更新情報
ホーム > 更新情報一覧 > 特別講演会のお知らせ【2019.10. 9 Dr. Mark D. Zabel】

北海道支部について

特別講演会のお知らせ【2019.10. 9 Dr. Mark D. Zabel】(2019.10.07更新)

演題

Cellular prion protein folds into a physiologic prion to modulate B cell responses to extracellular bacterial infections

演者

Dr. Mark D. Zabel

所属

Prion Research Center, Department of Microbiology, Immunology, and Pathology College of Veterinary Medicine & Biomedical Sciences Colorado State University, USA

日時

2019年10月9日 (水) 16:00 ~

場所

北海道大学 遺伝子病制御研究所 5F セミナー室

主催

北海道大学遺伝子病制御研究所大学院医学院分子神経免疫学、動物機能医科学研究室 世話人:村上正晃、長谷部 理絵

概要
Recent evidence suggests protein aggregation and/or misfolding serves physiological functions in various biological contexts. We tested whether the cellular prion protein (PrPC), the prototypical pathologic amyloid-forming protein, aggregates and coordinates signaling events involved in B cell activation. We show PrPC transforms from soluble to insoluble after activating B cells in vitro. We further show that while prnp-knockout (PrP KO) mice develop normal splenic architecture and lymphocyte proportions, PrPC deficiency renders these mice immunocompromised. B cells from PrP KO mice show impaired calcium signaling, SRC family kinase phosphorylation, and antibody production. We further show PrPC likely signals in cooperation with CD21/35 because Cr2-knockout mice mirror the PrP KO phenotype, and CD21/35 directly interacts with PrP. Further, we show inefficient translocation of CD21/35 to lipid rafts in PrP KO mice when challenged with extracellular bacteria in vivo and B cell activation in vitro. Crosslinking CD21 in conjunction with IgM and/or CD40 renders PrPC protease-resistant and insoluble. These results implicate cellular prion protein aggregation as an immunologic mechanism that modulates B cell activation.
 
連絡先
北海道大学遺伝子病制御研究所分子神経免疫学分野 

札幌市北区北15条西7丁目
上村大輔
011-706-5120、kamimura@igm.hokudai.ac.jp

関連資料