Reactome | Endorepellin is the 85-kDa C-terminal domain V of HSPG2 (per...

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created	[InstanceEdit:3814823] Jupe, S, 2013-07-08
dbId	3814824
displayName	Endorepellin is the 85-kDa C-terminal domain V of HSPG2 (per...
literatureReference	[LiteratureReference:3827969] Domain structure and organisation in extracellular matrix proteins [LiteratureReference:2396059] Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan [LiteratureReference:2396054] Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin [LiteratureReference:3828012] BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan [LiteratureReference:3828007] Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis
modified	[InstanceEdit:3827985] Jupe, S, 2013-07-09
schemaClass	Summation
text	Endorepellin is the 85-kDa C-terminal domain V of HSPG2 (perlecan). It consists of a series of laminin-like globular (LG) domains interconnected by short epidermal growth factor-like repeats (Hohenester & Engel 2002). Endorepellin has angiostatic activity (Mongiat et al. 2003) which is primarily localised in the LG3 domain (Bix et al. 2004). Bone morphogenetic protein 1 (BMP1), its isoform mammalian Tolloid (mTLD), mammalian Tolloid-like-1 and -2 (TLL1, TLL2) (Gonzalez et al. 2005) and cathepsin-L1 (Cailhier et al. 2008) can liberate LG3 by cleaving endorepellin between Asn4196 and Asp4197.

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