Klickstein L B, Barbashov S F, Liu T, Jack R M, Nicholson-Weller A
Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA.
Immunity. 1997 Sep;7(3):345-55. doi: 10.1016/s1074-7613(00)80356-8.
Molecular definition of the cellular receptor for the collagen domain of C1q has been elusive. We now report that C1q binds specifically to human CR1 (CD35), the leukocyte C3b/C4b receptor, and the receptor on erythrocytes for opsonized immune complexes. Biotinylated or radioiodinated C1q (*C1q) bound specifically to transfected K562 cells expressing cell surface CR1 and to immobilized recombinant soluble CR1 (rsCR1). *C1q binding to rsCR1 was completely inhibited by unlabeled C1q and the collagen domain of C1q and was partially inhibited by C3b dimers. Kinetic analysis in physiologic saline of the interaction of unlabeled C1q with immobilized rsCR1 using surface plasmon resonance yielded an apparent equilibrium dissociation constant (K[eq2]) of 3.9 nM. Thus, CR1 is a cellular C1q receptor that recognizes all three complement opsonins, namely, C1q, C3b, and C4b.
C1q胶原结构域细胞受体的分子定义一直难以捉摸。我们现在报告,C1q特异性结合人CR1(CD35),即白细胞C3b/C4b受体以及红细胞上调理素化免疫复合物的受体。生物素化或放射性碘化的C1q(C1q)特异性结合表达细胞表面CR1的转染K562细胞以及固定化的重组可溶性CR1(rsCR1)。未标记的C1q和C1q的胶原结构域可完全抑制C1q与rsCR1的结合,C3b二聚体可部分抑制该结合。使用表面等离子体共振对未标记的C1q与固定化rsCR1在生理盐水中的相互作用进行动力学分析,得出表观平衡解离常数(K[eq2])为3.9 nM。因此,CR1是一种细胞C1q受体,可识别所有三种补体调理素,即C1q、C3b和C4b。