Inhibition of bFGF activity by complement C1s: covalent binding of C1s with bFGF.
The first complement component C1s formed large aggregates with bFGF when bFGF and C1s were incubated at 37 degrees C overnight. Under non-reducing conditions, a part of the aggregates did not penetrate into 5% polyacrylamide gel in the presence of SDS, and the rest penetrated into 5% gel but not into 12% gel. The aggregates were dissociated into monomers by reducing with 2-mercaptoethanol. Both active and inactive C1s formed aggregates with bFGF. In addition, a portion of bFGF was degraded by active C1s but not by inactive C1s. Aggregates were not formed when 2-mercaptoethanol (2 mM) was added to the incubation mixture. After the incubation with C1s the growth-stimulating activity of bFGF was measured by using human umbilical vein endothelial cells (HUVEC) as indicator cells. The aggregate formation between C1s and bFGF significantly reduced the activity of bFGF.
Sakiyama
H
H
Division of Cell Biology and Oncology, National Institute of Radiological Sciences, Chiba, Japan.
Kaji
K
K
Nakagawa
K
K
Nagino
K
K
D001681:Biological Assay; D002454:Cell Differentiation; D019902:Chondrocytes / Q000166:cytology; D003172:Complement C1 / Q000378:metabolism / Q000494:pharmacology*; D004730:Endothelium, Vascular; D016222:Fibroblast Growth Factor 2 / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006801:Humans; D011485:Protein Binding
D003172:Complement C1; D016222:Fibroblast Growth Factor 2