HSPG2 (perlecan) is cleaved by BMP1, TLL1, TLL2, Cathepsin L1

Stable Identifier
Reaction [transition]
Homo sapiens
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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.

Literature References
PubMed ID Title Journal Year
18658137 Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis

Cailhier, JF, Iozzo, RV, Raymond, MA, Pshezhetsky, AV, H├ębert, MJ, Laplante, P, Prat, A, Brassard, N, Sirois, I, Lepage, S

J. Biol. Chem. 2008
15591058 BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan

Zhang, Y, Iozzo, RV, Bix, G, Fu, J, Gonzalez, EM, Greenspan, DS, Gopalakrishnan, B, Reed, CC

J. Biol. Chem. 2005
Catalyst Activity

serine-type endopeptidase activity of BMP1, TLL1, TLL2, Cathepsin L1 [extracellular region]

Orthologous Events
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