Fibulin‐1 binds the amino‐terminal head of β‐amyloid precursor protein and modulates its physiological function

@article{Ohsawa2001Fibulin1BT,
  title={Fibulin‐1 binds the amino‐terminal head of $\beta$‐amyloid precursor protein and modulates its physiological function},
  author={Ikuroh Ohsawa and Chizuko Takamura and Shinichi Kohsaka},
  journal={Journal of Neurochemistry},
  year={2001},
  volume={76}
}
Genetic studies have implicated amyloid precursor protein (APP) in the pathogenesis of Alzheimer's disease. While accumulating lines of evidence indicate that APP has various functions in cells, little is known about the proteins that modulate its biological activity. Toward this end, we employed a two‐hybrid system to identify potential interacting factors. We now report that fibulin‐1, which contains repetitive Ca2+‐binding EGF‐like elements, binds to APP at its amino‐terminal growth factor… 
Identification of a novel amyloid precursor protein processing pathway that generates secreted N‐terminal fragments
  • L. VellaR. Cappai
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2012
TLDR
SH‐SY5Y studies indicate the generation of APP NTFs involves a novel APP processing pathway, regulated by protein kinase C, but independent of α‐ secretase or β‐secretase 1 (BACE) activity.
The Amyloid Precursor Protein Represses Expression of Acetylcholinesterase in Neuronal Cell Lines*
TLDR
Whether APP is involved in the regulation of acetylcholinesterase (AChE), which is a key protein of the cholinergic system and has been shown to accelerate amyloid fibril formation and increase their toxicity, is examined and regulated in two neuronal cell lines by APP in a manner independent of the generation of sAPPα, sAPPβ, and AICD.
Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo*
TLDR
It is demonstrated that meprin β is a physiologically relevant enzyme in APP processing, and n-terminal APP fragments were in the range of those responsible for caspase-induced neurodegeneration, and cytotoxicity to primary neurons treated by these fragments was not detected.
The Collagen Chaperone HSP47 Is a New Interactor of APP that Affects the Levels of Extracellular Beta-Amyloid Peptides
TLDR
HSP47 is unveiled as a new functional interactor of APP and imply it as a potential target for preventing the formation and/or growth amyloid plaques.
Identification of a Region of β-Amyloid Precursor Protein Essential for Its Gelatinase A Inhibitory Activity*
TLDR
The decapeptide region of APP is likely an active site-directed inhibitor that has high selectivity toward gelatinase A and the complex formation was prevented completely by a hydroxamate-based synthetic inhibitor.
The biological role of the Alzheimer amyloid precursor protein in epithelial cells
TLDR
An overview on the functions of sAPP as an epithelial growth factor is presented and it is suggested that Proliferation and migration are known to be part of complex processes such as wound healing which, therefore, might be facilitated by the growth factor function of s APP.
The amyloid precursor protein and postnatal neurogenesis/neuroregeneration.
Identification of Amino Acid Residues of the Matrix Metalloproteinase-2 Essential for Its Selective Inhibition by β-Amyloid Precursor Protein-derived Inhibitor*
TLDR
It is speculated that the direction of interaction makes the active site-bound APP-IP resistant to cleavage, thereby supporting the inhibitory action of the peptide inhibitor.
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TLDR
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