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PubMedDate not supplied

Clinical applications of complement measurements in rheumatic diseases.

There is now convincing evidence that the complement system is involved in the pathogenesis of at least some of the manifestations of human rheumatic diseases. Complement measurements in serum and/or pathologic fluids from patients with these disorders not only reflect this involvement but also may provide important clues regarding the activity and extent of the disease processes. Future studies should provide additional information concerning the usefulness of such measurements for predicting the outcome of specific therapeutic regimens, and perhaps also be the basis for the evolution of new and more rational forms of therapy.

Antigen-Antibody Reactions↗
PubMed1985

Interaction of Ross River virus with the complement system.

In the absence of virus-specific antibody, Ross River virus failed to activate either the classical or alternative complement pathways. Instead, it inhibited the cleavage of C3 via both pathways. The virus did not appear to act by disrupting C3bBb complexes or by preventing cleavage of factor B by factor D. Instead Ross River virus was found to interfere with the actual cleavage of C3 by activated factor B (C3bBb) of the alternative pathway and C4b2a of the classical pathway.

Alphavirus↗
PubMed1976

Complement and the clinician.

The estimation of complement in serum, and in other body fluids, particularly synovial fluid, now has an established place in the assessment, prognosis and response to treatment of those diseases associated with immunological phenomena. Some knowledge of the complement sequence itself, the patterns characteristic of various disease processes and the interacting factors which may affect the levels of the various components have been summarised. Disease states closely resembling lupus erythematosus have been associated with genetically determined deficiencies of classic pathway components and deficiencies of terminal sequence components may lead to severe recurrent infections.

Collagen Diseases↗
PubMed1997

Stability of C3 convertase in the rat classical complement pathway.

It has been reported that rat serum complement causes efficient hemolysis of antibody-sensitized sheep erythrocytes (EA) at 20 C but not at 37 C. In connection with this, we demonstrated that C3 convertase of rat complement was significantly unstable at 37 C using purified components of rat complement.

Animals↗
PubMed1993

C1 inhibitor functional deficiency in systemic lupus erythematosus (SLE).

C1 inhibitor (C1-inh) was assayed in eight SLE patients presenting with consistently low levels of intact C4. C1-inh antigenic levels were normal in all patients; however, the function of the C1-inh tested against C1s and C1r was variable and outside the normal functional range in seven of the eight patients. The molecular weight of patients' C1-inh protein was 105 kD, corresponding to the size of the intact molecule. The C1-inh gene was analysed in all patients. Restriction fragments generated with TaqI, PstI and HgiAI gave no indication of a major C1-inh gene rearrangement. Direct genomic sequencing of exon VIII revealed three polymorphic point mutations, but there were no changes from the normal gene in or around the reactive-centre residue of C1-inh. Furthermore, we found no evidence for a C1-inh autoantibody in patients which could affect normal C1-inh function in vitro. These results indicate that the etiology of C1-inh dysfunction in SLE is heterogeneous and distinct from that reported in either hereditary or acquired angioedema.

Base Sequence↗
PubMed1979

Genetic basis of acquired C4 deficiency.

A study of the family of a patient who had an SLE-like syndrome and an extremely low serum C4 revealed an inheritance of C4 types and HLA region markers which indicated that the patient had 60--70% of "normal" C4 level prior to the onset of disease. Thus the extremely low C4 level during her disease may result from a combination of genetically determined low normal C4 and increased consumption/hyposynthesis secondary to her SLE.

Adult↗
PubMed1989

An estimate on the frequency of duplicated haplotypes and silent alleles of human C4 protein polymorphism. I. Investigations in healthy Caucasoid families.

The frequency of duplicated and non-expressed C4 alleles was determined by segregation analysis in 31 German and five French families with altogether 274 individuals by submitting the complete data from C4 protein phenotyping, including C4 beta chains, and the other classical MHC markers to the family analysis programme (FAP). From 120 unrelated German haplotypes the following frequencies were derived for silent alleles: C4A*Q0 0.2000, C4B*Q0 0.2083, and for the total of homo- and heteroduplicated C4A resp. C4B alleles: C4"DA"* 0.1333, C4"DB"* 0.1000. The true occurrence of the duplicated C4A*2, "DB*21" haplotype, first observed in French families, was found to be 0.0250 in the German sample. While the frequency of duplicated C4 haplotypes confirms earlier estimates, the increase in the frequency of silent alleles corresponds to those assumed from investigations at the DNA level. The results demonstrate classical protein typing with inclusion of C4 beta chain types to be an indispensable and powerful tool for haplotype recognition; they support the hypothesis that deletion at one C4 locus is accompanied by duplication at the other in a majority of haplotypes.

Alleles↗
PubMed1990

A new duplication C4B*1,12 at the C4B locus associated with BF*S07 in a Tunisian population.

Twenty-five Tunisian families were analyzed for their complement alleles in order to detect duplications at the C4 loci. In this population, the most characteristic duplications are C4A2, B1.12 or C4A1, B1,12 always associated with BFS07 and C2C. This previously undescribed C4B1,12 duplication was found in seven families, five times in association with HLA-A2, B50.

Alleles↗