Elongation factor-1alpha as a homologous complement activator of Jurkat cells.
Although increasing evidence exist suggesting that apoptotic cells activate homologous complement, the homologous complement activators are only poorly characterized. We found that cell lysate of Jurkat cells contained a homologous complement activator of 50 kDa. Digestion of the 50 kDa activator with lysylendopeptidase yielded peptide fragments, with sequences identical to those of EF-1alpha. The 50 kDa activator was removed by immunoadsorption with anti-EF-1alpha, suggesting that the 50 kDa activator is EF-1alpha. The homologous complement activation did not proceed with EGTA-serum. In addition, C4b, a fragment produced by activation of the classical or lectin pathways was found to bind with EF-1alpha. These results suggest that EF-1alpha activates the homologous complement through the classical or lectin pathway.
Aoki
H
H
Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Takizawa
F
F
Tsuji
S
S
Nagasawa
S
S
D000595:Amino Acid Sequence; D017209:Apoptosis; D015153:Blotting, Western; D003167:Complement Activation; D015935:Complement C4b / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005434:Flow Cytometry; D006801:Humans; D019169:Jurkat Cells; D008969:Molecular Sequence Data; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1 / Q000737:chemistry / Q000378:metabolism*; D020539:Sequence Analysis, Protein
D020648:Peptide Elongation Factor 1; D015935:Complement C4b