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Prion protein and its ligand stress inducible protein 1 regulate astrocyte development
Author(s) -
Arantes Camila,
Nomizo Regina,
Lopes Marilene H.,
Hajj Glaucia N. M.,
Lima Flavia R. S.,
Martins Vilma R.
Publication year - 2009
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.20861
Subject(s) - astrocyte , biology , glial fibrillary acidic protein , microbiology and biotechnology , signal transduction , nestin , wild type , kinase , protein kinase a , neural stem cell , stem cell , mutant , biochemistry , immunology , central nervous system , neuroscience , immunohistochemistry , gene
Prion protein (PrP C ) interaction with stress inducible protein 1 (STI1) mediates neuronal survival and differentiation. However, the function of PrP C in astrocytes has not been approached. In this study, we show that STI1 prevents cell death in wild‐type astrocytes in a protein kinase A‐dependent manner, whereas PrP C ‐null astrocytes were not affected by STI1 treatment. At embryonic day 17, cultured astrocytes and brain extracts derived from PrP C ‐null mice showed a reduced expression of glial fibrillary acidic protein (GFAP) and increased vimentin and nestin expression when compared with wild‐type, suggesting a slower rate of astrocyte maturation in PrP C ‐null animals. Furthermore, PrP C ‐null astrocytes treated with STI1 did not differentiate from a flat to a process‐bearing morphology, as did wild‐type astrocytes. Remarkably, STI1 inhibited proliferation of both wild‐type and PrP C ‐null astrocytes in a protein kinase C‐dependent manner. Taken together, our data show that PrP C and STI1 are essential to astrocyte development and act through distinct signaling pathways. © 2009 Wiley‐Liss, Inc.