Role of C4-Binding Protein in the Defective Lysis of Sensitized Sheep Erythrocytes by Mouse Complement

Amerongen, A. van; Dijk, Hans van; Willers, J. M. N.

doi:10.1159/000233099

Cited by 5 publications

(1 citation statement)

References 15 publications

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“…Although it is known that sialic acid acts as a receptor site for factor H [28,291, to our knowledge no information is available in this respect for C4bp. Indirect evidence has been presented against a role for sialic acid in the binding of mouse C4bp [30]. However, in a preliminary study we observed that the neuraminidase treatment of IgE (DES) enhanced the formation of the classical pathway C3 convertase.…”

Section: Discussionmentioning

confidence: 91%

Mechanism of activation of the classical pathway of complement by monoclonal IgE (DES). Restricted regulation of C4b by C4b‐binding protein

Saint-Remy¹

1984

Eur J Immunol

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A human monoclonal IgE from patient DES, IgE (DES), has been shown to activate the classical pathway of complement. The mechanism of this activation has been investigated and can be summarized as follows: (a) IgE (DES) is able to bind and activate C1 in a dose-dependent fashion. This activation increases with the size of the aggregates used, but the affinity of C1 for IgE (DES) is weaker than for IgG. (b) A classical pathway C3 convertase can be assembled on IgE (DES) using purified C1, C4 and C2. The formation decay of this convertase is similar to that formed on IgG with an half-life of 9 min at 37 degrees C. (c) The extrinsic regulation of the C3 convertase by C4bp is restricted on IgE (DES) as compared to IgG. This restriction is shown on both the formation and the decay of the convertase. The mechanism of activation of the classical pathway of complement by IgE (DES) thus present some similarities with the assembly of the C3 convertase by the alternative pathway.

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Section: Discussionmentioning

confidence: 91%

Mechanism of activation of the classical pathway of complement by monoclonal IgE (DES). Restricted regulation of C4b by C4b‐binding protein

Saint-Remy¹

1984

Eur J Immunol

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Complement and Complement Reactions

Berger¹,

Hammer²,

Cole³

et al. 1988

The Complement System

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Study of the optimal reaction conditions for assay of the mouse alternative complement pathway

Dijk

Rademaker

Klerx

et al. 1985

Journal of Immunological Methods

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The optimal reaction conditions for hemolytic assay of alternative complement pathway activity in mouse serum were investigated. A microtiter system was used, in which a number of 7.5 x 106 rabbit erythrocytes per test well appeared to be optimal. Rabbit erythrocytes were superior as target cells over erythrocytes from a number of other animal species. The optimal conditions were as follows: an incubation temperature of 39°C, an ionic strength of about 200 mM, and a magnesium concentration of 2.5 mM. Incubation during 60 rain was not sufficient for an end-point titration. Addition of 1 mg of zymosan A per test well, however, enhanced and accelerated the hemolytic activity of mouse serum via the alternative pathway resulting in a maximum value after 45 min. This, most probably, proceeded by a mechanism involving the formation of a zymosan-C5-convertase and bystander lysis of the target cells. In contrast to the normal alternative pathway assay the zymosan-potentiated test did, most probably, not involve natural antibodies. Cobra venom factor was more efficient in enhancing the sensitivity of the assay for the mouse alternative complement pathway than zymosan. This makes this factor very useful for testing C-poor body fluids.

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Role of C4-Binding Protein in the Defective Lysis of Sensitized Sheep Erythrocytes by Mouse Complement

Cited by 5 publications

References 15 publications

Mechanism of activation of the classical pathway of complement by monoclonal IgE (DES). Restricted regulation of C4b by C4b‐binding protein

Mechanism of activation of the classical pathway of complement by monoclonal IgE (DES). Restricted regulation of C4b by C4b‐binding protein

Complement and Complement Reactions

Study of the optimal reaction conditions for assay of the mouse alternative complement pathway

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