Abstract
The binding of C1q to the human macrophage cell line U937 has been studied. Fluorescence microscopy with fluorescein-conjugated F(ab')2 anti-C1q antibody showed that 100% of the cell population is able to bind exogenous C1q. Monomeric C1q binding to U937 cells is very weak at normal ionic strength (I0.15) and was therefore investigated at I0.07, conditions which stabilize the binding. However, aggregation of C1q on dextran sulphate or a lipid A-rich lipopolysaccharide allowed a firm, binding at I0.15. Quantitative binding studies with monomeric 125I-C1q showed a concentration-dependent, saturable, specific and reversible binding involving specific membrane receptors. Scatchard plots of C1q binding indicated [1.6 +/- 0.7 (1 S.D.)] X 10(6) sites per cell with an equilibrium constant of (2.9 +/- 1.8) X 10(7) M-1 at I0.07. The location of the molecule region mediating C1q binding was established with collagen-like fragments prepared by partial pepsin digestion, confirming earlier results obtained by inhibition studies.
MeSH Terms
Binding Sites
Carrier Proteins
Cell Line
Collagen/metabolism
Fluorescent Antibody Technique
Humans
Hyaluronan Receptors
Kinetics
Macrophages/immunology
Membrane Glycoproteins
Mitochondrial Proteins
Osmolar Concentration
Peptide Fragments/metabolism
Peptide Hydrolases/pharmacology
Receptors, Complement/drug effects,metabolism
Chemicals
C1QBP protein, human
Carrier Proteins
Hyaluronan Receptors
Membrane Glycoproteins
Mitochondrial Proteins
Peptide Fragments
Receptors, Complement
complement 1q receptor
Collagen
Peptide Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Arvieux J
Reboul A
Bensa J C
Colomb M G
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