NR APUU
AU Hachiya,N.S.; Watanabe,K.; Sakasegawa,Y.; Kaneko,K.
TI Microtubules-associated intracellular localization of the NH2-terminal cellular prion protein fragment
QU Biochemical and Biophysical Research Communications 2004 Jan 16; 313(3): 818-23
PT journal article
AB By utilizing double-labeled fluorescent cellular prion protein (PrPc), we revealed that the NH2-terminal and COOH-terminal PrPc fragments exhibit distinct distribution patterns in mouse neuroblastoma neuro2a (N2a) cells and HpL3-4, a hippocampal cell line established from prnp gene-ablated mice [Nature 400 (1999) 225]. Of note, the NH2-terminal PrPc fragment, which predominantly localized in the intracellular compartments, congregated in the cytosol after the treatment with a microtubule depolymerizer (nocodazole). Truncated PrPc with the amino acid residues 1-121, 1-111, and 1-91 in mouse (Mo) PrP exhibited a proper distribution profile, whereas those with amino acid residues 1-52 and 1-33 did not. These data indicate the microtubules-associated intracellular localization of the NH2-terminal PrPc fragment containing at least the 1-91 amino acid residues.
MH Animals; Blotting, Western; Cell Culture; Cell Line, Tumor; Cytosol/metabolism; DNA/metabolism; Luminescent Proteins/metabolism; Mice; Microscopy, Fluorescence; Microtubules/*metabolism; Nocodazole/pharmacology; PrPc Proteins/*chemistry/metabolism; Protein Structure, Tertiary; Support, Non-U.S. Gov't; Tubulin/metabolism
AD Department of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo 187-8502, Japan.
SP englisch
PO USA