A protein kinase associated with paired helical filaments in Alzheimer disease.
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.
Vincent
I J
IJ
Department of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461.
Davies
P
P
D000255:Adenosine Triphosphate / Q000378:metabolism; D000544:Alzheimer Disease / Q000201:enzymology*; D000911:Antibodies, Monoclonal; D002451:Cell Compartmentation; D006427:Hemin / Q000494:pharmacology; D007700:Kinetics; D008854:Microscopy, Electron; D016874:Neurofibrillary Tangles / Q000201:enzymology*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D016875:tau Proteins / Q000378:metabolism
D000911:Antibodies, Monoclonal; D010750:Phosphoproteins; D047428:Protein Kinase Inhibitors; D016875:tau Proteins; D006427:Hemin; D000255:Adenosine Triphosphate; D011494:Protein Kinases