Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-10-2
pubmed:abstractText
An epitope-specific antibody directed against the first 16 amino acids of the beta amyloid protein (anti-BP16) immunoprecipitated the secreted form of the amyloid precursor protein (APP) from the conditioned medium of PC12 cells. This antibody caused neurite retraction in differentiated PC12 cells and inhibited cell-substratum adhesion in many neuronal and non-neuronal cell types. The inhibitory effect of anti-BP16 was abolished by preabsorption of the antibody with BP16 peptide. Antibodies directed against other domains of APP did not inhibit cell adhesion. The secreted form of APP may be important for cell adhesion in many different mammalian cell types.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
An antibody to beta amyloid and the amyloid precursor protein inhibits cell-substratum adhesion in many mammalian cell types.
pubmed:affiliation
Department of Neurology, Harvard Medical School, Boston, MA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't