AGRN binds Beta amyloid fibril via GAG chains

Stable Identifier
R-HSA-2467665
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Several agrin (AGRN) ligands require the presence of heparan-sulfate GAG sidechains and probably represent interactions with them. Extracellular ligands include Beta-amyloid (Donahue et al. 1999, Cotman et al. 2000). Other ligands (unconfirmed in humans) include alpha-synuclein fibrils (chicken - Liu et al. 2005), HB-GAM/pleiotropin (Dagget et al. 1996), thrombospondin and FGF2 (Cotman et al. 1999).
Literature References
PubMed ID Title Journal Year
10339611 Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma

Rafii, MS, Glass, DJ, Berzin, TM, Donahue, JE, Yancopoulos, GD, Stopa, EG, Fallon, JR

Proc. Natl. Acad. Sci. U.S.A. 1999
10673326 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain

Halfter, W, Cotman, SL, Cole, GJ

Mol. Cell. Neurosci. 2000
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!