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At least 19 recordsLinked to original sources
PubMed1984

IUD-induced changes in cervical secretion content of albumin, IgG and complement C3c.

Cervical secretion albumin, IgG, complement C3c, spinnbarkeit and amount of wet weight mucus recovered were analyzed in a group of 13 women using IUD as a contraceptive method and the results were compared to those obtained in a control group. Significant differences were obtained when concentrations and amounts of soluble proteins in the respective groups were compared, but spinnbarkeit and amount of wet weight mucus recovered were not affected by the presence of the IUDs.

Adult↗
PubMed1983

Complement C3c and C3d in plasma and synovial fluid in rheumatoid arthritis.

By means of recently developed immunochemical assays increased levels of the complement C3c and C3d split products were found in synovial fluids of patients with rheumatoid arthritis (RA) as compared with synovial fluids of patients with traumatic synovitis (TS). In plasma, only the C3d levels were significantly increased compared with plasma levels of patients with TS. Both split products were higher in RA synovial fluids (SF) than in RA plasma. A positive correlation between the C3d concentrations in plasma and the presence of IC in serum was found, and between the C3c levels and the concentration of polymorphonuclear cells in SF of RA patients. Due to differences in turn-over of C3c and C3d determination of plasma C3d levels may be a useful parameter for the evaluation of immunological activity in RA, while measurement of C3c in the synovial fluid may elucidate the actual inflammatory activity in the synovial membranes.

Antigen-Antibody Complex↗
PubMed1986

Platelet-associated immunoglobulins IgG, IgM, IgA and complement C3c in chronic idiopathic autoimmune thrombocytopenia: relation to the sequestration pattern of 111indium labelled platelets.

Levels of platelet-associated immunoglobulins (PAIg) IgG, IgM, IgA and complement C3c were related to parameters of 111Indium-labelled platelet kinetics in 17 patients with chronic idiopathic autoimmune thrombocytopenia (cAITP). Elevated levels of PAIg/C3c were found in 14 patients (82%) (PAIgG n = 13, PAIgM n = 11, PAIgA n = 1, PAC3c n = 5). Only PAIgG correlated with platelet counts (RS = -0.71, p less than 0.01). Mean platelet life span (MLS) was shortened in all patients (median 12.0 h, range 0.3-45.6 h) and correlated with the platelet counts (RS = 0.49, p less than 0.05). MLS was correlated with PAIgG (RS = -0.52, p less than 0.05), but not with PAIgM, PAIgA, or PAC3c. The site of sequestration was splenic in 10 patients and splenic-hepatic in 7 patients. Although no significant correlation between either site of platelet sequestration and any of the investigated PAIg/C3c was demonstrable, platelets coated with higher PAIgG levels were more readily sequestrated in the spleen, while elevations of PAC3c were found in 4 out of 7 patients with hepatic involvement.

Adolescent↗
PubMedDate not supplied

Epitope specificities and quantitative and serologic aspects of monoclonal complement (C3c and C3d) antibodies.

Twenty-two monoclonal antibodies to human C3c and ten to C3d were obtained by hybridization after the immunization of mice with complement-coated human red cells and/or purified human complement components. C3c antibodies were variable in their agglutination reactions with cells coated with C3 by antibody in vitro; more consistent and potent reactions with these cells were observed with anti-C3d, and all anti-C3d reacted with red cells coated with C3 in vivo. Immunoradiometric assays were used to estimate antibody concentration, affinity, and epitope specificity. The antibody content in ascitic fluids varied from less than 0.1 mg per ml to 5.6 mg per ml. The estimated values of antibody affinities for Sepharose-coupled C3 ranged from 2.8 X 10(6) l per M to 5.0 X 10(8) l per M; on average, IgM antibodies had higher affinities than IgG antibodies. Competitive binding assays showed that the monoclonal antibodies recognized at least seven different epitopes, four on the C3c and three on the C3d fragment of C3. When the results of serologic and quantitative assays were compared, no convincing relationship was found between serologic performance and epitope specificity, antibody concentration, or affinity. IgM antibodies generally gave higher agglutination scores than IgG antibodies, and Ig class was the only useful predictor of serologic efficacy.

Animals↗
PubMed1983

A single step immunoelectrophoresis method for the quantitation of complement C3c in biological fluids.

An intermediate gel rocket immunoelectrophoresis (IRI) suitable for direct quantitation of complement split products with C3c specificity is described. The technique represents a simple, quick, and reproducible method for the assessment of complement activity in biological fluids in diseases. The advantages of the quantitative approach of the IRI method as compared to the conventional crossed immunoelectrophoresis (CIE) are the increased sensitivity, specificity, and precision of the method; also, the assay capacity is superior to CIE. The IRI-C3c assay is therefore highly suitable as a scientific tool, and may also be useful for routine laboratory investigations.

Complement Activation↗
PubMedDate not supplied

[Determination of the fraction of C3c complement by radial immunodiffusion in the serum and saliva from the parotid gland of clinically normal subjects].

It was our intention to determine the C3c fraction in the serum and in the parotid saliva of 13 clinically normal individuals by the radial immunodiffusion method. The mean value of the seric C3c was 86.92 mg/dl and the confidence levels averaged 75.53 to 100.31 mg/dl. There was no measurable concentration of C3c in the parotid saliva.

Adolescent↗
PubMed1987

Competitive enzyme-linked immunoassay for the quantitation of platelet-associated immunoglobulins (IgG, IgM, IgA) and complement (C3c, C3d) with polyclonal and monoclonal reagents.

A competitive enzyme-linked immunoassay (CELIA) was developed for the quantitation of platelet-associated immunoglobulins and complement proteins. The use of unlabeled polyclonal rabbit or monoclonal antibodies to human immunoglobulins and enzyme-labeled anti-mouse or anti--rabbit IgG (double-step technique) resulted in a higher sensitivity compared to the single-step technique using only enzyme-labeled anti-human immunoglobulin antibody preparations. Sensitivity and results obtained by both techniques were compared. The range of normal values for platelet-associated IgG, IgM, IgA, C3c and C3d was assessed upon a large number of normal blood donors. When platelet-associated IgG was concomitantly assayed with polyclonal and monoclonal anti-IgG by the double-step technique on platelets obtained from normal donors and thrombocytopenic patients, identical results were obtained with both reagents. Problems related to the quantitation of immunoglobulins on platelets with different assays and antibody preparations are discussed.

Antibodies, Monoclonal↗
PubMed1994

Changes in immunoglobulin, complement and acute phase protein levels in the depressed patients and normal controls.

Recently, several authors have reported that immunoglobulin IgM, complement C3c, complement C4, and positive acute phase proteins (e.g., haptoglobin, alpha 1-acid glycoprotein and alpha 1-antitrypsin) were significantly increased, while negative acute phase proteins (e.g., albumin and transferrin), were decreased in depressed patients. In the present study, the levels of the immunoglobulin IgM, complement C3c, C4, alpha 1-antitrypsin and haptoglobin were found to be significantly increased in 20 unipolar depressed patients compared to healthy controls. The concentrations of total protein and albumin were significantly reduced in these patients. The concentrations of alpha 1-protein, (which is related to alpha 1-antitrypsin), and alpha 2-protein (which related to haptoglobin), were also significantly elevated in unipolar depressed patients. The results suggest that unipolar depression is associated with an acute phase response, which is possibly caused by changes in cytokines and corticosteroid secretion in depressed patients.

Acute-Phase Proteins↗
PubMed1992

Inhibition of the classical activation pathway of complement-mediated lysis by monoclonal antibodies to complement components C3c and C3d.

Eight epitope-mapped monoclonal antibodies (MoAbs) to complement component C3d and five to complement component C3c were investigated to determine whether they could inhibit the classical activation pathway of complement-mediated lysis (CML) by using blood group AB red cells sensitized by A or B MoAbs. Three IgM C3d MoAbs and one IgG1 C3c MoAb were able to inhibit CML in a dose-dependent manner. In the presence of excess complement, no inhibition was observed. The greatest inhibition was observed with two high-affinity IgM antibodies that were specific for epitope 1 on the C3d component. Some inhibition was observed with a high-affinity IgM antibody specific for epitope 3 of the C3d component and also with a lower-affinity IgG antibody specific for epitope 1 of the C3c component. The results indicate that some complement MoAbs have the capacity to distinguish between conformationally and/or functionally different forms of red cell-bound C3.

Antibodies, Monoclonal↗
PubMed1982

[Determination of various fractions of complement (Cl, C3c, C3a, C4) in a population of healthy neonates].

The authors have studied plasma levels of various complement fractions (C1,C3c,C3att.,C4) in 127 newborns. Referring to gestation period the studied subjects were divided as follows: 25 newborns (less than 37 weeks), 78 newborns (37-41 weeks), 21 newborns (more then 41 weeks). The mean values of various fractions results higher in the newborns with higher gestation period. Considering the gestational ages, the mean values obtained for each complement fraction are not different from those considered "normals". The range of single value turned out very wide. This fact should lead to prudence in the diagnostic valuation.

Complement C1↗
PubMed1979

Serum complement and protein metabolism in chronic dialysis patients.

1. Patients receiving regular hemodialysis treatment who are permitted to select their own diets are in danger of a protein deficiency manifested by a significant reduction in serum transferrin and in complement C3c. 2. Correlation analysis within the dialysis group revealed no secure connexion between the complement C3c and total hemolytic activity respectively, and transferrin levels. 3. Analysis of diets showed that protein intake and the serum transferrin level correlate. No such correlation was found for the complement C3c or total hemolytic activity. 4. Low transferrin levels in the serum appear to result in more severe anemia among dialysis patients. 5. Knowledge of the serum transferrin level permits much more exact assessment of the protein metabolism in regular hemodialysis patients than knowledge of the total hemolytic activity or the level of the complement C3c.

Blood Proteins↗
PubMed1981

Cleavage of membrane bound C3bi, an intermediate of the third component of complement, to C3c and C3d-like fragments by crude leucocyte lysosomal lysates and purified leucocyte elastase.

Partial degradation of the biologically-active major fragment of the third complement component (C3b) to C3bi is catalysed by the endopeptidase C3b inactivator (I) and its co-factor, beta 1H globulin (H). Complete degradation to the fragments C3c and C3d requires an additional protease, which can be simulated in vitro by trypsin. This study was designed to identify the in vivo correlate of trypsin. Purified and 125I-labelled C3b bound to sheep erythrocytes was used as substrate. Release of label into the supernate served as an index of proteolysis. The chain structure of the peptides in the supernate or remaining bound to the erythrocytes was assessed by SDS polyacrylamide gel electrophoresis. Significant cleavage of cell-bound C3b was obtained by treatment with I, H and extracts from human peripheral blood leucocyte azurophil granules. Purified elastase also removed label in the presence of I and H. The peptide remaining on the cell had the characteristic 33K molecular weight of C3d. The activity of elastase in cleaving was blocked by alpha-1-anti-trypsin, the chloromethyl ketone, MeO-Suc-Ala-Pro-Val-Ch2Cl and by rabbit antibody to elastase. Thus, elastase purified from azurophil granules of human polymorphonuclear neutrophils (PMN) is a potent catalyst of the cleavage of C3bi to C3c- and C3d-like fragments and may contribute in vivo to the control of complement-mediated inflammation.

Animals↗
PubMed1985

Familial occurrence of complement dysfunction in Crohn's disease: correlation with intestinal symptoms and hypercatabolism of complement.

Complement was studied in Crohn's disease probands with early onset and in their first degree relatives. Controls included 24 healthy volunteers and 24 patients with ulcerative colitis or peptic ulcers. Subnormal generation of chemotactic activity by the alternative pathway was shown in eight of 21 probands and in six of 33 relatives, a frequency in both groups significantly different from controls (p less than 0.005), with a strong connection between findings in patients and relatives. As previously shown in patients with Crohn's disease, the subnormal generation was related to decreased utilisation of complement C3 in relatives. Raised levels of circulating complement C3c split products suggested complement involvement in Crohn's disease probands. In contrast, plasma C3c was normal in all relatives, and none of the six cases with complement dysfunction had gastrointestinal symptoms or a history of inflammatory bowel disease. Our data suggest, that complement abnormality seen in Crohn's disease patients does not simply reflect mucosal inflammation or hypercatabolism of complement.

Adolescent↗
PubMed1991

Failure to detect deposition of complement and immunoglobulin in allergen-induced late-phase skin reaction in atopic subjects.

There still remains some controversy regarding the possible role of immune complexes in the pathogenesis of the late-phase skin reaction (LPSR). To assess this, skin biopsies were obtained from LPSR induced in atopic human subjects 6, 24 and 48 h after allergen challenge. Cryostat sections were stained by direct immunofluorescence for the presence of fibrinogen, immunoglobulin classes IgM and IgG and for the complement components C1q and C3c. Complement components were observed in only two of the 29 biopsies studied. In both instances, only C3c was detected. One of these subjects also had unequivocal IgG staining at 6 h. IgM staining was detected in two out of 10 subjects at 6 h but no significant deposition of immunoglobulins could be found at 24 or 48 h. Fibrinogen deposition was observed in about half of the biopsies at each time-point. This study suggests that substantial complement and immunoglobulin deposition are not overt features of the allergen-induced LPSR, although the presence of small amounts of immune complexes, below the sensitivity of the method employed cannot be excluded. Fibrin deposition occurs in the LPSR but does not appear to be a prerequisite for LPSR development.

Allergens↗
PubMed1989

[Serum levels of acid alpha 1-glycoprotein, haptoglobin, C 3c component of the complement and immunoglobulins IgG, IgA and IgM in liver damage in patients with chronic renal failure treated by repeated hemodialysis].

Thirty-five patients with chronic renal failure treated with repeated haemodialyses were divided into 3 groups: without evidence of hepatocellular damage (n = 11), with HBs-negative hepatocellular damage (n = 13), with HBS-positive, HBe-positive hepatocellular damage (n = 10). The concentrations of acid alpha 1-glycoprotein, haptoglobin, C3c complement component, IgG, IgA, IgM were determined in the serum before haemodialysis. The serum concentration of acid alpha 1-glycoprotein was statistically significantly higher in the patients in comparison with the healthy subjects. The concentrations of haptoglobin and C3c complement component in the serum were not statistically significantly different form those in healthy controls. The serum levels of IgG, IgA and IgM in patients with hepatocellular damage HBs-positive and HBe-positive were statistically significantly higher in relation to healthy subjects, the serum IgG level in this group was statistically significantly higher than in the group without hepatocellular damage and the group with HBs-negative hepatocellular damage.

Adult↗
PubMed1987

Enrichment of subgingival microflora on human serum leading to accumulation of Bacteroides species, Peptostreptococci and Fusobacteria.

This study was undertaken to identify ecological factors that favour opportunistic pathogenic species in the subgingival microflora. In a first approach, human serum as a substitute for gingival exudate, was used for batch-wise enrichment of subgingival plaque. The microflora resulting after 5-6 enrichment steps consisted of black-pigmented and non-black-pigmented Bacteroides species, Peptostreptococcus micros and Fusobacterium nucleatum as the main organisms. It is noted that the same group of species was found to be enriched independent upon the origin of the subgingival plaque sample. It was suggested that these organisms are favoured by the increased flow of gingival exudate during inflammation. The consortium of organisms was capable of selective degradation of serum (glyco-)proteins. Four different types of degradation occurred. After a prolonged period of growth complete degradation of immunoglobulins, haptoglobin, transferrin and complement C3c was observed. Partial degradation of immunoglobulins, haptoglobin, transferrin, albumin, alpha 1-antitrypsin and complement C3c and C4 was generally observed after 48 h of growth. Besides, immunoglobulin protease activity yielding Fc and Fab fragments was found. The consortium was also capable of consuming carbohydrate side-chains as indicated by an altered electrophoretic mobility of the serum glycoproteins.

Bacteroides↗