Abstract:
:Using antibodies recognizing the phosphorylation state of specific sites, phosphorylation states of tau were monitored in fetal rat primary cultured neurons. When cultured neurons were treated with okadaic acid (OA) or calyculin A (CalA) at concentrations sufficient to inhibit protein phosphatase 2A (PP2A), phosphorylation of Ser-199/Ser-202 (numbered according to the human tau 441) and Ser-235 increased. On the other hand, treatment with Ca2+ ionophore, A23187, induced dephosphorylation of Ser-199/Ser-202, Thr-205, Ser-396 and Ser-404, and this dephosphorylation was repressed by inhibitors of protein phosphatase 2B (PP2B), cyclosporin A and FK506. These results indicate that PP2A and PP2B are differentially involved in dephosphorylation of tau in neurons.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Saito T,Ishiguro K,Uchida T,Miyamoto E,Kishimoto T,Hisanaga Sdoi
10.1016/0014-5793(95)01292-0subject
Has Abstractpub_date
1995-12-04 00:00:00pages
238-42issue
3eissn
0014-5793issn
1873-3468pii
0014579395012920journal_volume
376pub_type
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