Abstract
We have identified a protein kinase in immunoaffinity-purified preparations of paired helical filaments from brain tissue of individuals with Alzheimer disease. The kinase phosphorylates the filament proteins in vitro in a manner independent of second messenger regulation or of modulation by heparin and polyamines. Physiological concentrations of hemin, an oxidized heme porphyrin, inhibit the kinase and abolish Alz-50 immunoreactivity of the proteins. Since paired helical filaments are composed of hyperphosphorylated proteins, association of a protein kinase with the filaments provides a mechanism for abnormal processing of the proteins in disease.
MeSH Terms
Adenosine Triphosphate/metabolism
Alzheimer Disease/enzymology
Antibodies, Monoclonal
Cell Compartmentation
Hemin/pharmacology
Kinetics
Microscopy, Electron
Neurofibrillary Tangles/enzymology
Phosphoproteins/metabolism
Phosphorylation
Protein Kinase Inhibitors
Protein Kinases/metabolism
Substrate Specificity
tau Proteins/metabolism
Chemicals
Antibodies, Monoclonal
Phosphoproteins
Protein Kinase Inhibitors
tau Proteins
Hemin
Adenosine Triphosphate
Protein Kinases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Vincent I J
Department of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461.
Davies P
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