Activation of C1 by monoclonal antibodies directed against C1q |
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| Authors: | E Kilchherr V N Schumaker L K Curtiss |
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| Affiliation: | 1. The Department of Chemistry and Biochemistry University of California, Los Angeles, CA 90024 USA;2. The Molecular Biology Institute, University of California, Los Angeles, CA 90024 USA;1. The Research Institute of the Scripps Clinic Torrey Pines Boulevard, La Jolla, Calif. 92037 USA;1. Key Laboratory of Superlight Materials and Surface Technology, Ministry of Education, College of Materials Science and Chemical Engineering, Harbin Engineering University, Harbin, 150001, China;2. Fundamental Science on Nuclear Safety and Simulation Technology Laboratory, Harbin Engineering University, Harbin, 150001, China;1. Department of Radiology, Children''s Hospital of Philadelphia, Philadelphia, PA, 19104, USA;2. Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA;1. Scuola Normale Superiore, Pisa, Italy;2. Department of Computer Science, KU Leuven, Belgium |
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| Abstract: | Eleven monoclonal antibodies directed against the subcomponent C1q of the first component of human complement, C1, were prepared and tested for binding to intact C1q and to the collagenous portion, the C1q stalks. All of the monoclonals bound well to the intact C1q. Eight out of the eleven exhibited strong binding to the collagenous stalks, while three bound very weakly, if at all, to the stalks and, thus, were presumed to bind to the pepsin-sensitive region which includes the C1q heads. For one of the latter monoclonals, this was confirmed by electron microscopy. Five of the monoclonals were purified by C1q affinity chromatography. When tested with C1 reassembled from its subunits, two of these purified monoclonal antibodies markedly enhanced the rate of spontaneous activation. |
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