A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes.
SP40,40 was isolated from the soluble membrane attack complex (SC5b-9) by HPLC using a reverse-phase column. Amino acid compositions of its alpha- and beta-subunits were similar to each other with the exception of glycine content. Amino-terminal sequences of its alpha- and beta-subunits were identical to those of the subunits prepared from human serum, respectively, indicating that there was no degradation of SP40,40 during incorporation into SC5b-9. When guinea pig erythrocytes were incubated with C56f, C7, C8 and C9 in the presence of SP40,40, SP40,40 enhanced the hemolysis. The protein, however, inhibited the hemolysis when erythrocytes were pre-incubated with C56f and SP40,40 prior to the addition of C7, C8 and C9. These findings indicate that SP40,40 modulates the formation of membrane attack complex by interacting with C56f at the first step, and that the co-existence of other factors, besides C56f, is required for the enhancing activity of SP40,40.
Choi
N H
NH
Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University, Tokyo, Japan.
Mazda
T
T
Tomita
M
M
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D051152:Clusterin; D015938:Complement Membrane Attack Complex / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000276:immunology*; D006023:Glycoproteins; D006461:Hemolysis; D018832:Molecular Chaperones
D000596:Amino Acids; D001798:Blood Proteins; D051152:Clusterin; D015938:Complement Membrane Attack Complex; D006023:Glycoproteins; D018832:Molecular Chaperones