PubMed HealthSearch

PubMed · 268620

Interaction between the third complement protein and cell surface macromolecules.

Abstract

The activated form of the third complement protein, C3b, forms a stable complex with components of plasma membranes and particulate entities such as zymosan. The complex resists the action of detergents and protein denaturants as well as extremes of temperature, salt concentration, and pH. It can, however, be broken by exposure to hydroxylamine or by ammonolysis followed by incubation with sodium dodecyl sulfate. Thus, the complex appears to result from a hydrophobic interaction as well as a bond susceptible to nucleophilic attack.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

S K Law, R P Levine. 1977. Interaction between the third complement protein and cell surface macromolecules.. https://doi.org/10.1073/pnas.74.7.2701

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Spontaneous thioester bond formation in alpha 2-macroglobulin, C3 and C4.

Purified alpha 2-macroglobulin and complement proteins C3 and C4 were treated with ammonia to break their intramolecular thioester bonds and reform the original free cysteinyl and glutamyl side chains. When this reaction was performed at low temperature a conformational intermediate was trapped which lacked a thioester, but which could refold to the native structure and spontaneously reform the thioester and full biological function. The findings suggest that these proteins may undergo spontaneous post-translational self-modification forming the thioesters without involvement of enzymes or high energy metabolites such as ATP.

Complement C3

Expression of complement components of the alternative pathway by glioma cell lines.

Glioma cell lines express proteins of the complement alternative pathway, namely C3, factor B, factor H, and factor I. Secretion of these proteins was shown by a sensitive and specific ELISA. C3 and factor H were rapidly secreted by glioma cell line CB193 and reached a concentration of 140 ng/ml/10(6) cells after 72 h of culture. Factor B and factor I were secreted at a lower rate and reached concentrations of 25 and 15 ng/ml/10(6) cells, respectively. Western blot and immunoprecipitation experiments showed that secreted proteins were identical to the corresponding plasma proteins. For factor H, besides the well known 150-kDa species, an additional polypeptide of 45 kDa with factor H immunoreactivity was observed. This species corresponded to the N-terminal truncated form found in plasma. In preliminary experiments, we observed control of these syntheses by cytokines. IL-1 beta significantly increased C3 secretion, with no effect on factor H. Secretion of factor H was enhanced by IFN-gamma. These results show that a glioma cell line could be a useful tool to study complement biosynthesis by glial cells in humans.

Complement C3