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. 1983 May;52(2):305–310.

Fibronectin binds to C1q: possible mechanisms for their co-precipitation in cryoglobulins from patients with systemic lupus erythematosus.

I Kono, T Sakurai, T Kabashima, K Yamane, H Kashiwagi
PMCID: PMC1535854  PMID: 6602675

Abstract

Fibronectin and C1q frequently co-precipitated in cryoglobulins from patients with SLE. As a portion of the C1q molecule is similar to collagen to which fibronectin has a high affinity, we studied whether fibronectin specifically bound to C1q. Fibronectin was found to bind to both native and heat-inactivated C1q. The binding was enhanced by Ca++ and low ionic strength. We have also demonstrated that fibronectin is capable of binding to C1q fixed to immune complexes. The interaction between fibronectin and C1q may play a role in cryoglobulin formation and in clearance of immune complexes by reticuloendothelial system.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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