Barbera, Stefano and Raucci, Luisa and Tassone, Giusy and Tinti, Laura and Prischi, Filippo and Santucci, Annalisa and Mongiat, Maurizio and Tosi, Gian Marco and Galvagni, Federico and Dimberg, Anna and Pozzi, Cecilia and Orlandini, Maurizio (2023) Dimerization of the C-type lectin-like receptor CD93 promotes its binding to Multimerin-2 in endothelial cells. International Journal of Biological Macromolecules, 224. pp. 453-464. DOI https://doi.org/10.1016/j.ijbiomac.2022.10.136
Barbera, Stefano and Raucci, Luisa and Tassone, Giusy and Tinti, Laura and Prischi, Filippo and Santucci, Annalisa and Mongiat, Maurizio and Tosi, Gian Marco and Galvagni, Federico and Dimberg, Anna and Pozzi, Cecilia and Orlandini, Maurizio (2023) Dimerization of the C-type lectin-like receptor CD93 promotes its binding to Multimerin-2 in endothelial cells. International Journal of Biological Macromolecules, 224. pp. 453-464. DOI https://doi.org/10.1016/j.ijbiomac.2022.10.136
Barbera, Stefano and Raucci, Luisa and Tassone, Giusy and Tinti, Laura and Prischi, Filippo and Santucci, Annalisa and Mongiat, Maurizio and Tosi, Gian Marco and Galvagni, Federico and Dimberg, Anna and Pozzi, Cecilia and Orlandini, Maurizio (2023) Dimerization of the C-type lectin-like receptor CD93 promotes its binding to Multimerin-2 in endothelial cells. International Journal of Biological Macromolecules, 224. pp. 453-464. DOI https://doi.org/10.1016/j.ijbiomac.2022.10.136
Abstract
Blocking the signaling activated by the plasma membrane receptor CD93 has recently been demonstrated a useful tool in antiangiogenic treatment and oncotherapy. In the proliferating endothelium, CD93 regulates cell adhesion, migration, and vascular maturation, yet it is unclear how CD93 interacts with the extracellular matrix activating signaling pathways involved in the vascular remodeling. Here for the first time we show that in endothelial cells CD93 is structured as a dimer and that this oligomeric form is physiologically instrumental for the binding of CD93 to its ligand Multimerin-2. Crystallographic X-ray analysis of recombinant CD93 reveals the crucial role played by the C-type lectin-like and sushi-like domains in arranging as an antiparallel dimer to achieve a functional binding state, providing key information for the future design of new drugs able to hamper CD93 function in neovascular pathologies.
Item Type: | Article |
---|---|
Uncontrolled Keywords: | Angiogenesis; CD93; Crystallography; Mass spectrometry; Neovascularization |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 04 Jan 2023 11:48 |
Last Modified: | 07 Aug 2024 20:13 |
URI: | http://repository.essex.ac.uk/id/eprint/33829 |
Available files
Filename: 1-s2.0-S0141813022023789-main.pdf
Licence: Creative Commons: Attribution-Noncommercial-No Derivative Works 3.0