TY - JOUR
T1 - Phospho-Tau Protein Expression in the Cell Cycle of SH-SY5Y Neuroblastoma Cells
T2 - A Morphological Study
AU - Flores-Rodríguez, Paola
AU - Harrington, Charles R.
AU - Wischik, Claude M.
AU - Ibarra-Bracamontes, Vanessa
AU - Zarco, Natanael
AU - Navarrete, Araceli
AU - Martínez-Maldonado, Alejandra
AU - Guadarrama-Ortíz, Parménides
AU - Villanueva-Fierro, Ignacio
AU - Ontiveros-Torres, Miguel Angel
AU - Perry, George
AU - Alonso, Alejandra D.
AU - Floran-Garduño, Benjamin
AU - Segovia, José
AU - Luna-Muñoz, José
AU - Avila, Jesus
N1 - Publisher Copyright:
© 2019 - IOS Press and the authors. All rights reserved.
PY - 2019
Y1 - 2019
N2 - It has been reported that the main function of tau protein is to stabilize microtubules and promote the movement of organelles through the axon in neurons. In Alzheimer's disease, tau protein is the major constituent of the paired helical filament, and it undergoes post-translational modifications including hyperphosphorylation and truncation. Whether other functions of tau protein are involved in Alzheimer's disease is less clear. We used SH-SY5Y human neuroblastoma cells as an in vitro model to further study the functions of tau protein. We detected phosphorylated tau protein as small dense dots in the cell nucleus, which strongly colocalize with intranuclear speckle structures that were also labelled with an antibody to SC35, a protein involved in nuclear RNA splicing. We have shown further that tau protein, phosphorylated at the sites recognized by pT231, TG-3, and AD2 antibodies, is closely associated with cell division. Different functions may be characteristic of phosphorylation at specific sites. Our findings suggest that the presence of tau protein is involved in separation of sister chromatids in anaphase, and that tau protein also participates in maintaining the integrity of the DNA (pT231, prophase) and chromosomes during cell division (TG-3).
AB - It has been reported that the main function of tau protein is to stabilize microtubules and promote the movement of organelles through the axon in neurons. In Alzheimer's disease, tau protein is the major constituent of the paired helical filament, and it undergoes post-translational modifications including hyperphosphorylation and truncation. Whether other functions of tau protein are involved in Alzheimer's disease is less clear. We used SH-SY5Y human neuroblastoma cells as an in vitro model to further study the functions of tau protein. We detected phosphorylated tau protein as small dense dots in the cell nucleus, which strongly colocalize with intranuclear speckle structures that were also labelled with an antibody to SC35, a protein involved in nuclear RNA splicing. We have shown further that tau protein, phosphorylated at the sites recognized by pT231, TG-3, and AD2 antibodies, is closely associated with cell division. Different functions may be characteristic of phosphorylation at specific sites. Our findings suggest that the presence of tau protein is involved in separation of sister chromatids in anaphase, and that tau protein also participates in maintaining the integrity of the DNA (pT231, prophase) and chromosomes during cell division (TG-3).
KW - Alzheimer's disease
KW - SC35
KW - SH-SY5Y
KW - cell cycle
KW - phospho-tau protein
KW - staurosporine
UR - http://www.scopus.com/inward/record.url?scp=85072565041&partnerID=8YFLogxK
U2 - 10.3233/JAD-190155
DO - 10.3233/JAD-190155
M3 - Artículo
C2 - 31424392
AN - SCOPUS:85072565041
SN - 1387-2877
VL - 71
SP - 631
EP - 645
JO - Journal of Alzheimer's Disease
JF - Journal of Alzheimer's Disease
IS - 2
ER -