PubMed · 7555791
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
S Meri. 1994. [Complement deficiencies].. https://pubmed.ncbi.nlm.nih.gov/7555791/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
The complement C1-esterases have been shown to cleave the MHC class I molecules, which are important participants in the activation of T lymphocytes, between the alpha 2- and the alpha 3-domain of the heavy chain. The possible involvement of the C1-esterases in the regulation of peripheral self-tolerance is discussed. It is hypothesized that the C1-esterase-mediated cleavage of the MHC class I molecules either induces: a soluble fragment of the outer two domains of the MHC class I molecule, in association with beta 2-microglobulin, to bind to the T cell receptors and prevent the cells from being activated, or produces a change in the exposure of the alpha 3-domain that remain on the cell surface, acting as mediator of a 'veto signal' that prevents these cells from being activated.
Explore the source record for details and available documents.
The effects of the gold salt sodium aurothiomalate and of d-penicillamine on complement were studied in vitro. Total haemolytic complement was inhibited by 0.05-1mM gold. The inhibitory potency of gold was inversely correlated to the concentration of complement in the system, but was not diminished by albumin or decomplemented serum protein in concentrations approaching those circulating in blood. Penicillamine which itself slightly inhibited complement, prevented or reversed the action of gold. Conversion of C1s to C1esterase was not inhibited. Gold inhibited the action of C1esterase on component C4, but not the action on small-molecular synthetic ester substrates. Only very high gold concentrations (375-560 microM) inhibited the conversion of C3 to C3b. No inhibition of the alternative pathway was detected.