Complement (Basel, Switzerland)最新文献

{"title":"Inhibition of C1q functions by RHP, a protein elevated in sera from patients with rheumatoid arthritis.","authors":"C L Rosano,&nbsp;C B Braun,&nbsp;K E Hechemy,&nbsp;N Parhami,&nbsp;P S Satoh,&nbsp;C Hurwitz","doi":"10.1159/000463036","DOIUrl":"https://doi.org/10.1159/000463036","url":null,"abstract":"<p><p>We have previously shown that serum levels of C1q, unbound to C1r X C1s, are elevated in rheumatoid arthritis. We have also shown that RHP, a newly described serum protein which affects the C1q-anti C1q precipitin reaction, is also present at elevated levels in rheumatoid arthritis. We now show that RHP inhibits the hemolytic activity of C1q, disaggregates C1, and inhibits the ability of C1q bound to latex beads or to aggregated IgG to enhance the oxidative metabolism of neutrophils.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 2","pages":"57-64"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463036","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14387788","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":"Origin of the fourth component of complement related Chido and Rodgers blood group antigens.","authors":"J P Atkinson,&nbsp;A C Chan,&nbsp;D R Karp,&nbsp;C C Killion,&nbsp;R Brown,&nbsp;D Spinella,&nbsp;D C Shreffler,&nbsp;R P Levine","doi":"10.1159/000463037","DOIUrl":"https://doi.org/10.1159/000463037","url":null,"abstract":"<p><p>We have reviewed the relationship between C4 and its related blood group and discussed the mechanisms whereby a fragment of C4 could become attached to erythrocytes (E). We hypothesize that there is chronic fluid-phase activation of C4 by either C1 to form C4b or spontaneous cleavage of the thioester to form iC4. These activated molecules bind to E. Proteolytic degradation of the bound C4b or iC4 would leave a covalently attached fragment of C4 on E and thereby give rise to the Ch and Rg blood group antigens. This system is of further immunopathologic interest since this 'normal' activation or turnover of C4 is closely regulated. In patients deficient in regulatory proteins, this spontaneous or normal turnover of C4 and C3 may initiate a pathologic condition.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 2","pages":"65-76"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14101937","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":"Enhancing effect of autologous human erythrocytes on generation of C3 cleavage products beyond iC3b.","authors":"H H Jepsen,&nbsp;B Teisner,&nbsp;J Folkersen,&nbsp;S E Svehag","doi":"10.1159/000463046","DOIUrl":"https://doi.org/10.1159/000463046","url":null,"abstract":"<p><p>The in vitro formation of C3d and C3c in fresh normal human serum (NHS) after addition of five different activators of the complement (C) system was studied. Following C-activation in NHS (n = 53) by Sephadex G-200 beads, the conversion of C3 was found to proceed to iC3b with a variable but restricted generation of C3d. Similar results were obtained by use of heat-aggregated IgG, Escherichia coli, zymosan, and cobra venom factor. However, comparing the C3d concentration following activation in the presence and absence of autologous red blood cells (RBC) at 37 degrees C the generated C3d was found to be 2- to 3-fold higher in the presence of RBC after 30, 60, and 210 min. Preincubation of RBC with polyclonal anti-CR1 antibodies resulted in a dose-dependent reduction of the amount of C3d generated. C-activation induced by Sephadex G-200 beads, in the absence of RBC, generated iC3b without a significant production of C3d. After removal of the activator beads, addition of RBC resulted in a decrease of iC3b and a clear increase in the C3c and C3d concentration within 3 h. Western blotting analysis of the C3d produced in the presence of RBC showed that the molecular weight (36 kilodaltons) was similar to that of C3d formed in vivo.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 3","pages":"120-9"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463046","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14185163","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":"A second variant of properdin deficiency: the detection of properdin at low concentrations in affected males.","authors":"A G Sjöholm,&nbsp;C Söderström,&nbsp;L A Nilsson","doi":"10.1159/000463047","DOIUrl":"https://doi.org/10.1159/000463047","url":null,"abstract":"<p><p>A selective deficiency of properdin (P) was identified in a 58-year-old male and in his 29-year-old nephew, both of whom were clinically healthy. As determined by different immunochemical methods P at low concentrations (about 2 mg/l) was detectable in serum and plasma. Three female relatives, including the mother and daughter of one of the P-deficient males showed moderately low P concentrations. The findings clearly suggested that the deficiency was inherited as an X-linked trait. Three males belonging to another family with P deficiency also showed detectable P concentrations. By contrast, no P (less than 0.1 mg/l) was found in 8 males belonging to three other families. We suggest that there are two variants of X-linked P deficiency: P deficiency type 1, characterized by extremely low P concentrations (less than 0.1 mg/l); and P deficiency type 2 recognizable by P concentrations of about 2 mg/l. The P detected in P deficiency type 2 had subunits of normal molecular weight (52 kilodaltons), but eluted in a lower molecular weight range than did the P of normal serum, either on gel filtration (Ultrogel AcA 22) or on size exclusion chromatography (TSK-4000). The evidence suggested that the P concentration may be one determinant of P oligomer formation. P-deficient serum type 2 did not support fluid phase C3 cleavage in the presence of such alternative pathway activators as inulin and zymosan, nor did it support efficient lysis of guinea pig erythrocytes in agarose gel. By contrast, rabbit erythrocytes were efficiently lyzed, but at a slow rate. P-deficient serum type 1 did not support lysis of rabbit erythrocytes in the assay system used. The reaction was clearly promoted by very low concentrations of purified P. Partially purified P from a male with P deficiency type 2 was shown to be hemolytically active. Further evidence of P function in P deficiency type 2 was obtained by using IgG-presensitized serogroup W-135 meningococci in an alternative pathway-mediated serum bactericidal assay.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 3","pages":"130-40"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463047","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14271940","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":"Patients with CLL and hypocomplementaemia have an impaired serum bactericidal activity against the Salmonella minnesota Re mutant.","authors":"L Varga,&nbsp;F Clas,&nbsp;G Füst,&nbsp;K Pálóczi,&nbsp;G Szegedi,&nbsp;M Loos,&nbsp;S R Hollán","doi":"10.1159/000463030","DOIUrl":"https://doi.org/10.1159/000463030","url":null,"abstract":"<p><p>The bactericidal effect of 25 serum samples from 23 patients with chronic lymphocytic leukaemia (CLL) against the Salmonella minnesota S form and Re mutant has been studied. No killing of the S form was observed in any of the sera tested, whereas a normal bactericidal effect was found against the Re mutant (group 1) in 17/25 sera of CLL patients. By contrast, in 8 serum samples from 6 CLL patients no killing or a markedly delayed killing of the Re strain was observed (group 2). Significant differences in the complement levels were found between the sera of group 1 and group 2. In group 1 mostly normal or elevated complement levels were observed, while in group 2 levels of C4 and C2 were found to be strongly decreased. A significant correlation was found between the bactericidal effect on the one hand and the C4 and C2 levels on the other.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"40-5"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463030","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14465588","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":"2nd European Meeting on Complement in Human Disease. September 19-22, 1988, Bari, Italy. Abstracts.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 4","pages":"180-219"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14332350","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 activation during cardiopulmonary bypass in children.","authors":"S Meri,&nbsp;M Aronen,&nbsp;M Leijala","doi":"10.1159/000463031","DOIUrl":"https://doi.org/10.1159/000463031","url":null,"abstract":"<p><p>Complement activation was evaluated prospectively in serial serum and plasma samples from 30 children, who underwent cardiopulmonary bypass operations. Each patient showed a decrease in total hemolytic C levels and increase in C3 activation product (C3a desArg and C3bi/c) levels. In 11 of the 30 patients surgery was associated with a complication: death (2), respiratory failure (RF, 9), septicaemia (4), postpericardiotomy syndrome (PPS, 1) and pancreatitis (1). Patients suffering from RF were younger, underwent longer perfusions and had somewhat more extensive changes in the C system, although no direct correlation between high C3a desArg levels and RF existed. Instead, the increase in C3a desArg was in linear correlation with the perfusion time. Most complications during the latter postoperative period were associated with distinct episodes of lower grade C activation.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"46-54"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463031","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14098606","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":"Effects of anti-C4 antibody on complement production by splenic and peritoneal macrophages.","authors":"J N Goldman,&nbsp;K S O'Rourke,&nbsp;J D McMannis,&nbsp;M B Goldman","doi":"10.1159/000463027","DOIUrl":"https://doi.org/10.1159/000463027","url":null,"abstract":"<p><p>We have previously shown that administration of anti-C4 antibody to cells in culture can suppress the synthesis and secretion of C4. Lymphoid cells must be present along with the C4 secreting macrophages to achieve suppression of full magnitude and long duration. In this publication we have demonstrated that treatment of peritoneal macrophages with intact anti-C4 antibody results in reduction of intracellular and secreted C4. Intracellular levels of pro-C4 rapidly returned to normal after removal of the suppressing antibody and extracellular levels of C4 secreted into the media returned to normal within 24-48 h. This is in marked contrast to our previously published results with splenic fragments where intracellular pro-C4 remained markedly reduced long after removal of anti-C4. Using pulse-chase experiments we now demonstrate that, after recovery from suppression, intracellular pro-C4 levels remain low in splenic macrophages because nascent C4 is processed through the cell more rapidly. This results in a smaller intracellular pool of C4, even in the face of normal or high levels of C4 synthesis in the postsuppression phase. Finally, we demonstrate that suppression of full magnitude and duration could only be achieved with intact anti-C4 antibody. F(ab')2 fragments were not capable of inducing complete suppression.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"13-26"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463027","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14465586","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 C5a receptor antagonism by protamine and poly-L-Arg on human leukocytes.","authors":"U B Olsen,&nbsp;J Selmer,&nbsp;J U Kahl","doi":"10.1159/000463049","DOIUrl":"https://doi.org/10.1159/000463049","url":null,"abstract":"<p><p>It is shown that protamine selectively and dose-dependently inhibits complement C5a-induced leukocyte responses such as histamine release from basophils, chemiluminescence and beta-glucuronidase release from neutrophils. Protamine produces parallel rightward displacements of the C5a dose-response curves. The inhibitory capacity of the polypeptide is reversible and disappears following repeated washing of exposed cells. In neutrophils poly-L-Arg similarly and specifically antagonizes C5a-induced chemiluminescence and enzyme release. This polymer alone, however, degranulates basophils and neutrophils, leading to histamine and enzyme release, respectively. It is concluded that on human neutrophils the arginine-rich polycations protamine and poly-L-Arg exhibit a competitive C5a receptor antagonism. In addition, protamine inhibits the C5a receptors on basophils. It is hypothesized that molecular conformations of the arginine-rich polycations might bind reversibly to, and block negatively charged groups at the C5a-receptor sites.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 3","pages":"153-62"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463049","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14309960","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":"Acute phase reactants and complement activation in patients with acute myocardial infarction.","authors":"T E Mollnes,&nbsp;K E Tambs,&nbsp;Y Myreng,&nbsp;L F Engebretsen","doi":"10.1159/000463029","DOIUrl":"https://doi.org/10.1159/000463029","url":null,"abstract":"<p><p>The acute phase proteins, C-reactive protein (CRP), orosomucoid, alpha 1-antitrypsin and haptoglobin, the native complement components C3 and C4, activation products of C3, and the terminal SC5b-9 complement complex were quantified in samples obtained on admittance and on days 1, 2, 3 and 6 in 21 patients with non-complicated acute myocardial infarction (AMI) and in 22 controls. For all proteins peak and median concentrations were higher in the AMI group than in the controls, but the difference was significant only for CRP and orosomucoid. Median CRP concentration was 46 mg/l in the AMI group and 2.5 in the control group. The corresponding orosomucoid concentrations were 1.6 and 1.2 g/l. There was no correlation between the concentration of CRP in peripheral blood and the degree of complement activation. Furthermore, no correlation was observed between complement activation and the size of infarction. The present study cannot demonstrate that the increased concentrations of CRP and other acute phase reactants observed in patients with AMI, are associated with systemic fluid-phase complement activation. Furthermore, the complement activation previously shown locally in infarcted myocardium cannot be demonstrated systemically in non-complicated AMI.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"33-9"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463029","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13596250","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}