Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining

Author:

Tanaka Misaki1,Fujiwara Ai1,Suzuki Akio1,Yamasaki Takeshi1,Hasebe Rie1,Masujin Kentaro23,Horiuchi Motohiro1

Affiliation:

1. Laboratory of Veterinary Hygiene, Graduate School of Veterinary Medicine, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Japan

2. National Agriculture Food Research Organization (NARO), 3-1-5 Kannondai, Tsukuba, Ibaraki, 305-0856, Japan

3. Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, USA

Publisher

Microbiology Society

Subject

Virology

Reference48 articles.

1. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain

2. Stimulation of PrPC Retrograde Transport toward the Endoplasmic Reticulum Increases Accumulation of PrPSc in Prion-infected Cells

3. Evidence for synthesis of scrapie prion proteins in the endocytic pathway;Borchelt;J Biol Chem,1992

4. Activation of the JNK-c-Jun pathway during the early phase of neuronal apoptosis induced by PrP106-126 and prion infection

5. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive;Caughey;J Biol Chem,1991

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