Mortalin/GRP75 binds to complement C9 and plays a role in resistance to complement-dependent cytotoxicity

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Abstract

Background: Mortalin was shown to contribute to removal of the complement membranolytic C5b-9 complex from the target cell surface. Results: Modulations of mortalin expression and activity affect deposition of C5b-9 and cell death. Conclusion: Mortalin, through its ATPase domain, regulates the C5b-9 deposition and confers resistance to complement-dependent cytotoxicity. Significance: Mortalin is a potential therapeutic target in autoimmune diseases and in cancer immunotherapy. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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Ray, M. S., Moskovich, O., Iosefson, O., & Fishelson, Z. (2014). Mortalin/GRP75 binds to complement C9 and plays a role in resistance to complement-dependent cytotoxicity. Journal of Biological Chemistry, 289(21), 15014–15022. https://doi.org/10.1074/jbc.M114.552406

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