期刊
BIOPOLYMERS
卷 106, 期 2, 页码 184-195出版社
WILEY
DOI: 10.1002/bip.22754
关键词
extracellular matrix; fibulin-7; peptides; cell adhesion; endothelial cell
资金
- International Research Fellowship of the Japan Society for the Promotion of Science (JSPS)
- Ministry of Education, Culture, Sports, Science and Technology (MEXT)-Supported Program for the Strategic Research Foundation at Private Universities [S1101009]
- JSPS [26.04914]
- Intramural Research Program of the National Institute of Dental and Craniofacial Research, NIH
- Grants-in-Aid for Scientific Research [15F15120, 15K09326, 14F04914] Funding Source: KAKEN
Despite the research done on pathological angiogenesis, there is still a need for the development of new therapies against angiogenesis-related diseases. Fibulin-7 (Fbln7) is a member of the extracellular matrix fibulin protein family. The Fbln7 C-terminal fragment, Fbln7-C, binds to endothelial cells and inhibits their tube formation in culture. In this study, we screened 12 synthetic peptides, covering the fibulin-globular domain of Fbln7-C, to identify active sites for endothelial cell adhesion and in vitro antiangiogenic activity. Three peptides, fc10, fc11, and fc12, promoted Human Umbilical Vein Endothelial Cells (HUVECs) adhesion, and the morphology of HUVECs on fc10 was similar to that on Fbln7-C. EDTA and the anti-integrin 1 function-blocking antibody inhibited HUVECs adhesion to both fc10 and fc12, and heparin inhibited HUVECs adhesion to both fc11 and fc12. fc10 and fc11 inhibited HUVECs tube formation. Our results suggest that three peptides from Fbln7-C are biologically active for endothelial cell adhesion and disrupt the tube formation, suggesting a potential therapeutic use of these peptides for angiogenesis-related diseases. (c) 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 184-195, 2016.
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