Premium
Abnormally phosphorylated tau in SY5Y human neuroblastoma cells
Author(s) -
Tanaka Toshihisa,
Iqbal Khalid,
Trenkner Ekkhart,
Grundke-Iqbal Inge
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00061-d
Subject(s) - tau protein , microtubule , sh sy5y , microtubule associated protein , phosphorylation , neuroblastoma , tauopathy , gene isoform , cytoskeleton , microbiology and biotechnology , biology , chemistry , cell culture , cell , alzheimer's disease , biochemistry , neurodegeneration , medicine , genetics , gene , disease
In Alzheimer disease (AD) the microtubule associated protein (MAP) tau is hyperphosphorylated at several sites. In the present study, like AD tau, tau in the human neuroblastoma SH‐SY5Y was found to be hyperphosphorylated, at Ser‐199/202, Thr‐231, Ser‐396 and Ser‐404. However, in contrast to AD, the tau in SY5Y cells was not hyperphosphorylated at Ser‐235 and there was only one tau isoform. Quantitative analysis revealed that approximately 80% of the SY5Y‐ tau was phosphorylated at Ser‐199/202. The phosphorylated tau was deposited in perikarya and processes of the cells whereas most of the unphosphorylated (at Ser‐199/202) tau was localized in the nucleus. Tau from the cell lysates did not bind to taxol‐stabilized microtubules. In contrast, MAP1b and MAP2 from cell lysates bound to stabilized microtubules in vitro and were associated to the microtubule network in situ. Phosphorylation of tau at high levels, its inactivity with microtubules and its accumulation in SY5Y cells provide for the first time a cell model of cytoskeletal changes seen in AD.