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Complement Factor H-Related Proteins FHR1 and FHR5 Interact With Extracellular Matrix Ligands, Reduce Factor H Regulatory Activity and Enhance Complement Activation

And another publication in (more or less) easy words!

🔬 Exciting new insights from Alexandra Papp, Mihály Józsi, and their team on Complement Factor H-Related Proteins FHR1 and FHR5! 🧪🧬

Their research aimed to understand whether FHR1 and FHR5 could bind to extracellular matrix (ECM) components and affect local Factor H (FH) activity and complement activation. They found that both FH and the FHRs displayed variable binding to ECM components.

💡 The team identified laminin, fibromodulin, osteoadherin, and PRELP as ligands of FHR1 and FHR5. They discovered that FHR1 bound to these ECM components through its C-terminal complement control protein (CCP) domains 4-5, while FHR5 bound via its middle region, CCPs 3-7.

🚀 FHR1 and FHR5 inhibited the binding of FH to the identified ECM proteins in a dose-dependent manner, which led to reduced FH cofactor activity. Moreover, both FHR1 and FHR5 enhanced alternative complement pathway activation on immobilized ECM proteins when exposed to human serum, resulting in increased deposition of C3-fragments, factor B, and C5b-9.

🌟 This groundbreaking research by Alexandra Papp, Mihály Józsi, and their team unveils novel ECM ligands of FH family proteins and suggests that FHR1 and FHR5 are competitive inhibitors of FH on ECM. When bound to these ligands, they may enhance local complement activation and promote inflammation under pathological conditions.

👏 Congratulations for their remarkable findings! Stay tuned for more discoveries in this field! #complementfactorH #FHR1 #FHR5 #extracellularmatrix #inflammation #research

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