Linked Life Data

7929215

Source:http://linkedlifedata.com/resource/pubmed/id/7929215

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1994-11-17
pubmed:abstractText
A beta is a 39-43-amino acid peptide that accumulates as extracellular aggregates in Alzheimer's disease-afflicted brain tissue. Contact between these aggregates and neurons is potentially pathogenic, although little is known about the cellular transduction mechanisms. We have investigated the impact of A beta aggregates on the neuronal control of protein tyrosine phosphorylation, which underlies signal transduction for multiple families of growth factor and adhesion receptors. Added to cultures of rat and human nerve cell lines, A beta aggregates evoked a non-desensitizing increase (1.3-3.6-fold) in tyrosine phosphorylation in a band at 118 kDa. The 118-kDa protein was determined by immunoprecipitation to be pp125FAK, not previously documented in cells of neuronal lineage. Immunoblots with anti-focal adhesion kinase (FAK) showed that A beta aggregates had no effect on FAK protein levels. The increase in FAK tyrosine phosphorylation occurred at doses of A beta aggregates that evoked lactate dehydrogenase release; evoked tyrosine phosphorylation preceded the first detectable lactate dehydrogenase release by 4 h. Like degeneration, the FAK response was dependent on A beta aggregation and neuronal differentiation. Since tyrosine phosphorylation of FAK is essential to its activity as a transduction component of integrin-, peptide-, and lysophosphatidic acid-mediated signaling, the data establish a link between A beta aggregates and signal transduction pathways implicated in diverse cell functions including neurite outgrowth, control of the cell cycle, and apoptosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25247-50
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:7929215-Amino Acid Sequence, pubmed-meshheading:7929215-Amyloid beta-Peptides, pubmed-meshheading:7929215-Animals, pubmed-meshheading:7929215-Cell Adhesion Molecules, pubmed-meshheading:7929215-Dose-Response Relationship, Drug, pubmed-meshheading:7929215-Focal Adhesion Kinase 1, pubmed-meshheading:7929215-Focal Adhesion Protein-Tyrosine Kinases, pubmed-meshheading:7929215-Hippocampus, pubmed-meshheading:7929215-Humans, pubmed-meshheading:7929215-Molecular Sequence Data, pubmed-meshheading:7929215-Neurons, pubmed-meshheading:7929215-Peptide Fragments, pubmed-meshheading:7929215-Phosphorylation, pubmed-meshheading:7929215-Protein-Tyrosine Kinases, pubmed-meshheading:7929215-Rats, pubmed-meshheading:7929215-Signal Transduction, pubmed-meshheading:7929215-Tumor Cells, Cultured, pubmed-meshheading:7929215-Tyrosine
pubmed:year
1994
pubmed:articleTitle
Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide.
pubmed:affiliation
Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't