Chondroitin sulfate proteoglycan form of cellular and cell-surface Alzheimer amyloid precursor.
The biological function of the amyloid precursor protein (APP) is still 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 present on the cell surface of C6 glioma cells. In addition, densitometric quantitation of Western blots showed that approximately 50% of the mature cell-associated full length APP is in the proteoglycan form. These findings suggest that the proteoglycan nature of APP may be important for the implementation of its biological function.
Shioi
J
J
Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029.
Refolo
L M
LM
Efthimiopoulos
S
S
Robakis
N K
NK
D016564:Amyloid beta-Protein Precursor / Q000276:immunology / Q000378:metabolism*; D015153:Blotting, Western; D002809:Chondroitin Sulfates / Q000276:immunology / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D005910:Glioma / Q000378:metabolism / Q000648:ultrastructure; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D008715:Methionine / Q000378:metabolism; D011233:Precipitin Tests; D011509:Proteoglycans / Q000276:immunology / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D016564:Amyloid beta-Protein Precursor; D006025:Glycosaminoglycans; D011509:Proteoglycans; D002809:Chondroitin Sulfates; D008715:Methionine; D003545:Cysteine