22 research outputs found
<b>A Ca<sup>2+</sup>-CALMODULIN-DEPENDENT PROTEIN KINASE IN THE PARTICULATE FRACTION OF RAT BRAIN AND ENDOGENOUS PHOSPHORYLATION OF PARTICULATE-BOUND SUBSTRATES</b>
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Increases in phosphorylation by Ca2+/calmodulin-dependent protein kinase II following hippocampal long-term potentiation
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Mitogen-Activated Protein Kinase Activation by Stimulation with Thyrotropin-Releasing Hormone in Rat Pituitary GH3 Cells1
No full text<b>Ca<sup>2+</sup>-CALMODULIN-DEPENDENT AND CYCLIC AMP-DEPENDENT PHOSPHORYLATION OF NEUROFILAMENTS AND GLIAL FIBRILLARY ACIDIC </b><b>PROTEIN</b>
No full text<b>ACTIVATION OF Ca<sup>2+</sup>/CALMODULIN-DEPENDENT PROTEIN KINASE II BY AUTOPHORYLATION: SPECIFIED SUBSTRATES ENHANCE THE KINASE ACTIVITY</b>
No full textInvolvement of p38 Mitogen-Activated Protein Kinase Activation in Bromocriptine-Induced Apoptosis in Rat Pituitary GH3 Cells1
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In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons
Get PDFAbstractUsing 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 (Ca1A) 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
