PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Complement C4”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 811 records · Page 45Linked to original sources
PubMed1986

Evidence that a nicked C4b, C4b', is a functionally active C4b derivative.

Factor I-catalyzed C4b cleavage is a regulatory reaction for the classical pathway of the complement system. Although the reaction was shown to be a two-step reaction, production of a nicked form of C4b, C4b', as an intermediate cleavage product and subsequent splitting of C4b' into C4c and C4d, it is not known which of the two steps represents the inactivation of the C4b function in the assembly of C3 convertase, C4b,2a. We have purified C4b' and assessed the ability of C4b' to assemble C3 convertase with C2 by utilizing size exclusion high performance liquid chromatography. Evidence was obtained demonstrating that C4b' still retains the function of C4b to assemble C3 convertase. Thus, the substantial step for the inactivation of the C4b function appears to be the second cleavage reaction, that is, the cleavage of C4b' into C4c and C4d.

Catalysis↗
PubMed1988

Derivation of the sequence of the signal peptide in human C4b-binding protein and interspecies cross-hybridisation of the C4bp cDNA sequence.

A 5' cDNA clone coding for human C4b-binding protein (C4bp) was isolated, characterised and sequenced to complete the cDNA sequence coding for residues 1-32 thus confirming the protein sequence data of Chung et al. [(1985) Biochem. J. 230, 133-141]. The sequence extended to allow derivation of the putative leader peptide sequence which was 32 residues in length and showed a high of hydrophobicity typical of other documented leader sequences. Cross hybridisation was detected between the human C4bp cDNA probes and genomic DNA isolated from various species on Southern blots suggesting that genomic sequence homologous to that coding for C4bp has been conserved during evolution.

Amino Acid Sequence↗
PubMed1978

Complement receptors: specific detection by molecular complexes.

Immune complexes of BSA-anti BSA (IgG F(ab')2) will activate human complement by the alternate pathway. The C3 bound to these complexes binds to human peripheral blood mononuclear cells which bear complement receptors. This interaction is visualized by fluoresceinated antigen (BSA-FITC) or fluorescein conjugated antisera directed at the C3 component of complement. The assay appears to be more sensitive than the usual IgMEAC rosette technique and correlates well with the rosette method.

Animals↗
PubMed1979

C3b binding immune complexes and immunoconglutinins in human sera. Detection by enzyme-linked immunosorbent assay (ELISA).

An enzyme-linked immunosorbent assay (ELISA) designed to measure autoantibodies against C3b (immunoconglutinins: IK) also detects immune complexes (IC). Solid phase C3b, in addition to binding IK of IgG, IgM and IgA classes, bound aggregated human IgG, IgA and aggregated immunologically purified anti-tetanus toxid antibodies as well as model complexes of tetanus toxoid-human anti-toxoid. Significant C3b binding IgG, IgM and IgA activities were seen in the sera of 20 SLE patients but not in sera from healthy blood donors. Ultracentrifugation analysis of two SLE sera revealed C3b binding IgG and IgA activities in both light (7S) and heavy (greater than or equal to 11S) fractions. This indicates simultaneous presence of IK and IC in these sera. On the basis of the known relationship between IK and IC formation we suggest that the solid phase C3b ELISA may be of value in evaluating immune reactions in patients.

Antigen-Antibody Complex↗
PubMed1980

Analysis of the different types of leukocyte membrane complement receptors and their interaction with the complement system.

The specificity, distribution, and structure of 8 different types of leukocytes membrane complement (C) receptors (CR1, CR2, CR3, and receptors for C1q, beta 1H, C3e, C3a, and C5a) are discussed. Recent data are reviewed on the synthesis of C components by macrophages and B lymphocytes, and how these components may function in the activation of these two cell type by the C system. Commonly used C receptor assay procedures are evaluated in terms of both specificity and sensitivity. Specific assay procedures are recommended for measuring CR1 (C4b-C3b receptor), CR2 (C3d receptor), CR3 (C3bi receptor), and the beta 1H receptor. Assays include both rosette and fluorescence procedures for detection of C receptors on either mouse or human leukocytes. Primary systems have been selected for optimal sensitivity and specificity, and where possible, acceptable alternative systems that are less sensitive or specific are suggested for laboratories lacking facilities for C purification.

Animals↗
PubMed1981

Hemolysis by the complement of tanned erythrocytes coated with cobra venom factor: a sensitive method to detect the alternative complement pathway activity of serum.

Sheep (Esh), human (Ehu), rabbit (Erab) or guinea pig (Egp) erythrocytes were treated with tannic acid and coated with cobra venom factor (CoVF), which activates the alternative complement pathway (ACP). Tanned erythrocytes (TE) coated with CoVF (TECoVF) were efficiently hemolyzed by guinea pig serum l(GPS) and/or rabbit serum (RabS) in Mg2+-EGTA-GVB (gelatin veronal-buffered saline containing 2 mM MgCl2 and 10 mM ethyleneglycol-bis(beta-aminoethyl ether)N,N'-tetraacetate). The reactivity of TEsh-CoVF, TEhu-CoVF and TErab-CoVF to the ACP of guinea pig and/or rabbit increased with the increased amount of CoVF fixed on TE until it was sensitive enough to be hemolyzed by serum diluted over 80 times in Mg2+-EGTA-GVB. The hemolysis of TECoVF by GPS was confirmed to be the result of ACP activation by the findings that the reaction was inhibited in EDTA-GVB, heating of GPS at 50 degrees C diminished its hemolytic potency, and fractions of factor B and factor D were essential to the sensitization of TECoVF for hemolysis by GPS in EDTA-GVB. On the other hand, none of the TE coated with CoVF were hemolyzed by human serum (HuS) diluted over 1 : 40. Although the low efficiency of HuS in TE-CoVF hemolysis remains to be explained, TE-CoVF will be useful for the detection of ACP activity of guinea pig and rabbit sera.

Animals↗
PubMed1984

Regulatory proteins for the activated third and fourth components of complement (C3b and C4b) in mice. I. Isolation and characterization of factor H: the serum cofactor for the C3b/C4b inactivator (factor I).

Factor H, purified from mouse EDTA-plasma using a 4-step procedure, consists of a single polypeptide chain of Mr 150,000 on SDS-PAGE. Mouse H (Hmo) was required for the cleavage of fluid-phase mouse C3b by mouse I (Imo). The final product of degradation of fluid-phase mouse C3b was iC3b, consisting of fragments of the alpha'-chain (alpha'-70, alpha'-43) linked by disulfide bonds to an intact beta-chain. Imo alone was capable of cleavage of membrane-bound mouse C3b and of generating iC3b. The addition of Hmo nevertheless had an enhancing effect on Imo activity, but cleavage did not proceed beyond iC3b. These observations suggest that one important function of Hmo is to permit the inactivation of fluid-phase C3b, and to inhibit irreversibly its activity. The concentration of H in the plasma of male and female BALB/c mice was not significantly different. Among different inbred strains of mice, large differences were observed in the plasma levels of H, and plasma H levels were positively correlated with the plasma levels of C3. This observation, taken together with the well known role of H in the control of the activation of the alternative pathway, suggests that the turnover of C3 is controlled to some extent by H.

Animals↗
PubMed1986

New methods for the preparation of the cellular intermediate EAC14.

The cellular intermediate EAC14 was successfully prepared by incubating optimally sensitized sheep erythrocytes (EA) with normal serum diluted in complement diluent buffer containing suitable amounts of inhibitors of EAC142 formation from EAC14 and C2, namely polymyxin E and polymyxin B. EAC14 cells could also be prepared by incubating EA with normal serum diluted in Mg2+ free complement diluent buffer in the presence or absence of sucrose. The cellular intermediates prepared by these methods exhibited characteristic EAC142 formation and decay profiles and were found to be suitable for C2 estimations.

Animals↗
PubMed1991

A flow cytometric assay for measuring complement receptor 1 (CR1) and the complement fragments C3d and C4d on erythrocytes.

A flow cytometric assay (FCA) was developed to measure complement receptor 1 (CR1) and the complement fragments C3d and C4d on erythrocytes. It was possible to measure these parameters accurately with intra- and interassay coefficients of variation of 2.0% and 6.5% respectively. The method was able to discriminate between low and high levels of erythrocyte CR1, C3d and C4d. Comparison with a previously described RIA method gave excellent correlation coefficients with r2 values of 0.94, 0.93 and 0.91 for CR1, C3d and C4d respectively. The flow cytometric assay was used to measure CR1, C3d and C4d on the erythrocytes of 98 healthy individuals and the 95% upper limits for C3d and C4d were established. There was a wide distribution of CR1 levels amongst these individuals but their C3d and C4d levels were low and often not above background. The possible application of this method in clinical medicine is discussed.

Antigens, CD↗
PubMed1994

Rapid, activity-guided isolation of sex-limited protein (Slp) from mouse serum by fractionated precipitation and high-performance liquid chromatography.

We have recently demonstrated that sex-limited protein (Slp) plays a key role in an EDTA-resistant mouse complement activation pathway. A rapid procedure, utilizing classical chromatography methods on an FPLC system, was developed for the isolation of functionally active Slp. The method is based on the fractionated precipitation of serum by polyethylene glycol 6000, followed by heparin Sepharose Cl-6B affinity chromatography, Mono Q anion exchange and Superose 12 gel filtration. The isolation of Slp was monitored by a hemolytic assay. The procedure resulted in the purification of Slp, which by SDS-PAGE gave a single band of M(r) 2000,000 under non-reducing conditions, and under reducing conditions three bands corresponding to M(rs) of 105,000, 76,000 and 37,000.

Animals↗