Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1997-12-10
|
pubmed:abstractText |
beta-Amyloid precursor protein (beta-APP), the source of the fibrillogenic amyloid beta-peptide (A beta) that accumulates in the brain of victims of Alzheimer's disease, is a multifunctional protein that is widely expressed in the nervous system. beta-Amyloid precursor protein is axonally transported and accumulates in presynaptic terminals and growth cones. A secreted form of beta-APP (sAPP alpha) is released from neurons in response to electrical activity and may function in modulation of neuronal excitability, synaptic plasticity, neurite outgrowth, synaptogenesis, and cell survival. A signaling pathway involving guanosine 3',5'-cyclic monophosphate is activated by sAPP alpha and modulates the activities of potassium channels, N-methyl-D-aspartate receptors, and the transcription factor NF kappa B. Additional functions of beta-APP may include modulation of cell adhesion and regulation of proliferation of nonneuronal cells. Alternative enzymatic processing of beta-APP liberates A beta, which has a propensity to form amyloid fibrils; A beta can damage and kill neurons and increase their vulnerability to excitotoxicity. The mechanism involves generation of oxyradicals and impairment of membrane transport systems (e.g., ion-motive ATPases and glutamate and glucose transporters). Genetic mutations or age-related metabolic changes may promote neuronal degeneration in Alzheimer's disease by increasing production of A beta and/or decreasing levels of neuroprotective sAPP alpha.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PSEN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PSEN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-2
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0031-9333
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
77
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1081-132
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:9354812-Alzheimer Disease,
pubmed-meshheading:9354812-Amyloid beta-Peptides,
pubmed-meshheading:9354812-Amyloid beta-Protein Precursor,
pubmed-meshheading:9354812-Animals,
pubmed-meshheading:9354812-Apolipoproteins E,
pubmed-meshheading:9354812-Humans,
pubmed-meshheading:9354812-Membrane Proteins,
pubmed-meshheading:9354812-Mutation,
pubmed-meshheading:9354812-Nervous System,
pubmed-meshheading:9354812-Neurites,
pubmed-meshheading:9354812-Neurons,
pubmed-meshheading:9354812-Presenilin-1,
pubmed-meshheading:9354812-Presenilin-2,
pubmed-meshheading:9354812-Protein Processing, Post-Translational,
pubmed-meshheading:9354812-Synapses
|
pubmed:year |
1997
|
pubmed:articleTitle |
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives.
|
pubmed:affiliation |
Sanders-Brown Research Center on Aging, Lexington, Kentucky, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|