Cellular signaling pathways and cytoskeletal organization.
We describe a possible mechanism by which the amyloid precursor protein (APP) may be linked to the intraneuronal pathology of Alzheimer's disease (AD). Extracellular proteolytic products of APP may directly or indirectly transduce signals to cells under normal as well as pathological conditions. This activity appears to reside in the cysteine-rich amino terminus of APP. How APP or its metabolic products may affect the phosphorylation of tau is considered.
Kosik
K S
KS
Harvard Medical School, Department of Neurology, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA.
Qiu
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WQ
Greenberg
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S
D000595:Amino Acid Sequence; D016564:Amyloid beta-Protein Precursor / Q000235:genetics / Q000502:physiology*; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000502:physiology; D003599:Cytoskeleton / Q000648:ultrastructure*; D006801:Humans; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases; D008969:Molecular Sequence Data; D009474:Neurons / Q000502:physiology*; D010766:Phosphorylation; D012333:RNA, Messenger / Q000235:genetics; D015398:Signal Transduction; D016875:tau Proteins / Q000378:metabolism
D016564:Amyloid beta-Protein Precursor; D012333:RNA, Messenger; D016875:tau Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases