PMID: 6975126Sep 29, 1981Paper

Interaction of collagen with C1q via its collagen-like portion

Biochimica Et Biophysica Acta
E J MenzelK B Reid

Abstract

Interactions between human collagens type I, II and III with human C1q or its collagen-like fragment (CLF) were investigated with different techniques. It was found that in solution both C1q and CLF form stable complexes with the native collagens. No preferential binding to a specific collagen type was observed. If C1q (CLF) was adsorbed to polystyrene or fixed to erythrocytes, a more efficient interaction with collagen was displayed by C1q than by CLF. If collagen represents the solid phase, the binding of CLF is stronger than that of C1q. Inhibition studies indicate that the interaction between C1q and collagens takes place via the collagen-like part of C1q. Intermolecular attraction due to polar amino acid residues seems to be of major importance for this interaction.

References

Jan 1, 1979·International Archives of Allergy and Applied Immunology·R AllanH Isliker
Jan 1, 1975·International Archives of Allergy and Applied Immunology·M TakahashiM Matsuura
Jan 1, 1977·Journal of Immunological Methods·J Menzel
Oct 20, 1975·Biochimica Et Biophysica Acta·A J BaileyA Delaunay
Jan 1, 1976·Analytical Biochemistry·R L Trelstad, K R Lawley
Nov 1, 1967·Clinica Chimica Acta; International Journal of Clinical Chemistry·H Stegemann, K Stalder
Oct 1, 1962·Analytical Biochemistry·T BITTER, H M MUIR
Sep 1, 1964·The Journal of Clinical Investigation·P BORNSTEIN, K A PIEZ

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