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PubMed1979

Interactions of complement with the red-cell membrane.

Interactions of the complement components with the red-cell membrane are, as delineated, many and complex. Much is known about the nature of the complement components that take part in these interactions, but relatively little is known about the membrane or the components of the membrane with which they interact. Such understanding will be essential if we are to be able to explain the great resistance to complement lysis shown by normal red cells or the abnormalities that result in increased or decreased interacition of complement with abnormal red cells.

Antibodies↗
PubMed1977

The activation of the C3b feedback cycle with human complement components. I. Through the classical pathway.

Reaction between the fourth, the oxidized second and the activated first components of human complement generated the stable enzyme C4oxy2 capable of cleaving the third component and depleting total complement in human serum. This enzyme was shown further to activate the C3b feedback cycle as shown by its ability to consume factor B in serum and the reduction in the extent of complement consumption in the presence of EDTA. OxyC2 on its own gave rise to C3 cleavage in normal human serum by a pathway needing classical pathway components. This unexpected finding suggests that there may be a 'C-1 tickover' in serum analogous to the 'C3b tickover'; the presence of oxyC2 allowing the 'capture' of the trivial amounts of C42 normally formed. In preliminary experiments in the rat, C4oxy2 was successfully formed in vivo, where it gave rise to cleavage of C3, consumption of C5, depletion of cobra venom factor cofactors and a biphasic change in the neutrophil count.

Animals↗
PubMed1978

Testing of hemolytic complement components in domestic animals.

Total complement (C) and its components were assayed in the serum of 8 species of domestic animals, using commercially prepared cellular intermediates of sheep erythrocytes and functionally pure guinea pig and human components of the C system. Testing was done according to methods recommended by the producer for testing human C components. The late-acting components (C6 throug C9) and C1 were detected in carnivorous (dog and cat) and omnivorous (swine) animals. Undetectable or low titers of C4, C2, C3, and C5 were present in large herbivorous animals (cattle, horse, sheep, and goat), indicating major differences in comparison with human or guinea pig components of C. Porcine serum contained an inhibiting substance which interfered with testing C2 and later-acting components at serum dilutions up to 1:100. All components except C2 were detected in chicken serum. The binding or activation (or both) of C4, C2, C3, and C5 is more species specific than is the binding or activation (or both) of other components. Requirements for species specificity between antibody and C1 were not detected. Presence of C1 inactivator was detected in bovine, caprine, equine, and ovine sera. The CH50 (50% hemolysis) titers of C components tested in pooled serum samples from the 8 species of clinically healthy domestic animals are presented.

Animals↗
PubMed1978

The structural events associated with the attachment of complement components to cell membranes in reactive lysis.

Electron microscopic study of the events occurring at the cell membrane during reactive lysis by complement, showed that a foliaceous particle was formed at the C5b-7 stage, that enlarged to a particle with a variable number of arms at the C5b-8 stage. Up to this point, no typical complement lesions were found. At the C5b-9 stages, the particles were completely converted to typical complement lesions, i.e. hollow cylinders projecting from the cell membrane and partly penetrating it. C5b-9 complexes assembled in the fluid phase did not show the typical structure of the lesions, but were amorphous masses of fibres.

Complement C5↗