CELLULAR PROCESSING AND PROTEOGLYCAN NATURE OF AMYLOID PRECURSOR PROTEINS

被引：4

作者：

ROBAKIS, NK ^{[1
]}

VASSILACOPOULOU, D ^{[1
]}

EFTHIMIOPOULOS, S ^{[1
]}

SAMBAMURTI, K ^{[1
]}

REFOLO, LM ^{[1
]}

SHIOI, J ^{[1
]}

机构：

[1] CUNY MT SINAI SCH MED,FISHBERG RES CTR NEUROBIOL,NEW YORK,NY 10029

来源：

ALZHEIMERS DISEASE: AMYLOID PRECUSOR PROTEINS, SIGNAL TRANSDUCTION, AND NEURONAL TRANSPLANTATION | 1993年 / 695卷

关键词：

D O I：

10.1111/j.1749-6632.1993.tb23041.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Amyloid beta protein (beta/A(4) or A beta), the main proteinaceous component ofthe amyloid depositions ofthe Alzheimer's brain, derives from the proteolytic processing of the amyloid precursor protein (APP). Cleavage of the amyloid precursor by at least two distinct secretase activities produces soluble secreted APP. The major secretase cleavage (site I) takes place between A beta 16 and 17, while the minor cleavage (site II) takes place after A beta Lys 28 and may produce potentially amyloidogenic secreted APP. Full-length cellular APP is cleaved by secretase intracellularly in the Trans-Golgi Network (TGN) or in post-Golgi vesicles. The resultant soluble APP is transported to the plasma membrane and exocytosed. The biological activity of the APP is still not completely understood, although it seems to act as a cell adhesion molecule. Recent studies have shown that in glioma cells, most of the soluble secreted APP occurs as a chondroitin sulfate proteoglycan (CSPG). In addition, full length APP CSPG has been detected in neuroblastoma and fibroblast cells as well as on the surface of glioma cells, and in human brain. These results suggest that the proteoglycan nature of the APP proteins may be important for their biological function.

引用

页码：132 / 138

页数：7

共 22 条

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