C1q binding and C1 activation by various isolated cellular membranes.

Cellular and subcellular membranes obtained from heart, liver, and brain tissue from human, baboon, bovine, rabbit, and rat bound highly purified, radioiodinated human C1q with a high affinity (Ka = 10(8) to 10(10) M-1). The majority of these membrane preparations were able to activate fully assembled C1 as evidenced by the conversion of 125I-C1s, incorporated into C1 complexes, to 125I-C1s. C1 activation by baboon heart mitochondrial membranes required an intact C1 complex and appeared to be mediated by the binding of the C1q subcomponent in that excess C1q completely blocked C1 activation. Several experiments suggested that the heart mitochondrial membrane binding site for C1q is an integral component of the mitochondrial membrane and that C1q interacted with the membrane binding site through its globular head regions. It is suggested that the binding of C1q and the activation of C1 by cellular and subcellular membranes may be involved in the initiation and/or enhancement of the inflammatory process after acute tissue damage.