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Volume 17, Number 3,
Issue of February 1, 1997
pp. 1004-1010
Copyright ©1997 Society for Neuroscience
Cell Surface Amyloid  -Protein Precursor Colocalizes with 1
Integrins at Substrate Contact Sites in Neural Cells
Received Aug. 19, 1996; revised Nov. 11, 1996; accepted Nov. 18, 1996.
Tsuneo Yamazaki1, 3,
Edward H. Koo2, 3, and
Dennis J. Selkoe1, 3
Departments of 1 Neurology and 2 Pathology,
Harvard Medical School, Boston, Massachusetts 02115, and
3 Center for Neurological Diseases, Brigham and Women's
Hospital, Boston, Massachusetts 02115
Amyloid  -protein (A), the principal constituent of the senile
plaques seen in Alzheimer's disease (AD), is derived by proteolysis from the -amyloid precursor protein (PP). The distribution and trafficking of cell surface PP are of particular interest because some of these molecules are direct precursors of secreted A and because the localization of PP at the cell surface may be related directly to its physiological functions. Recently, we reported that, in
cultured hippocampal neurons, cell surface PP is preferentially expressed on axons in a striking discontinuous pattern. In this study,
we describe the colocalization of cell surface PP and integrins in
primary cultured cells. In rat hippocampal neurons, cell surface PP
was colocalized selectively with  11 and 51 integrin
heterodimers at these characteristic segmental locations. In rat
cortical astrocytes, both cell surface PP and 1 integrin were
located at the cell periphery in the "spreading" stage shortly after plating. In "flattened" astrocytes cultured for several days,
PP was found in punctate deposits called point contacts. In these
sites, PP was colocalized with 11, but not with 51 integrin heterodimers, the latter of which were situated at focal contact sites. In both neurons and astrocytes examined after shearing, clathrin and -adaptin were colocalized with PP on the surface that directly contacts the substratum. These results are consistent with the putative role of PP in cell adhesion and suggests that PP either interacts with selected integrins or shares similar cellular machinery to promote cell adhesion.
Key words:
amyloid -protein precursor;
amyloid -protein;
integrins;
cell adhesion;
clathrin;
substrate attachment;
point
contacts
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