Studying the mechanism of CD47–SIRPα interactions on red blood cells by single molecule force spectroscopy
Source abstract
Abstract
The interaction forces and binding kinetics between SIRPα and CD47 were investigated by single-molecule force spectroscopy (SMFS) on both fresh and experimentally aged human red blood cells (hRBCs). We found that CD47 experienced a conformation change after oxidation, which influenced the interaction force and the position of the energy barrier between SIRPα and CD47. Our results are significant for understanding the mechanism of phagocytosis of red blood cells at the single molecule level.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Erythrocyte Function and Pathophysiology · Lipid Membrane Structure and Behavior · Force Microscopy Techniques and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P.R. China
University of Chinese Academy of Sciences, Beijing 100049, P.R. China
Institute of Immunology, The First Bethune Hospital Academy of Translational Medicine, Jilin University, ChangChun, 130012, China
References (28)
Show source-provided references
1. Lindberg · J. Cell Biol. · 1993 · 123 · 48510.1083/jcb.123.2.485 ↗
2. Matozaki · Trends Cell Biol. · 2009 · 19 · 7210.1016/j.tcb.2008.12.001 ↗
3. Sato · Biochem. Biophys. Res. Commun. · 2003 · 309 · 58410.1016/j.bbrc.2003.08.031 ↗
4. Barclay · Nat. Rev. Immunol. · 2006 · 6 · 45710.1038/nri1859 ↗
5. van den Berg · Trends Immunol. · 2008 · 29 · 20310.1016/j.it.2008.02.004 ↗
6. Burger · Blood · 2012 · 119 · 551210.1182/blood-2011-10-386805 ↗
7. Fossati-Jimack · J. Autoimmun. · 2002 · 18 · 1710.1006/jaut.2001.0563 ↗
8. Khandelwal · Transfusion · 2007 · 47 · 172510.1111/j.1537-2995.2007.01348.x ↗
9. Stewart · Transfusion · 2005 · 45 · 149610.1111/j.1537-2995.2005.00564.x ↗
10. Anniss · Transfus. Apher. Sci. · 2002 · 27 · 23310.1016/S1473-0502(02)00070-8 ↗
11. Shan · Nanoscale · 2012 · 4 · 128310.1039/c2nr11541g ↗
12. Zhu · Nat. Nanotechnol. · 2010 · 5 · 78810.1038/nnano.2010.212 ↗
13. Wildling · J. Biol. Chem. · 2012 · 287 · 10510.1074/jbc.M111.304873 ↗
14. Hinterdorfer · Proc. Natl. Acad. Sci. U. S. A. · 1996 · 93 · 347710.1073/pnas.93.8.3477 ↗
15. Florin · Science · 1994 · 264 · 41510.1126/science.8153628 ↗
16. Shan · Chem. Commun. · 2011 · 47 · 809110.1039/c1cc11453k ↗
17. Zhao · Nanoscale · 2013 · 5 · 322610.1039/c3nr00553d ↗
18. Zhang · Phys. Chem. Chem. Phys. · 2013 · 15 · 650810.1039/c3cp51072g ↗
19. Hao · Nat. Commun. · 2013 · 4 · 212110.1038/ncomms3121 ↗
20. Riener · Anal. Chim. Acta · 2003 · 497 · 10110.1016/j.aca.2003.08.041 ↗
21. Shen · Phys. Med. Biol. · 2007 · 52 · 218510.1088/0031-9155/52/8/010 ↗
22. Evans · Biophys. J. · 1997 · 72 · 154110.1016/S0006-3495(97)78802-7 ↗
23. Brown · Trends Cell Biol. · 2001 · 11 · 13010.1016/S0962-8924(00)01906-1 ↗
24. Rietsch · Annu. Rev. Genet. · 1998 · 32 · 16310.1146/annurev.genet.32.1.163 ↗
25. Bustamante · Annu. Rev. Biochem. · 2004 · 73 · 70510.1146/annurev.biochem.72.121801.161542 ↗
26. Li · Nature · 2002 · 418 · 99810.1038/nature00938 ↗
27. Oberhauser · J. Mol. Biol. · 2002 · 319 · 43310.1016/S0022-2836(02)00306-6 ↗
28. Finke · Virus Res. · 2005 · 111 · 12010.1016/j.virusres.2005.04.004 ↗