J Lulé, G J Fournié, C Bousquet, J M Dueymes, J P Pourrat, J J Conté
{"title":"Quantification of large C3 fragments as an index of complement activation in mice. I. In vitro studies.","authors":"J Lulé, G J Fournié, C Bousquet, J M Dueymes, J P Pourrat, J J Conté","doi":"10.1159/000467821","DOIUrl":"https://doi.org/10.1159/000467821","url":null,"abstract":"<p><p>This paper describes a method which enables one to evaluate the mouse C3 activation. It is based on differences of solubility of native and activated C3 molecules in polyethylene glycol. The apparent molecular weights of C3 molecules detected were found to be about 230-240 kilodaltons for native C3 and 210 and 220 kilodaltons, respectively, for the two 'activated' C3 molecules. In vitro studies showed the specificity and the sensitivity of this evaluation.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 2","pages":"97-102"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467821","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600968","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":"Purification of functional subunits of the eighth component of human complement (C8) under nondenaturing conditions.","authors":"A G Rao, J M Sodetz","doi":"10.1159/000467835","DOIUrl":"https://doi.org/10.1159/000467835","url":null,"abstract":"<p><p>A simple procedure is described for purifying the noncovalently associated alpha-gamma and beta subunits of human C8 in the absence of denaturants and in yields significantly higher than previously obtainable. The procedure utilizes either conventional or high-pressure molecular sieve chromatography in the presence of 1.5 M NaCl. This ionic strength promotes dissociation of alpha-gamma from beta and facilitates their physical separation under mild conditions. Yields are typically 60-75% and, as judged by several criteria, each subunit is functionally identical to those isolated by earlier methods using sodium dodecyl sulfate. This new procedure eliminates the need for this detergent and thereby avoids the major solubility and yield problems encountered during its removal.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 4","pages":"182-6"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467835","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600971","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. Kaidoh, T. Fujita, Y. Takata, S. Natsuume‐Sakai, M. Takahashi
{"title":"Simplified method for purification of mouse beta 1H.","authors":"T. Kaidoh, T. Fujita, Y. Takata, S. Natsuume‐Sakai, M. Takahashi","doi":"10.1159/000467813","DOIUrl":"https://doi.org/10.1159/000467813","url":null,"abstract":"A simple three-step method was described for purification of murine beta 1H, one of the essential regulatory proteins of complement system. The method consists of heparin-Sepharose affinity chromatography; gel filtration on a Sepharose 6B column, and DNA-cellulose affinity chromatography. By this method over 10 mg of beta 1H can be purified by more than 200-fold from 100-ml of EDTA serum of various strains. Overall yield of beta 1H was about 45%. The purified beta 1H was homogeneous as judged by SDS-polyacrylamide gel electrophoresis and immunoelectrophoresis. The purified mouse beta 1H showed physicochemical properties very similar to those described for human beta 1H: mouse beta 1H is a beta-globulin consisting of a single polypeptide chain of molecular weight of 160,000. Purified mouse beta 1H retained its functional activity as the essential cofactor for the cleavage of fluid-phase human C3b by the human C3b inactivator. Immunization of rabbits with the purified mouse beta 1H resulted in the production of the potent and monospecific antibody.","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 1 1","pages":"44-51"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467813","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"65234339","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":"C4-binding protein in sera of patients with systemic lupus erythematosus and mixed essential cryoglobulinemia.","authors":"J A Schifferli, A Bakkaloglu, N Amos, D K Peters","doi":"10.1159/000467819","DOIUrl":"https://doi.org/10.1159/000467819","url":null,"abstract":"<p><p>C4-binding protein (C4BP) concentration was measured in sera of patients with systemic lupus erythematosus (SLE) (59) and mixed essential cryoglobulinemia (MEC) (6). The mean concentration of C4BP was not significantly different from the normal controls in both groups of patients; 1 patient with MEC and 11 patients with SLE had concentrations below the normal range. In addition there was no significant correlation between C4BP and C3, C4 or factor B concentrations in patients with SLE. These results suggest that C4BP is not consumed in these two diseases where strong activation of the classical pathway is known to occur in vivo. In addition, the significantly increased C4BP/C4 ratio, evident in both groups of patients, may provide a protective mechanism against C3 conversion by the classical pathway.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 2","pages":"81-6"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467819","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600966","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}
W Miyazaki, T Izawa, Y Nakano, M Shinohara, K Hing, T Kinoshita, K Inoue
{"title":"Effects of K-76 monocarboxylic acid, an anticomplementary agent, on various in vivo immunological reactions and on experimental glomerulonephritis.","authors":"W Miyazaki, T Izawa, Y Nakano, M Shinohara, K Hing, T Kinoshita, K Inoue","doi":"10.1159/000467829","DOIUrl":"https://doi.org/10.1159/000467829","url":null,"abstract":"<p><p>K-76 monocarboxylic acid (K-76 COOH) caused rapid reduction in hemolytic activities of complement and some of its components, especially C5, when injected into guinea pigs or rats. K-76 COOH suppressed Forssman shock in guinea pigs and mice and heterologous passive cutaneous anaphylaxis in guinea pigs. It also reduced the amount of protein excreted in the urine of rats with nephrotoxic nephritis and greatly prolonged the survival of (NZB X NZW) F1 female mice with a spontaneous systemic lupus erythematosus-like disease. The glomeruli of mice treated with K-76 COOH retained almost the normal histological appearance even at 1 year of age. K-76 COOH-treated mice became less sensitive to the infection of Escherichia coli, staphylococcus aureus, or Streptococcus pneumoniae, probably by enhancement of phagocytosis due to inhibition of factor I. K-76 COOH did not have any significant effect on a delayed-type contact skin reaction in mice, or on experimental allergic encephalitis in guinea pigs.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 3","pages":"134-46"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000467829","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17600969","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. Historical perspectives and some current issues.","authors":"M M Mayer","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 1","pages":"2-26"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17167133","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 Kaidoh, T Fujita, Y Takata, S Natsuume-Sakai, M Takahashi
{"title":"Simplified method for purification of mouse beta 1H.","authors":"T Kaidoh, T Fujita, Y Takata, S Natsuume-Sakai, M Takahashi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A simple three-step method was described for purification of murine beta 1H, one of the essential regulatory proteins of complement system. The method consists of heparin-Sepharose affinity chromatography; gel filtration on a Sepharose 6B column, and DNA-cellulose affinity chromatography. By this method over 10 mg of beta 1H can be purified by more than 200-fold from 100-ml of EDTA serum of various strains. Overall yield of beta 1H was about 45%. The purified beta 1H was homogeneous as judged by SDS-polyacrylamide gel electrophoresis and immunoelectrophoresis. The purified mouse beta 1H showed physicochemical properties very similar to those described for human beta 1H: mouse beta 1H is a beta-globulin consisting of a single polypeptide chain of molecular weight of 160,000. Purified mouse beta 1H retained its functional activity as the essential cofactor for the cleavage of fluid-phase human C3b by the human C3b inactivator. Immunization of rabbits with the purified mouse beta 1H resulted in the production of the potent and monospecific antibody.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 1","pages":"44-51"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17304857","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":"Monoclonal antibodies to human C4. I. Purification of hemolytically active C4 from small volumes of normal serum.","authors":"D G Spinella, D D Shah, P D Hale, R P Levine","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A C4-specific monoclonal antibody has been developed that allows the rapid purification of C4 from whole serum or plasma by affinity chromatography. 1- to 2-ml volumes of serum are loaded onto a small column of antibody-coupled agarose beads and washed through with buffer. C4 is eluted by adjusting the pH to 11.2. The purified C4 is free of extraneous proteins as detected by SDS-polyacrylamide gel electrophoresis and retains high activity as assessed by hemolytic assay and incorporation of [14C]-methylamine. Columns are reusable, and the entire procedure can be adapted for large-scale purifications.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 4","pages":"187-93"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17459586","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}
S L Newman, J E Devery-Pocius, G D Ross, P M Henson
{"title":"Phagocytosis by human monocyte-derived macrophages. Independent function of receptors for C3b (CR1) and iC3b (CR3).","authors":"S L Newman, J E Devery-Pocius, G D Ross, P M Henson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human monocytes and monocyte-derived macrophages were examined for their ability to bind and ingest C3-coated sheep erythrocytes (E). Greater than 90% of monocytes and macrophages formed rosettes with EC3b and EC3bi prepared with 15,000-20,000 molecules of C3 per E. Binding of EC3b to the monocyte or macrophage surface was inhibited by rabbit anti-C3b receptor (CR1), but was not inhibited by two different monoclonal anti-C3bi receptor (CR3) antibodies. EC3bi rosette formation was inhibited by monoclonal anti-CR3, but not by anti-CR1. Monocytes and macrophages did not form rosettes with similarly prepared EC3d,g or EC3d. Macrophages cultured for 7 days, but not freshly isolated monocytes, phagocytosed both EC3b and EC3bi. This ability was a consequence of macrophage maturation, as no external stimuli were present during in vitro culture. Experiments directed to determine if EC3b was converted to EC3bi before ingestion suggested that macrophage CR1 and CR3 mediated phagocytosis independently. No evidence was obtained that during the phagocytosis assay, macrophage factor I converted EC3b to EC3bi. The number of E bound or ingested by monocytes and macrophages was dependent on the number of molecules of C3b or iC3b bound per E. Monocytes and macrophages did not require the presence of either Ca++ or Mg++ for rosette formation with EC3b, whereas both divalent cations were required for optimum rosette formation with EC3bi. The presence of divalent cations was required for macrophage phagocytosis of EC3b and EC3bi. For ingestion of EC3b, Mg++ alone was sufficient, and the addition of Ca++ did not increase the number of EC3b ingested. For ingestion of EC3bi, both Ca++ and Mg++ were required for optimal phagocytosis, and their effect was concentration dependent and additive.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"1 4","pages":"213-27"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17304859","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}