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Beta amyloid precursor protein mediates neuronal cell‐cell and cell‐surface adhesion
Author(s) -
Breen K. C.,
Bruce M.,
Anderton B. H.
Publication year - 1991
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490280109
Subject(s) - neural cell adhesion molecule , cell adhesion molecule , neurite , cell adhesion , microbiology and biotechnology , fibronectin , laminin , l1 , cell , amyloid precursor protein , cell–cell interaction , adhesion , chemistry , extracellular matrix , biology , biochemistry , alzheimer's disease , in vitro , pathology , disease , medicine , gene , organic chemistry
The beta‐amyloid precursor protein (APP) is a membrane‐bound glycoprotein which has been proposed to play a role both as a growth factor and a mediator of cell adhesion. Using the Ncuro‐2A neuroblastonia cell line, we have investigated the capacity of APP to mediate neural cell adhesion. The cells express the protein at a high level, the immunohistochemical staining pattern at the level of the membrane having a punctate pattern. Fab' fragments of antibodies to the extracellular portion of the molecule were found to inhibit cell binding to a collagen substrate, but not to laminin, fibronectin, or poly‐I‐lysine. Fab' fragments of antibodies to the nerve cell adhesion molecule N‐CAM also inhibited binding of Neuro‐2A cells specifically to collagen. This inhibition of cell‐surface binding was accompanied by a repression of neurite outgrowth in differentiating cells in the presence of antibodies. APP antibodies also inhibited neuron‐neuron and neuron‐glial binding, but not glial‐glial cell adhesion. These data suggest that the APP, which is expressed primarily on differentiated neuronal cells, may play a role in the mediation of both cell‐cell and cell‐substrate adhesion.