M Schapira, A de Agostini, J A Schifferli, R W Colman
{"title":"Biochemistry and pathophysiology of human C1 inhibitor: current issues.","authors":"M Schapira, A de Agostini, J A Schifferli, R W Colman","doi":"10.1159/000467851","DOIUrl":"https://doi.org/10.1159/000467851","url":null,"abstract":"","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"111-26"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467851","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15024471","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Kinetic study of rheumatoid factor influence on complement-mediated modulation of immune precipitation.","authors":"V D Miletić, B D Rodić","doi":"10.1159/000467863","DOIUrl":"https://doi.org/10.1159/000467863","url":null,"abstract":"<p><p>Human monoclonal IgM kappa rheumatoid factor PA (mRF) expressed various effects on complement-dependent modulation of ovalbumin/antiovalbumin lattice formation measured kinetically by laser light scattering (LLS): (1) in the absence of complement, mRF (44.2-177 U/ml) caused enhancement of LLS in a dose-dependent manner; (2) mRF partially prevented expression of complement-mediated inhibition of lattice formation and, at the same time, complement inhibits mRF-dependent LLS enhancement; (3) complement caused disruption of lattice-mRF bonds during solubilization of preformed lattice-mRF complex as demonstrated by specific mRF activity in supernatants. This effect is dependent on complement activity and on both complement and mRF concentrations; (4) ovalbumin/antiovalbumin complexes gradually lost the ability to react with mRF during the first 2 min of complement-mediated inhibition of lattice formation.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"204-10"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467863","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14946687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
T Seya, S Nagasawa, M Matsukura, H Hasegawa, J P Atkinson
{"title":"Generation of C3d,g and C3d by urokinase-treated plasma in association with fibrinolysis.","authors":"T Seya, S Nagasawa, M Matsukura, H Hasegawa, J P Atkinson","doi":"10.1159/000467857","DOIUrl":"https://doi.org/10.1159/000467857","url":null,"abstract":"<p><p>In the breakdown of fluid phase C3 in plasma, the process of conversion of iC3b to C3c and 'C3d' has not been elucidated. Using fluorescent labeled iC3b as a substrate, urokinase (UK) treated but not normal plasma was found to exhibit effective 'C3d' production. To address the relationship between the fibrinolytic activity specific for UK-activated plasma and this 'C3d' production, an assay system was developed that permitted the simultaneous determination of both activities. This method indicated that 'C3d' generation paralleled that of plasmin-dependent fibrinogen degradation. A Km of iC3b for plasmin was 3.0 X 10(-6) mol/l which is similar to the Km of fibrinogen. Plasmin cleavage of iC3b gave rise to C3d1 (Mr 42,000) and C3d2 (Mr 28,000). Purified plasmin C3d1 showed the same Mr and pI as C3d,g prepared from iC3b, by H and I. C3d2 was derived from C3d1. From these in vitro experiments with urokinase-treated plasma, we conclude that in parallel with fibrinolysis efficient cleavage of fluid phase iC3b to C3c + C3d,g and C3d occurs and we hypothesize that this is one mechanism for the generation of C3d in vivo.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"165-74"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467857","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14070405","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
B Uring-Lambert, S Gas, J Goetz, G Mauff, S F Goldmann, M Frössler, K Bender, G Hauptmann
{"title":"Detection of the genetic polymorphism of human C2 (native protein and C2a fragment) by immunoblotting after polyacrylamide gel isoelectric focusing.","authors":"B Uring-Lambert, S Gas, J Goetz, G Mauff, S F Goldmann, M Frössler, K Bender, G Hauptmann","doi":"10.1159/000467861","DOIUrl":"https://doi.org/10.1159/000467861","url":null,"abstract":"<p><p>The polymorphism of the second component of human complement (C2) was studied by means of isoelectric focusing in polyacrylamide gels followed by immunoblotting with a specific antihuman C2 antibody. The polymorphism was studied in native C2 and in the C2a fragment obtained by activation of the classical pathway with heat-aggregated human IgG. Serum samples previously typed with the hemolytic overlay technique were analyzed. They comprised samples of homozygous C2*C, C2*B, C2*Q0, heterozygous C2*BC and C2*CQ0 individuals. The patterns obtained by immunoblotting corresponded to those obtained by the hemolytic overlay technique. As expected, the homozygous C2*Q0 sample (complement C2 deficiency) did not show any band pattern. The C2a fragment presented also a polymorphic variation which correlated exactly with the native C2 polymorphism. It appears thus that the polymorphic site of the C2 protein is carried by the C2a fragment for the C2*C and C2*B variants. In addition, this method is easier to perform than the common hemolytic overlay technique and the rare C2-deficient serum is not needed.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"185-92"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467861","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15027930","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M Cicardi, D Frangi, L Bergamaschini, M Gardinali, G Sacchi, A Agostoni
{"title":"Acquired C1 inhibitor deficiency with angioedema symptoms in a patient infected with Echinococcus granulosus.","authors":"M Cicardi, D Frangi, L Bergamaschini, M Gardinali, G Sacchi, A Agostoni","doi":"10.1159/000467853","DOIUrl":"https://doi.org/10.1159/000467853","url":null,"abstract":"<p><p>A patient with echinococcosis, acquired deficiency of the inhibitor of the activated first component of complement and angioedema symptoms has been studied. These symptoms started 7 months after the surgical removal of an echinococcus liver cyst. Eight years later, when the complement was investigated, a marked deficiency of the C1 inhibitor, C1, C4 and CH50 was present. The patient was therefore successfully treated with tranexamic acid. After 4 years, the woman needed another operation because of a relapse of echinococcosis; afterwards she was symptom-free without medications, while the complement profile remained unchanged. Circulating immune complexes were detected by the conglutinin method. The patient's serum was demonstrated to possess an anticomplementary activity without affecting the C1 inhibitor when incubated with normal human serum at 37 degrees C. At present, 16 years after the onset of the symptoms, there are no signs of lymphoproliferative disease.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"133-9"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467853","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15196448","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Allotypes of properdin factor B(Bf) and lymphocytotoxic antibody production.","authors":"J A Davidson, P A Dyer","doi":"10.1159/000467814","DOIUrl":"https://doi.org/10.1159/000467814","url":null,"abstract":"<p><p>We have investigated the properdin factor B(Bf) polymorphism in relation to lymphocytotoxic antibody production. The Bf phenotypes of 1,113 individuals was determined; these consisted of 360 cytotoxic antibody-negative normal healthy controls, 293 HLA typing antisera, 330 sera from pregnant multiparous women, and 130 renal patients awaiting cadaveric transplantation. The allotype BfF was found to be strongly associated with cytotoxic antibody production in multiparous women.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 1","pages":"52-7"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467814","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17459583","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"LPS stimulation of complement (C3) synthesis by a human monocyte cell line.","authors":"W K Nichols","doi":"10.1159/000467823","DOIUrl":"https://doi.org/10.1159/000467823","url":null,"abstract":"<p><p>The human monocyte-like cell line, U937, was utilized as a model system to assess the influence of lipopolysaccharides (LPS) from Escherichia coli and other immunomodulatory agents on the biosynthesis of complement component C3 by monocytoid cells. The amount of C3 accumulated in the medium of cultured cells was measured by an enzyme-linked immunoabsorbent assay (ELISA). In the presence of LPS (0.01 and 0.10 microgram/ml) C3 production by U937 cells was increased by 2- and 5-fold, respectively. C3 production was also increased in the presence of lymphokine-containing supernatants obtained from human peripheral blood mononuclear cells after their stimulation with concanavalin A-sepharose. Human gamma-interferon (50-500 units/ml) stimulated C3 production by U937 cells. Stimulation of C3 production by LPS or mononuclear cell supernatants was blocked by cycloheximide. LPS (0.10 and 1.0 microgram/ml) also stimulated PGE2 production by U937 cells but failed to increase PGE2 at the lowest concentration (0.01 micrograms/ml) shown to increase C3 biosynthesis. Although exogenous PGE1 (10(-7) and 10(-6) M) promoted a small increase in C3 production, the effect of LPS was not decreased by a concentration of indomethacin (10(-6) M) that inhibited biosynthesis of PGE2. Therefore, LPS-induced C3 synthesis is not mediated by an increase in PGE2 in U937 cells. In summary, these observations suggest that C3 biosynthesis by monocytes/macrophages can be modulated by mediators of cellular immune responses found in the microenvironment of a localized inflammatory reaction.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 2","pages":"108-15"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467823","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17654737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Y Fukumoto, K Tsumoto, A Tashiro, N Ohtomo, T Yoshida
{"title":"Distributions and recoveries of complement components during cold ethanol fractionation of human plasma.","authors":"Y Fukumoto, K Tsumoto, A Tashiro, N Ohtomo, T Yoshida","doi":"10.1159/000467834","DOIUrl":"https://doi.org/10.1159/000467834","url":null,"abstract":"<p><p>The distributions and recoveries of the hemolytic activities and quantities of protein of complement components during cold ethanol fractionation were studied. Most of the components were recovered in Cohn's fraction III, with slight activities in fractions I and IV. The hemolytic activities of C1 and C5 were recovered in high yields in fraction III. The recoveries of activities of late components of complement (C6-C9) in fraction II + III were also high. These results suggest that many complement components can be isolated from Cohn's ethanol fractions.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 4","pages":"177-81"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467834","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Rapid, homogeneous phase, liposome-based assays for total complement activity.","authors":"G Akots, J C Braman, R J Broeze, D W Bowden","doi":"10.1159/000467828","DOIUrl":"https://doi.org/10.1159/000467828","url":null,"abstract":"<p><p>A simple, rapid assay for determining total complement activity has been developed. Complement activity is quantitated spectrophotometrically by measuring the amount of liposome-encapsulated enzyme unmasked by the action of anti-Dnp antibody and complement on Dnp-tagged liposomes. The assay is homogeneous in nature and is nonisotopic. The activity of complement in guinea pig serum has been measured and shown to be proportional to complement concentration. The assay was modified to measure the complement-fixing titer of anti-Dnp antibody preparations. We have compared two monoclonal anti-Dnp antibodies (IgG1 and IgM) for their ability to fix complement. The IgM antibody preparation was 450-fold more effective than the IgG1 preparation in mediating complement-dependent damage to Dnp liposomes. In addition, the test was modified to measure complement fixation by soluble antigen-antibody complexes. This complement fixation format is capable of detecting 2 pmol Dnp antigen.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 3","pages":"125-33"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467828","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17459585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Prelytic reduction of high-energy phosphates induced by antibody and complement in nucleated cells. 31P-NMR study.","authors":"R Tirosh, H Degani, G Berke","doi":"10.1159/000467839","DOIUrl":"https://doi.org/10.1159/000467839","url":null,"abstract":"<p><p>Using 31P-NMR spectroscopy, we have investigated possible involvement of metabolic processes in the lysis of nucleated cells induced by low levels of antibody to cell surface antigens and complement. Within 10 min of antibody plus complement attack, before onset of overt lysis, we have observed a marked, selective reduction in the intracellular content of phosphocreatine and adenosine triphosphate (ATP). A longer attack is accompanied by total depletion of either phosphocreatine or ATP in residual cells which preserved other phosphate compounds. The results indicate that in nucleated cells formation of putative complement-dependent membrane channels induces exhaustive hydrolysis of ATP. It is suggested that ATP deprivation could in turn lead to colloid-osmotic swelling, membrane rupture, and cell death.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 4","pages":"207-12"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467839","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}