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Cross‐linking of β‐amyloid protein precursor catalysed by tissue transglutaminase
Author(s) -
Ho Gilbert J.,
Gregory Eugene J.,
Smirnova Irina V.,
Zoubine Mikhail N.,
Festoff Barry W.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00663-6
Subject(s) - senile plaques , tissue transglutaminase , amyloid precursor protein , synapse , chemistry , p3 peptide , extracellular , neuroscience , alzheimer's disease , biochemistry of alzheimer's disease , amyloid (mycology) , microbiology and biotechnology , biochemistry , biology , enzyme , pathology , disease , medicine , inorganic chemistry
Alzheimer's disease is characterized by progressive dementia, cortical atrophy with synaptic loss, and the accumulation of neurofibrillary tangles and senile plaques containing β‐amyloid. The β‐amyloid protein precursor (β‐APP), may normally be involved in cell adhesion related to synaptic maintenance. Loss of synapses correlates with dementia, suggesting that synaptic deficits may underlie the disease. Synapse stability may depend on the action of tissue transglutaminase (tTG), an enzyme capable of crosslinking large, multi‐domain extracellular glycoproteins, that is active and present at synapses. We now show that β‐APP is a substrate for tTG in vitro that results in dimers and multimers by silver staining and immunoblotting. This novel post‐translational modification suggests further roles for β‐APP in synaptic function as well as in Alzheimer's disease.