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Hypoxia induces expression of a GPI‐anchorless splice variant of the prion protein
Author(s) -
Kikuchi Yutaka,
Kakeya Tomoshi,
Nakajima Osamu,
Sakai Ayako,
Ikeda Kikuko,
Yamaguchi Naoto,
Yamazaki Takeshi,
Tanamoto Kenichi,
Matsuda Haruo,
Sawada Junichi,
Takatori Kosuke
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06452.x
Subject(s) - messenger rna , exon , cytosol , alternative splicing , biology , rna splicing , microbiology and biotechnology , cell culture , glycoprotein , gene , signal peptide , peptide sequence , biochemistry , rna , genetics , enzyme
The human prion protein (PrP) is a glycoprotein with a glycosylphosphatidylinositol (GPI) anchor at its C‐terminus. Here we report alternative splicing within exon 2 of the PrP gene ( PRNP ) in the human glioblastoma cell line T98G. The open reading frame of the alternatively spliced mRNA lacked the GPI anchor signal sequence and encoded a 230 amino acid polypeptide. Its product, GPI‐anchorless PrP (GPI − PrPSV), was unglycosylated and soluble in non‐ionic detergent, and was found in the cytosolic fraction. We also detected low levels of alternatively spliced mRNA in human brain and non‐neuronal tissues. When long‐term passaged T98G cells were placed in a low‐oxygen environment, alternatively spliced mRNA expression increased and expression of normally spliced PrP mRNA decreased. These findings imply that oxygen tension regulates GPI − PrPSV expression in T98G cells.