What question did this study set out to answer?

Determine whether stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) phosphorylates recombinant tau protein at sites characteristically hyperphosphorylated in Alzheimer's disease.

April 1, 1997Journal of Neurochemistry

Stress‐Activated Protein Kinase/c‐Jun N‐Terminal Kinase Phosphorylates τ Protein

View Full Paper

Ask AI

Bookmark

Authors

CRC. Hugh ReynoldsAhmadu Bello University MUMichelle A. UttonGuy's Hospital GGGraham GibbBraemar (United Kingdom)

Discussion

Member takes

Implication

In vitro study demonstrates that c-Jun N-terminal kinase phosphorylates tau at pathological Alzheimer sites, suggesting cellular stress drives neurofibrillary tangle formation.

Key Points

Determine whether stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) phosphorylates recombinant tau protein at sites characteristically hyperphosphorylated in Alzheimer's disease.
Conducted in vitro phosphorylation assays using purified recombinant SAPK/JNK and recombinant human tau protein.
Identified targeted serine and threonine residues via Western blot analysis with phosphorylation-dependent tau antibodies, comparing phosphorylation profiles to glycogen synthase kinase-3 (GSK-3).
Recombinant SAPK/JNK phosphorylated recombinant tau protein on serine and threonine residues across both primary phosphorylated domains of tau.
Unlike GSK-3, which targeted physiological sites seen in fetal and adult tau, SAPK/JNK readily phosphorylated Thr205 and Ser422, epitopes hyperphosphorylated pathologically in Alzheimer's neurofibrillary tangles.

Cite This Study

Reynolds et al. (1997) studied this question.

synapsesocial.com/papers/6a83cdc54d653d38678ddc87 https://doi.org/10.1046/j.1471-4159.1997.68041736.x

View Full Paper

Ask AI

Bookmark

April 1, 1997Journal of Neurochemistry

Stress‐Activated Protein Kinase/c‐Jun N‐Terminal Kinase Phosphorylates τ Protein

View Full Paper

Ask AI

Bookmark

Authors

CRC. Hugh ReynoldsAhmadu Bello University MUMichelle A. UttonGuy's Hospital GGGraham GibbBraemar (United Kingdom)

Discussion

Member takes

Implication

In vitro study demonstrates that c-Jun N-terminal kinase phosphorylates tau at pathological Alzheimer sites, suggesting cellular stress drives neurofibrillary tangle formation.

Key Points

Determine whether stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) phosphorylates recombinant tau protein at sites characteristically hyperphosphorylated in Alzheimer's disease.
Conducted in vitro phosphorylation assays using purified recombinant SAPK/JNK and recombinant human tau protein.
Identified targeted serine and threonine residues via Western blot analysis with phosphorylation-dependent tau antibodies, comparing phosphorylation profiles to glycogen synthase kinase-3 (GSK-3).
Recombinant SAPK/JNK phosphorylated recombinant tau protein on serine and threonine residues across both primary phosphorylated domains of tau.
Unlike GSK-3, which targeted physiological sites seen in fetal and adult tau, SAPK/JNK readily phosphorylated Thr205 and Ser422, epitopes hyperphosphorylated pathologically in Alzheimer's neurofibrillary tangles.

Cite This Study

Reynolds et al. (1997) studied this question.

synapsesocial.com/papers/6a83cdc54d653d38678ddc87 https://doi.org/10.1046/j.1471-4159.1997.68041736.x

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark