Inhibition of bFGF activity by complement C1s: covalent binding of C1s with bFGF
✍ Scribed by Hisako Sakiyama; Kazuhiko Kaji; Koichi Nakagawa; Ken Nagino
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 136 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0263-6484
No coin nor oath required. For personal study only.
✦ Synopsis
The ®rst complement component C1s formed large aggregates with bFGF when bFGF and C1s were incubated at 378C 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 growthstimulating activity of bFGF was measured by using human umbilical vein endothelial cells (HUVEC) as indicator cells. The aggregate formation between C1s and bFGF signi®cantly reduced the activity of bFGF.
📜 SIMILAR VOLUMES
## Abstract ## Objective Suppression of bone destruction is required as part of an effective therapeutic strategy for autoimmune arthritis. Although numerous antirheumatic drugs are in clinical use, little is known about whether they inhibit bone destruction by acting on activated T cells or other
We have previously shown that CD4 ligands inhibit interleukin-2 (IL-2) production and T cell proliferation in human peripheral CD4 + T lymphocytes, in an MHC-independent way. Two major pathways implicated in T cell activation are inhibited by binding of CD4 ligands to the CD4 molecule, i. e. Ca 2+ s