{"title":"Depletion of complement by light and porphyrin does not depend on sequential activation.","authors":"N Bauman, B S Pease","doi":"10.1159/000467852","DOIUrl":"https://doi.org/10.1159/000467852","url":null,"abstract":"<p><p>The mechanism of complement depletion from human serum fortified with porphyrin and irradiated with light has been reinvestigated, with the conclusion that it did not depend on the normal sequence of complement activation. Thus, disappearance of the activities of C3, C4, and C5 was not dependent on divalent cations. Purified C3-C7 were labile to porphyrin/light treatment in the absence of other components. The depletion of C4 was not prevented by potent inhibitors of C1 and, unlike the depletion of C4 seen in response to aggregated gamma globulin, was insensitive to change in temperature. Electrophoresis showed an alteration of C3 unlike that caused by cobra venom factor and that light/porphyrin treatment nonspecifically altered many serum proteins.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"127-32"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467852","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15196447","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":"An improved method for preparation of C1-depleted serum and its application to hemolytic assay of C1.","authors":"Y Fukumoto, K Tsumoto, A Tashiro, N Ohtomo, T Yoshida","doi":"10.1159/000467854","DOIUrl":"https://doi.org/10.1159/000467854","url":null,"abstract":"<p><p>Serum depleted of the first component of complement (C1D) was prepared by treating fresh human serum with Sepharose-IgG in the presence of triethylenetetramine-N,N,N',N'',N''',N'''-hexa-acetic acid and di-isopropyl fluorophosphate at acidic pH (5.2). The total hemolytic activity of this C1D could be increased to approximately 75% of that of the original serum by the addition of excess purified C1. A linear relation was obtained on determination of C1 hemolytic activity using C1D, and the C1 titers of sera from patients measured by this simple method showed a good correlation with those measured using intermediate cells.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"140-6"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467854","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15196449","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":"XIth International Complement Workshop. November 3-5, 1985, Miami, Fla., USA. Abstracts.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 1","pages":"1-96"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15176054","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 J Boulanger, R P Smith, A L Baltch, F A Blumenstock, T M Saba
{"title":"Human plasma fibronectin effect on serum-mediated uptake of Pseudomonas aeruginosa PA 1348A by human granulocytes.","authors":"M J Boulanger, R P Smith, A L Baltch, F A Blumenstock, T M Saba","doi":"10.1159/000467866","DOIUrl":"https://doi.org/10.1159/000467866","url":null,"abstract":"<p><p>The effect of human plasma fibronectin on human granulocyte (PMN) phagocytosis of one strain of Pseudomonas aeruginosa (PA 1348A) was examined in a previously defined optimal phagocytic assay. Normal and fibronectin-deficient serum demonstrated similar rates of bacterial uptake by PMNs. Complement depletion of both sera inhibited phagocytosis. Addition of purified fibronectin did not alter phagocytosis. These findings strongly support the conclusion that fibronectin neither promotes nor inhibits opsonization for phagocytosis of this strain of P. aeruginosa.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"230-4"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467866","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15051774","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":"Immunoelectrophoretic analysis of C4 split products expressing D but not C epitopes: influence of storage, Ca2+ and Ca2+-chelating agents.","authors":"N E Petersen, J Folkersen, B Teisner, S E Svehag","doi":"10.1159/000467855","DOIUrl":"https://doi.org/10.1159/000467855","url":null,"abstract":"<p><p>Based on immunoelectrophoretic methods a heterogeneity in the electrophoretic mobility of C4d was observed. C4d was defined immunochemically as C4 molecules expressing D but lacking C epitopes. A beta-mobile form was observed when EDTA or heparin was not added to the sample prior to electrophoretic analysis. This component was generated during electrophoresis. Another C4d component migrating to the post-albumin region probably represented an in vivo generated split product. However, this C4d form was also produced during storage of serum or plasma at room temperature and its formation was enhanced in the presence of EDTA. Based on these findings standard conditions for collection and storage of clinical samples for quantification of C4d by electroimmunoassay are suggested.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"147-55"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467855","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13565370","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":"Inside-out vesicles prepared from complement lysed sheep red blood cells.","authors":"E W Rauterberg","doi":"10.1159/000467864","DOIUrl":"https://doi.org/10.1159/000467864","url":null,"abstract":"<p><p>Antibody sensitized sheep red blood cells were lysed to 68% by diluted human serum. The ghosts were shown to undergo vesiculation induced by low ionic strength buffer and gentle shearing forces like osmotically lysed ghosts. About 45% of the vesicles derived from complement lysed ghosts (as referred to vesicle protein) remained floating on top of a linear 3-18% dextran T110 gradient during ultracentrifugation. Using antibodies as probes for sideness about 90% of the floating vesicles displayed an inside-out orientation. Floating inside-out vesicles bear a slightly reduced but significant number of C9 molecules on their inverted extracellular side of the membrane as compared to the (leaky or collapsed) vesicles banding in the gradient. This finding suggests that the floating is not due to a lack of C5b-9 (under the assumption that all C9 was bound to C5b-9). It is concluded that lysis with diluted human serum may result partly in ineffective C5b-9 complexes and/or in lesions with limited permeability which do not impair vesicle floating on top of polymer gradients.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"211-8"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467864","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14946688","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":"Complement-mediated solubilization of immune complexes and their interaction with complement C3 receptors.","authors":"I Petersen, G Baatrup, H H Jepsen, S E Svehag","doi":"10.1159/000467850","DOIUrl":"https://doi.org/10.1159/000467850","url":null,"abstract":"<p><p>Some of the molecular events in the complement (C)-mediated solubilization of immune complexes (IC) have been clarified in recent years. The solubilization is primarily mediated by alternative C pathway proteins whereas factors in the classical pathway accelerate the process. Components of the membrane attack complex do not participate in the reaction. Besides affecting the size and solubility of circulating IC the interaction with C factors influences the reactivities of the complexes towards fluid phase reactants and mediates the reversible binding of IC to cellular C3 receptors. Our knowledge of the cellular localization, expression and structure of the C3 receptors, especially the C3b (CR1) receptor, has been considerably extended in the last few years, whereas our understanding of the physiological role of these receptors is still fragmentary. However, it is becoming increasingly evident that impaired solubilization of IC in patients with compromised C function may permit the complexes to deviate from their normal pattern of interaction with C3 receptors probably influencing both the organ distribution and clearance of IC and thereby also their phlogistic potentials.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"97-110"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467850","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14070406","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 F Schulz, A Helmberg, M Hosp, A Petzer, B Föger, M P Dierich
{"title":"Enzyme-linked immunoassay to monitor the purification of, and to screen for monoclonal antibodies against, C3b receptor.","authors":"T F Schulz, A Helmberg, M Hosp, A Petzer, B Föger, M P Dierich","doi":"10.1159/000467865","DOIUrl":"https://doi.org/10.1159/000467865","url":null,"abstract":"<p><p>An enzyme-linked immunosorbent assay both to screen for monoclonal anti-bodies to the C3b receptor and to monitor its purification was developed. The test requires only purified C3, converted to either the hemolytically no longer active iC3 or C3b. An NP-40 lysate of tonsil cells can be used as a source of CR1 in this test which works best under hypotonic conditions facilitating the interaction of iC3/C3b and CR1. Two monoclonal antibodies to CR1 were produced using this test for the screening of hybridomas. The identity of the molecule recognized by these antibodies with CR1 is demonstrated by immunoprecipitation and Western blot studies, as well as immunofluorescence and immunoperoxidase staining of cells and tissues known to contain CR1. Fractions from lentil-lectin and DEAE-Sephadex columns containing CR1 can be identified using this test.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"219-29"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467865","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14072453","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":"Conformational changes of complement components C3 and B induced at higher temperature.","authors":"A Takada, S Shirahama, Y Takada","doi":"10.1159/000467862","DOIUrl":"https://doi.org/10.1159/000467862","url":null,"abstract":"<p><p>When purified C3 or B of human complement was incubated at various temperatures for 30 min, B lost most of its antibody combining capability at 46 degrees C, and C3 lost it at higher than 50 degrees C. When C3, heated B, D and Mg++ ions were incubated, there was a precipitous decrease in C3 conversion in the presence of heated B between 44 and 46 degrees C. No C3 conversion was observed in the presence of B heated at 50 degrees C. When C3 heated higher than 50 degrees C was incubated with B, D and Mg++ ions, C3 conversion decreased dramatically, but B was converted almost normally, suggesting that B could be complexed with heated and conformationally altered C3 and cleaved by D. The fluorescence intensity of heated C3 excited at 288 nm gradually decreased between 44 and 46 degrees C. The fluorescence 288 nm gradually decreased between 44 and 46 degrees C. The fluorescence intensity of C3 was slightly increased by 1-anilino-8-naphthalene sulfonate (ANS) at 50 degrees C and significantly increased at 56 degrees C, while ANS enhancement of fluorescence of B began at 46 degrees C and was significant at 50 degrees C, indicating that the surface of B and C3 became hydrophobic between 44 and 46 degrees C, and 46 and 50 degrees C, respectively. These results suggest that conformations of C3 and B have low melting points at which they change confirmations drastically.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 4","pages":"193-203"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467862","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14969889","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":"Increased plasma levels of the terminal complement complex in patients with evidence of complement activation.","authors":"T E Mollnes, S S Frøland, M Harboe","doi":"10.1159/000467858","DOIUrl":"https://doi.org/10.1159/000467858","url":null,"abstract":"<p><p>The terminal C5b-9 complex of human complement has recently been described and quantified in normal human plasma by an enzyme-linked immunosorbent assay (ELISA). We collected EDTA plasma samples from 20 patients clinically suspected to have complement activation. The terminal complement complex (TCC) and C3d split products were measured. The TCC was increased in 8 patients, and 6 of these also had increased C3d values, whereas 4 patients had increased C3d and normal TCC values. Two different double-antibody assays were used to detect terminal pathway activation: the combination of anti-C6 and anti-C9 detecting only the whole complex, and the combination of anti-C6 and anti-C5 detecting intermediate complexes as well. There was a close correlation between the observations in these two assays, suggesting that in general the whole cascade including C9 is involved when the terminal pathway of complement is activated in vivo. Quantification of TCC in plasma is an important supplement to already established methods for the evaluation of complement activation in vivo.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"2 2-3","pages":"175-84"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467858","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14995524","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}