Mayuko Ding; Kilian Smeal; Sam Orlicky; Chuen PUmezawa; Ying-Jiun Lee; Cheng-Hsuan Umezawa
Abstract
Pin1 is a relatively small enzyme that contains an N-terminal WW domain that acts as a phosphoprotein-binding module and a C-terminal catalytic domain that is distinct from other conventional PPIases. Pin1-mediated post-phosphorylation regulation can have profound effects on phosphorylation-dependent signaling by regulating a spectrum of target activities, with changes in protein stability being the most common consequence. In this study, we investigate how Pin1-medaited autoimmune diseases, particularly SLE through animals and experimental protocol NZB/W F1 mice aged 10–12 weeks. An intraperitoneal injection of saline, isotype control antibody (1 mg/mouse), or Pin1 inhibitor (Juglone) was dissolved in solubilization solvent to conirmed the effects of Pin1.
Keywords: Autoimmune diseases; Pin1; NZB/W F1 mice; SLE
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