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The Journal of Neuroscience, September 1, 1999, 19(17):7486-7494

cAMP-Dependent Protein Kinase Phosphorylations on Tau in Alzheimer's Disease

Gregory A. Jicha1, Charles Weaver2, Eric Lane1, Cintia Vianna1, Yvonne Kress1, Julia Rockwood1, and Peter Davies1, 2

Departments of 1 Pathology and 2 Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461

To elucidate the role cAMP-dependent protein kinase (PKA) phosphorylations on tau play in Alzheimer's disease, we have generated highly specific monoclonal antibodies, CP-3 and PG-5, which recognize the PKA-dependent phosphorylations of ser214 and ser409 in tau respectively. The present study demonstrates by immunohistochemical analysis, CP-3 and PG-5 immunoreactivity with neurofibrillary pathology in both early and advanced Alzheimer's disease, but not in normal brain tissue and demonstrates that cAMP-dependent protein kinase phosphorylations on tau precede or are coincident with the initial appearance of filamentous aggregates of tau. Studies using heat-stable preparations demonstrate that neither site appears to be phosphorylated to any appreciable extent in normal rodent or human brain. Further analysis demonstrates that the beta  catalytic subunit of PKA (Cbeta ), the beta  II regulatory subunit of PKA (RIIbeta ), and the 79 kDa A-kinase-anchoring-protein (AKAP79), are tightly associated with the neurofibrillary pathology, positioning cAMP-dependent protein kinase to participate directly in the pathological hyperphosphorylation of tau seen in Alzheimer's disease.

Key words: tau; Alzheimer's disease; protein kinase; cAMP; phosphorylation; neurofibrillary pathology

Copyright © 1999 Society for Neuroscience  0270-6474/99/19177486-09$05.00/0


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