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.
Cailhier, JF, Iozzo, RV, Raymond, MA, Pshezhetsky, AV, Hébert, MJ, Laplante, P, Prat, A, Brassard, N, Sirois, I, Lepage, S
Zhang, Y, Iozzo, RV, Bix, G, Fu, J, Gonzalez, EM, Greenspan, DS, Gopalakrishnan, B, Reed, CC
serine-type endopeptidase activity of BMP1, TLL1, TLL2, Cathepsin L1 [extracellular region]
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