Chondroitin sulfate proteoglycan form of cellular and cell-surface Alzheimer amyloid precursor.

Abstract

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.

• Authors: J Shioi, L M Refolo, S Efthimiopoulos, N K Robakis
• Journal: Neuroscience letters (Neurosci Lett) Vol. 154 Issue 1-2 Pg. 121-4 (May 14 1993) ISSN: 0304-3940 [Print] Ireland
• PMID: 8361624 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Amyloid beta-Protein Precursor
• Glycosaminoglycans
• Proteoglycans
• Chondroitin Sulfates
• Methionine
• Cysteine

Topics

• Amyloid beta-Protein Precursor (immunology, metabolism)
• Blotting, Western
• Chondroitin Sulfates (immunology, metabolism)
• Cysteine (metabolism)
• Glioma (metabolism, ultrastructure)
• Glycosaminoglycans (metabolism)
• Humans
• Methionine (metabolism)
• Precipitin Tests
• Proteoglycans (immunology, metabolism)
• Tumor Cells, Cultured