J M Rasmussen, H V Marquart, R Rask, H H Jepsen, S E Svehag
{"title":"Quantification of C3dg/Epstein-Barr virus receptors on human B cells and B cell lines.","authors":"J M Rasmussen, H V Marquart, R Rask, H H Jepsen, S E Svehag","doi":"10.1159/000463040","DOIUrl":"https://doi.org/10.1159/000463040","url":null,"abstract":"<p><p>The expression of C3dg/Epstein-Barr virus receptors (CR2) on human peripheral blood and tonsillar B lymphocytes and Raji cells was quantified by measuring binding of unlabeled monoclonal anti-CR2 antibody (OKB7 and HB-5) in an indirect immunoenzymatic assay. Scatchard analysis of saturation binding curves revealed that Raji cells on the average express about 22,000 and 17,000 binding sites, with mean affinity constants of 9.9 X 10(10) and 8.7 X 10(10) M-1 for OKB7 and HB-5, respectively. Tonsillar mononuclear cells (TMC) expressed 16,700 and 17,600 binding sites for OKB7 and HB-5, respectively, with a significantly lower affinity constant for HB-5 (3.2 X 10(10) M-1) than for OKB7 (9.0 X 10(10) M-1). On the average 34% of E- peripheral blood mononuclear cells (PBMC) from healthy donors and 49% of TMC expressed the CR2 antigen. When correcting for the fraction of CR2-positive cells, the mean CR2 density was 12,600 on E- PBMC (n = 10) and 34,000 on TMC (n = 4).</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 2","pages":"98-107"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463040","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13974890","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-mediated inhibition of immune precipitation and differences in inhibitory action of genetic variants, C4A3 and C4B1.","authors":"L Paul, V M Skanes, J Mayden, R P Levine","doi":"10.1159/000463045","DOIUrl":"https://doi.org/10.1159/000463045","url":null,"abstract":"<p><p>The inhibition of immune precipitation is mediated by the classical complement pathway. We report here that the rate of precipitate formation depends on the genetic form of human C4 present during immune precipitation. C4A3 is more effective than C4B1 in its capacity to inhibit the rate of immune precipitate formation in serum and in serum-free reaction mixtures containing C1 and C4. Immune precipitates form within seconds after antigen is mixed with antibody, and the activation of the classical pathway is known to occur within seconds after C1 binds to antibody molecules. The covalent deposition of C4b on immune complexes is an essential step in the inhibition of immune precipitate formation, and if any of the reactions that lead to covalent C4b deposition become limiting, the rate of immune precipitation could exceed the complement system's inhibitory capacity. Hence, the inhibition of this rate may be an important function underlying the complement-mediated processing of immune complexes, and a decreased ability of the complement system to mediate this process in the presence of C4B1, in contrast to C4A3, could explain, at least in part, the association between the C4A-null phenotype and autoimmune diseases such as systemic lupus erythematosus.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 3","pages":"110-9"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463045","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14309957","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 prevents spontaneous cleavage of C3 in sera of patients with hereditary angioedema.","authors":"P Gronski, L Bodenbender, E J Kanzy, F R Seiler","doi":"10.1159/000463026","DOIUrl":"https://doi.org/10.1159/000463026","url":null,"abstract":"<p><p>We have studied the effects of polyclonal monospecific Fab' preparations against C1r, C1s, C1INH, C4, C4bp, and fragment Bb of factor B on complement activation in NHS and HAES. Furthermore, we have investigated complement activation in these sera after addition of purified C1s and purified C4bp. Blocking C1INH induced a spontaneous activation of the classical pathway in NHS and to a lesser extent in HAES. Addition of p-C1s resulted in a strong C3 conversion in NHS, but not in HAES. However, after the blocking of C4bp in HAES, addition of p-C1s produced a total C3 consumption. The ration of the protein concentration of C4bp to hemolytically active C4 was eight times higher in HAES than in NHS. This increased ratio may account for the resistance of HAES to the C1s induced C3 cleavage in our in vitro system and the stability of C3 in HAE despite C4 and C2 consumption in vivo.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463026","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14465585","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":"Structural basis of the binding specificity of the thioester-containing proteins, C4, C3 and alpha-2-macroglobulin.","authors":"A W Dodds, S K Law","doi":"10.1159/000463039","DOIUrl":"https://doi.org/10.1159/000463039","url":null,"abstract":"<p><p>We have previously noted a large difference in the specificity of the covalent binding reaction of human C4-A and C4-B. Here we report data on three other thioester-containing proteins. Human C3 is unreactive with glycine but its reactivity with glycerol (k'/ko = 23.0 M-1) is similar to that of human C4-B (k'/ko = 15.5 M-1). Human alpha 2-macroglobulin reacts with glycine (k'/ko = 206 M-1) in a manner similar to C4-B (k'/ko = 119 M-1) but its reactivity with glycerol (k'/ko = 1.2 M-1) is C4-A like (k'/ko = 1.3 M-1). Mouse C4 is C4-B like in its reaction with both glycine (k'/ko = 136 M-1) and glycerol (k'/ko = 26.0 M-1). Of these proteins, only C4-A shows a very high rate of reaction with glycine (k'/ko = 13,400 M-1). The comparison of the primary structures of these proteins has allowed us to propose the Leu Asp:Ile His substitutions at positions 1105 and 1106 in the human pro-C4 molecule as the residues largely responsible for the binding specificities of these proteins. The Leu:Ile change would not markedly affect the reactivity of these proteins, but may be necessary for allosteric reasons. The Asp in C4-A and His in C4-B seem likely to be the major specificity-defining residues.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 2","pages":"89-97"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463039","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13600079","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}
K J Micklem, G M Alder, C D Buckley, J Murphy, C A Pasternak
{"title":"Protection against complement-mediated cell damage by Ca2+ and Zn2+.","authors":"K J Micklem, G M Alder, C D Buckley, J Murphy, C A Pasternak","doi":"10.1159/000463048","DOIUrl":"https://doi.org/10.1159/000463048","url":null,"abstract":"<p><p>Ca2+ and Zn2+ prevent antibody-dependent complement-induced permeability changes in tonsil lymphocytes and Lettre cells. Lactate dehydrogenase leaks out from Lettre cells at high complement:cell ratios, under which conditions higher concentrations of Ca2+ and Zn2+ are required for protection. Ca2+ and Zn2+ do not inhibit complement activation or C9 binding to Lettre cells, and prevent leakage through preformed lesions. It is concluded that the extent of complement-induced membrane damage depends on the concentration of extracellular Ca2+, and may be modulated by changes in extracellular Ca2+ or Zn2+.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 3","pages":"141-52"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463048","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14309958","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":"Molecular basis for the microheterogeneity of human complement factor B.","authors":"G Garnier, C Davrinche, R Charlionet, M Fontaine","doi":"10.1159/000463038","DOIUrl":"https://doi.org/10.1159/000463038","url":null,"abstract":"<p><p>The involvement of sialic acids in the microheterogeneity of human complement factor B was investigated. Desialylation kinetics revealed all the charge intermediates from a complex native to a homogeneous form. The relation between this heterogeneity and posttranslational events was explored in cultured hepatoma cells. Intracellular factor B exhibited the same isoelectric focusing pattern as the desialylated purified protein, whereas a highly heterogeneous form was secreted. In contrast, when N-glycosylation was prevented by tunicamycin, both intracellular and secreted forms focused like intracellular factor B from control cultures. These data lead to the conclusion that the microheterogeneity of human factor B results from different degrees of sialylation of its N-glycans.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 2","pages":"77-88"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463038","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13974308","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":"Interaction between C3 nephritic factor and erythrocyte membranes. Presence of nephritic factor in patients' erythrocytes.","authors":"M López-Trascasa, M A Marín, G Fontán","doi":"10.1159/000463053","DOIUrl":"https://doi.org/10.1159/000463053","url":null,"abstract":"<p><p>The presence of IgG has been observed by fluorescence microscopy in the erythrocytes of 5 patients with NEF antibody. IgG subclass distribution of the IgG bound was analyzed by fluorescence-activated cell sorter. NEF activity was also determined in the eluted antibodies from the erythrocyte membrane. Three of five patients had NEF antibody bound to the erythrocyte membrane. IgG subclass distribution of NEF antibody sera was also investigated by means of protein A-Sepharose and using monoclonal antibodies against human IgG subclasses. NEF activity was mediated by IgG3 alone in 3 patients and by a combination of IgG1 and IgG3 in 2 patients.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 4","pages":"165-73"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463053","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14332349","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":"10.1159/000463055","DOIUrl":"https://doi.org/10.1159/000463055","url":null,"abstract":"","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"45 1","pages":"180-219"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463055","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"65223424","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":"Role of EAC1q4 in C1a transfer reaction (C1aTR) and further information on the nature of the EAC1q4 site.","authors":"F Xu, R Z Fei, G Y Ding, Z D Wang, F X Shen","doi":"10.1159/000463054","DOIUrl":"https://doi.org/10.1159/000463054","url":null,"abstract":"<p><p>The complement intermediates EAC1, EAC4, and EAC1q4 were prepared with guinea pig, porcine, as well as human complement. EAC4 and EAC1q4 were made from EC4 and EAC14 respectively. The C1a transfer reaction (C1aTR), the second step of Borsos' C1a fixation and transfer test, was carried out with various combinations of these intermediates. It was found that the EAC1q4, instead of the EAC4, was the C1a acceptor, and the C1rs subcomponents rather than the whole C1 molecule should have to transfer in the C1aTR. The EAC41 derived from EC4 generated no EAC1q4 in EDTA medium as the EAC14 did. This presented evidence for the joining of C4 to A in the EAC1q4 site.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 4","pages":"174-9"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463054","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13985888","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}
R A Harrison, T C Farries, F D Northrop, P J Lachmann, A E Davis
{"title":"Structure of C3f, a small peptide specifically released during inactivation of the third component of complement.","authors":"R A Harrison, T C Farries, F D Northrop, P J Lachmann, A E Davis","doi":"10.1159/000463028","DOIUrl":"https://doi.org/10.1159/000463028","url":null,"abstract":"<p><p>C3f, a peptide presumed to be generated by the combined actions of factors I and H on fluid-phase C3b, has been isolated and sequenced. The peptide is 17 residues long and has a molecular weight of 1,847 daltons. The amino-terminal sequence is, with the exception of a single residue, identical to that deduced for the 46-kilodalton polypeptide seen transiently in the generation of iC3b from C3b, and is in full agreement with the sequence deduced from cDNA analysis. In addition, high-pressure liquid chromatography of the digestion of C3b by factor I has shown that C3f is the sole peptide released during iC3b generation.</p>","PeriodicalId":77697,"journal":{"name":"Complement (Basel, Switzerland)","volume":"5 1","pages":"27-32"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000463028","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14465587","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}