TY - JOUR
T1 - Raji cell injury and subsequent lysis by the purified cytolytic alternative pathway of human complement
AU - Schreiber, Robert D.
AU - Pangburn, Michael K.
AU - Medicus, Rudolf G.
AU - Müller-Eberhard, Hans J.
N1 - Funding Information:
1 This is publication No. 1924 from the Department of Molecular Immunology, Research Institute of Scripps Clinic, La Jolla, Calif. This work was supported by United States Public Health Service Grants AI 07007 and HL 16411. * Recipient of Established Investigatorship 77-202 of the American Heart Association. 3 Recipient of National Institutes of Health Postdoctoral Fellowship AI 05569. 1 Present address: Universite De Lausanne, Institut De Biochimie, Chemin des Boveresses, CH-1066 Epalinges sur Lausanne, Switzerland. 5 Cecil H. & Ida Green Investigator in Medical Research, Research Institute of Scripps Clinic. Abbreviations used: C3bINA. C3b inactivator; PCAP, purified cytolytic alternative pathway; MAC, membrane attack complex; NHSsC4, normal human serum depleted of C4; RI, restriction index; E,, rabbit erythrocyte: Es, sheep erythrocyte: E,, human erythrocyte.
PY - 1980/3
Y1 - 1980/3
N2 - Lysis of Raji cells could be effected by the 11 proteins of the purified cytolytic alternative pathway of complement (PCAP) not including immunoglobulins. Lysis was dose dependent and slow, reaching completion only after 10-20 hr. Cellular uptake of complement proteins occurred early during incubation as evidenced by the binding of radiolabeled properdin and C9. 86Rb release paralleled C9 uptake and was complete in 2 hr. After inhibition of cell metabolism by puromycin the kinetics of cell lysis paralleled C9 uptake and 86Rb release. Raji cells appear to be weak activators of the alternative pathway since properdin and C9 deposition was approximately 10 times slower than their deposition on strong pathway activators. Control of cell-bound C3b by β1H was reduced and intermediate to strong activators and nonactivators. The results indicate that activation of the alternative pathway by Raji cells leads to formation and binding of the membrane attack complex which in turn produces functional membrane lesions. The initial membrane injury does not result in immediate cell death. The time course of cell lysis was 7 times slower than that of formation of the initial lesion.
AB - Lysis of Raji cells could be effected by the 11 proteins of the purified cytolytic alternative pathway of complement (PCAP) not including immunoglobulins. Lysis was dose dependent and slow, reaching completion only after 10-20 hr. Cellular uptake of complement proteins occurred early during incubation as evidenced by the binding of radiolabeled properdin and C9. 86Rb release paralleled C9 uptake and was complete in 2 hr. After inhibition of cell metabolism by puromycin the kinetics of cell lysis paralleled C9 uptake and 86Rb release. Raji cells appear to be weak activators of the alternative pathway since properdin and C9 deposition was approximately 10 times slower than their deposition on strong pathway activators. Control of cell-bound C3b by β1H was reduced and intermediate to strong activators and nonactivators. The results indicate that activation of the alternative pathway by Raji cells leads to formation and binding of the membrane attack complex which in turn produces functional membrane lesions. The initial membrane injury does not result in immediate cell death. The time course of cell lysis was 7 times slower than that of formation of the initial lesion.
UR - http://www.scopus.com/inward/record.url?scp=0018844878&partnerID=8YFLogxK
U2 - 10.1016/0090-1229(80)90050-1
DO - 10.1016/0090-1229(80)90050-1
M3 - Article
C2 - 6899978
AN - SCOPUS:0018844878
SN - 0090-1229
VL - 15
SP - 384
EP - 396
JO - Clinical Immunology and Immunopathology
JF - Clinical Immunology and Immunopathology
IS - 3
ER -