Endorepellin binds alpha2beta1 integrin

Stable Identifier
Reaction [binding]
Homo sapiens
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Endorepellin is the C-terminal domain V of perlecan, constituting amino acids 3687–4391 (Mongiat et al. 2004). It has anti-angiogenic properties, blocking endothelial cell adhesion to fibronectin and type I collagen (Mongiat et al. 2003). Endorepellin and a smaller fragement constituting the third laminin G–like (LG) domain (LG3) disrupts actin stress fibers and focal adhesions via an interaction with the collagen receptor alpha2beta1 integrin (Bix et al. 2004). Laminin G domains 1 and 2 of endorepellin bind specifically and with high affinity to Ig domains 3–5 of VEGFR2 (Willis et al. 2013).

Literature References
PubMed ID Title Journal Year
15240572 Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin

Bix, G, Fu, J, Gonzalez, EM, Macro, L, Barker, A, Campbell, S, Zutter, MM, Santoro, SA, Kim, JK, Höök, M, Reed, CC, Iozzo, RV

J. Cell Biol. 2004
Participant Of
Orthologous Events
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