CHONDROITIN SULFATE PROTEOGLYCAN FORM OF CELLULAR AND CELL-SURFACE ALZHEIMER AMYLOID PRECURSOR

The biological function of the amyloid precursor protein (APP) is stil l not fully understood. Recently, we reported that secreted truncated APP occurs in a chondroitin sulfate proteoglycan form. Here we present evidence that full length APP-chondroitin sulfate proteoglycan is pre sent on the cell surface of C6 glioma cells. In addition, densitometri c quantitation of Western blots showed that approximately 50% of the m ature cell-associated full length APP is in the proteoglycan form. The se findings suggest that the proteoglycan nature of APP may be importa nt for the implementation of its biological function.