Premium
Inhibition of bFGF activity by complement C1s: covalent binding of C1s with bFGF
Author(s) -
Sakiyama Hisako,
Kaji Kazuhiko,
Nakagawa Koichi,
Nagino Ken
Publication year - 1998
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/(sici)1099-0844(199809)16:3<159::aid-cbf779>3.0.co;2-8
Subject(s) - umbilical vein , incubation , chemistry , basic fibroblast growth factor , monomer , human umbilical vein endothelial cell , biochemistry , polyacrylamide gel electrophoresis , covalent bond , biophysics , chromatography , in vitro , enzyme , growth factor , biology , organic chemistry , receptor , polymer
The first complement component C1s formed large aggregates with bFGF when bFGF and C1s were incubated at 37°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 m M &base;) 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. © 1998 John Wiley & Sons, Ltd.