scholarly journals Inhibition of Glycosphingolipid Biosynthesis Reduces Secretion of the β-Amyloid Precursor Protein and Amyloid β-Peptide

2005 ◽  
Vol 280 (30) ◽  
pp. 28110-28117 ◽  
Author(s):  
Irfan Y. Tamboli ◽  
Kai Prager ◽  
Esther Barth ◽  
Michael Heneka ◽  
Konrad Sandhoff ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Amyloid Β Peptide ◽  
Β Amyloid ◽  
Glycosphingolipid Biosynthesis

Normal Cellular Processing of the β-Amyloid Precursor Protein Results in the Secretion of the Amyloid β Peptide and Related Moleculesa

1993 ◽  
Vol 695 (1) ◽  
pp. 109-116 ◽  
Author(s):  
CHRISTIAN HAASS ◽  
ALBERT Y. HUNG ◽  
MICHAEL G. SCHLOSSMACHER ◽  
TILMAN OLTERSDORF ◽  
DAVID B. TEPLOW ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Amyloid Β Peptide ◽  
Cellular Processing ◽  
Β Amyloid

scholarly journals Caffeine Stimulates Amyloid β-Peptide Release from β-Amyloid Precursor Protein-Transfected HEK293 Cells

1997 ◽  
Vol 69 (4) ◽  
pp. 1580-1591 ◽  
Author(s):  
Henry W. Querfurth ◽  
Jinwei Jiang ◽  
Jonathan D. Geiger ◽  
Dennis J. Selkoe
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Hek293 Cells ◽  
Amyloid Β Peptide ◽  
Peptide Release ◽  
Β Amyloid

scholarly journals Novel β-Secretase Cleavage of β-Amyloid Precursor Protein in the Endoplasmic Reticulum/Intermediate Compartment of NT2N Cells

1997 ◽  
Vol 138 (3) ◽  
pp. 671-680 ◽  
Author(s):  
Abraham S.C. Chyung ◽  
Barry D. Greenberg ◽  
David G. Cook ◽  
Robert W. Doms ◽  
Virginia M.-Y. Lee
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Neuronal Cell ◽  
Brefeldin A ◽  
Precursor Protein ◽  
Embryonal Carcinoma Cell ◽  
Amyloid Β Peptide ◽  
Wild Type ◽  
Intermediate Compartment ◽  
Β Amyloid

Previous studies have demonstrated that NT2N neurons derived from a human embryonal carcinoma cell line (NT2) constitutively process the endogenous wild-type β-amyloid precursor protein (APP) to amyloid β peptide in an intracellular compartment. These studies indicate that other proteolytic fragments generated by intracellular processing must also be present in these cells. Here we show that the NH2-terminal fragment of APP generated by β-secretase cleavage (APPβ) is indeed produced from the endogenous full length APP (APPFL). Pulse–chase studies demonstrated a precursor–product relationship between APPFL and APPβ as well as intracellular and secreted APPβ fragments. In addition, trypsin digestion of intact NT2N cells at 4°C did not abolish APPβ recovered from the cell lysates. Furthermore, the production of intracellular APPβ from wild-type APP appears to be a unique characteristic of postmitotic neurons, since intracellular APPβ was not detected in several non-neuronal cell lines. Significantly, production of APPβ occurred even when APP was retained in the ER/ intermediate compartment by inhibition with brefeldin A, incubation at 15°C, or by expression of exogenous APP bearing the dilysine ER retrieval motif.

scholarly journals Modulation of Secreted β-Amyloid Precursor Protein and Amyloid β-Peptide in Brain by Cholesterol

1998 ◽  
Vol 273 (26) ◽  
pp. 16576-16582 ◽  
Author(s):  
David S. Howland ◽  
Stephen P. Trusko ◽  
Mary J. Savage ◽  
Andrew G. Reaume ◽  
Diane M. Lang ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Amyloid Β Peptide ◽  
Β Amyloid
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