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Hsp70 binds to PrP C in the process of PrP C release via exosomes from THP‐1 monocytes
Author(s) -
Wang Guihua,
Zhou Xiangmei,
Bai Yu,
Yin Xiaomin,
Yang Lifeng,
Zhao Deming
Publication year - 2011
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20090391
Subject(s) - microvesicles , endosome , microbiology and biotechnology , exosome , secretion , chemistry , intracellular , extracellular , hsp70 , glycoprotein , biology , biochemistry , heat shock protein , microrna , gene
PrP C (cellular prion protein) is a GPI (glycophosphatidylinositol)‐anchored protein present on the surface of a number of peripheral blood cells. PrP C must be present for the generation and propagation of pathogenic conformer [PrP Sc (scrapie prion protein)], which is a conformational conversion form of PrP C and has a central role in transmissible spongiform encephalopathies. It is important to determine the transportation mechanism of normal PrP C between cells. Exosomes are membrane vesicles released into the extracellular space upon fusion of multivesicular endosomes with the plasma membrane. We have identified that THP‐1 monocytes can secrete exosomes to culture medium, and the secreted exosomes can bear PrP C . We also found that Hsp70 interacts with PrP C not only in intracellular environment, but in the secreted exosomes. However, the specific markers of exosomes, Tsg101 and flotillin‐1, were found with no interaction with PrP C . Our results demonstrated that PrP C can be released from THP‐1 monocytes via secreted exosomes, and in this process, Hsp70 binds to PrP C , which suggests that Hsp70 may play a potential functional role in the release of PrP C .