Fecal Material ◽  
Present Communication ◽  
Number Of Particles

Studies of rotavirus particles in humans, monkeys and various non-primates with acute gastroenteritis have involved detection of virus in fecal material by electron microscopy. The EM techniques most commonly employed have been the conventional negative staining (Fig. 1) and immune aggregation (Fig. 2) procedures. Both methods are somewhat insensitive and can most reliably be applied to samples containing large quantities of virus either naturaLly or as a result of concentration by ultracentrifugation. The formation of immune complexes by specific antibody in the immune aggregation procedures confirms the rotavirus diagnosis, but the number of particles per given microscope field is effectively reduced by the aggregation process. In the present communication, we describe use of an on-grid immunoelectron microscopic technique in which rotavirus particles are mounted onto microscope grids that were pre-coated with specific antibody. The technique is a modification of a method originalLy introduced by Derrick (1) for studies of plant viruses.

Localization of Immune Complexes in the Basement Membrane of the Ductuli Efferentes of the Rhesus Monkey

1980 ◽  
Vol 38 ◽  
pp. 456-457
Author(s):  
D. Marsh
Keyword(s):  
Basement Membrane ◽  
Fluorescence Microscopy ◽  
Rhesus Monkey ◽  
Immune Complex ◽  
Immune Complexes ◽  
Vas Deferens ◽  
Frozen Sections ◽  
Efferent Ducts ◽  
Complex Deposition ◽  
Sperm Antibodies

As a result of vasectomy, spermatozoa are confined to the epididymis and vas deferens, where they degenerate, releasing antigens that enter the circulation or are engulfed by macrophages. Multiple antigens of the sperm can elicit production of autoantibodies; circulating anti-sperm antibodies are found in a large percentage of vasectomized men, indicating the immunogenicity of the sperm. The increased prevalence of macrophages in the liomen of the rhesus monkey testicular efferent ducts after vasectomy led to further study of this region. Frozen sections were used for evaluation of immunopathological status by fluorescence microscopy with fluorescein-conjugated antibody. Subsequent granular deposits of immune complexes were revealed by positive immunofluorescence staining for complement. The immune complex deposition in the basement membrane surrounding the efferent ducts implies that this region is involved in antigen leakage (Fig. 1).

Antiheparin Activity of Human Serum and Platelet Factor 4

1973 ◽  
Vol 30 (01) ◽  
pp. 093-105 ◽  
Author(s):  
C.H.J Sear ◽  
L Poller ◽  
F.R.C Path
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Blood Serum ◽  
Whole Blood ◽  
Platelet Rich Plasma ◽  
Gel Filtration ◽  
Normal Serum ◽  
Platelet Factor ◽  
Mean Values ◽  
Antiheparin Activity

SummaryThe antiheparin activity of normal serum has been studied by comparing the antiheparin activities of sera obtained from normal whole blood, platelet-rich plasma and platelet-’free’ plasma with a purified platelet extract during differential isoelectric precipitation and by gel filtration chromatography.The mean values for the activity of PRP-serum and PFP-serum were 106% (S.D. 11) and 10% (S.D. 3) of untreated whole blood respectively. The activity of whole blood serum, PRP serum and whole blood serum plus platelet extract precipitated under identical physical conditions, i.e. pH 7.0, I =0.008, indicating that the activities of the three samples are probably associated with PF4. PF4 precipitated from human platelet extract at pH 4.0, but this is probably due to the difference in the two biochemical environments investigated, i.e. serum and platelet extract.The gel filtration experiments revealed striking similarities between the major antiheparin activities of serum and platelet extract. At physiological pH and ionic strength both activities were associated with high molecular weight material, but at physiological pH and elevated ionic strength both activities behaved as much smaller entities of molecular weight between 25,000 and 30,000 daltons and it seems very likely that both activities are associated with the same molecule, i.e. PF4.

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