TY - JOUR
T1 - Microtubules-associated intracellular localization of the NH 2-terminal cellular prion protein fragment
AU - Hachiya, Naomi S.
AU - Watanabe, Kota
AU - Sakasegawa, Yuji
AU - Kaneko, Kiyotoshi
N1 - Funding Information:
We greatly thank S.B. Prusiner and D.A. Harris for discussions and comments, T. Onodera for providing us the HpL3-4 cell line, M. Kawabata, E. Nannri, C. Ota, and Y. Yamaura for technical assistances. This work was supported by grants from the Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Agency, Health and Labour Sciences Research Grants, Research on Advanced Medical Technology, nano-001, and the Ministry of Health, Labor, and Welfare of Japan.
PY - 2004/1/16
Y1 - 2004/1/16
N2 - By utilizing double-labeled fluorescent cellular prion protein (PrP C), 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 PrP C 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.
AB - By utilizing double-labeled fluorescent cellular prion protein (PrP C), 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 PrP C 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.
KW - Fluorescent protein
KW - Microtubules
KW - Nocodazole
KW - Prion protein
KW - Proteolytic cleavage
KW - Subcellular localization
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U2 - 10.1016/j.bbrc.2003.11.167
DO - 10.1016/j.bbrc.2003.11.167
M3 - Article
C2 - 14697265
AN - SCOPUS:0347063992
VL - 313
SP - 818
EP - 823
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -