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

Junichi Shioi; Lawrence M. Refolo; Spiros Efthimiopoulos; Nikolaos K. Robakis

doi:10.1016/0304-3940(93)90186-O

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

Junichi Shioi, Lawrence M. Refolo, Spiros Efthimiopoulos, Nikolaos K. Robakis

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

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.

Original language	English
Pages (from-to)	121-124
Number of pages	4
Journal	Neuroscience Letters
Volume	154
Issue number	1-2
DOIs	https://doi.org/10.1016/0304-3940(93)90186-O
State	Published - 14 May 1993

Keywords

Alzheimer's amyloid precursor
C6 cell
Cell surface
Proteoglycan

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10.1016/0304-3940(93)90186-O

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title = "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.",

keywords = "Alzheimer's amyloid precursor, C6 cell, Cell surface, Proteoglycan",

author = "Junichi Shioi and Refolo, \{Lawrence M.\} and Spiros Efthimiopoulos and Robakis, \{Nikolaos K.\}",

note = "Funding Information: We thank Drs. James A. Ripellino, Kumar Sam-bamurti and Menelaos Pangalos for useful suggestions. Supported by NIH Grants AGO8200 and AGO5138.",

year = "1993",

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doi = "10.1016/0304-3940(93)90186-O",

language = "English",

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T1 - Chondroitin sulfate proteoglycan form of cellular and cell-surface Alzheimer amyloid precursor

AU - Shioi, Junichi

AU - Refolo, Lawrence M.

AU - Efthimiopoulos, Spiros

AU - Robakis, Nikolaos K.

N1 - Funding Information: We thank Drs. James A. Ripellino, Kumar Sam-bamurti and Menelaos Pangalos for useful suggestions. Supported by NIH Grants AGO8200 and AGO5138.

PY - 1993/5/14

Y1 - 1993/5/14

N2 - 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.

AB - 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.

KW - Alzheimer's amyloid precursor

KW - C6 cell

KW - Cell surface

KW - Proteoglycan

UR - https://www.scopus.com/pages/publications/0027319004

U2 - 10.1016/0304-3940(93)90186-O

DO - 10.1016/0304-3940(93)90186-O

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AN - SCOPUS:0027319004

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VL - 154

SP - 121

EP - 124

JO - Neuroscience Letters

JF - Neuroscience Letters

IS - 1-2

ER -

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

Abstract

Keywords

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