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Biomedical subjects

M G Colomb

Publications and source records attributed to M G Colomb.

At least 91 records · Page 5Linked to original sources
PubMed1980

[The complement system and its biological activities].

The complement system is a non specific humoral defence mechanism which can be triggered by various effectors : immune-complexes, extrinsic proteases, bacterial cell-wall polysaccharides, viral membranes. Different peptides or multimolecular complexes are formed by a cascade of proteolytic cleavages; they take an active part in the inflammatory response and may contribute to different pathological manifestations.

Adhesiveness↗
PubMed1979

C1 inhibitor-dependent dissociation of human complement component C1 bound to immune complexes.

The interaction of C1 inhibitor with complement component C1 bound to immune complexes was examined by using 125I-labelled C1 subcomponents. The inhibitor binds rapidly to subcomponent C1s, and more slowly to subcomponent C1r. Formation of the C1r-C1 inhibitor complex causes rapid dissociation of subcomponents C1r and C1s from the antibody-antigen-component C1 aggregate. The rate and extent of this release are proportional to C1 Inhibitor concentration and are also dependent on ionic strength. Results obtained with purified C1 Inhibitor, plasma or serum as source of C1 Inhibitor are all closely comparable. Only slight dissociation of subcomponent C1q is observed under the same range of conditions. The implications of the release phenomenon are discussed in relation to the structure of component C1 and the possibility of differential turnover of C1 subcomponents.

Antibody Affinity↗
PubMed1979

Interaction of C1-inhibitor with the C1r and C1s subcomponents in human C1.

1. Insoluble IgG-ovalbumin aggregates were used to bind and activate C1 from human serum. The bound C1 provided a useful reagent for studying the interaction of C1 subcomponents with C1-inhibitor. 2. C1-inhibitor bound to both subcomponents (C1r and C1s in C1 and formed stable complexes of respective apparent molecular weights 197,000 and 185,000, as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The binding reaction proceeded more readily with C1s than with C1r and was correlated with the inhibition of C1s esterase activity. 3. At physiological ionic strength, binding of C1-inhibitor to subcomponents C1r and C1s caused release of these subcomponents from the C1-immune aggregates complex, indicating that C1-inhibitor binding decreased the inter-subcomponent binding forces in C1. At low ionic strength, however, this release did not occur.

Complement C1↗
PubMed1977

Purification of proenzymic and activated human C1s free ofC1r. Effect of calcium and ionic strength on activated C1s.

1. A rapid method for the purification of the proenzymic and activated forms of C1s is presented. In the case of proenzymic C1s, di-isopropyl phosphorofluoridate (0.5--5 mM) is added at all stages of the purification procedure, which includes euglobulin precipation followed by DEAE-cellulose chromatography and affinity chromatography on anti-C1r IgG-Sepharose 6B. The final step completely removes contaminant traces of C1r and/or C1r, ensuring that the final preparation of C1s is stable in the proenzyme form and suitable for activation studies. 2. The apparent molecular weight of C1s and C1s determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis is 85 000 +/- 2000. Reduction followed by alkylation of C1s gives two fragments of apparent molecular weights 57 000 and 28 000. Results of N-terminal amino acid determination and labelling with di-iso[3H]propyl phosphorofluoridate are consistent with previous reports. 3. The influence of calcium and ionic strength on the structure and activity of C1s has been investigated. Calcium leads to a shift of the sedimentation coefficient from 4.3 to 5.6 S, whereas variation in ionic strength has no effect on this parameter. The thermal inactivation curve is profoundly modified both by calcium and ionic strength. In contrast, the esterase activity is only slightly influenced as judged from the absence of gross modification of Km and V.

Calcium↗
PubMed1977

Proenzymic C1s associated with catalytic amounts of C1r. Study of the activation process.

1. Proenzymic C1s isolated from human plasma by euglobulin precipitation and DEAE-cellulose chromatography is associated with trace amounts of C1r (0.5--1% on a molar basis). Incubation for 2 h at 37 degrees C leads to the proteolytic activation of C1s. The proteolysis is characterized by the sigmoidal appearance of C1s esterase activity and of the typical heavy (57 000-dalton) and light (28 000-dalton) fragments of C1s on sodium dodecyl sulphate-polyacrylamide gel electrophoresis. 2. The C1s activation process observed is markedly temperature and concentration dependent, and the rate of activation is decreased by calcium and high ionic strength (I = 0.9). Diisopropyl phosphorofluoridate, benzamidine, polyanethol sulfonate and pentosane polysulphate inhibit the activation, which is also sensitive to C1-inactivator and anti-C1r IgC. From the kinetic experiments and from the inhibition characteristics, the activation of C1s can be attributed to the presence of C1r, which appears to undergo activation and then to activate secondarily C1s.

Calcium↗