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

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

Stable Identifier

R-HSA-3814820

Type

Reaction [transition]

Species

Homo sapiens

Compartment

extracellular region

ReviewStatus

5/5

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

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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, Hébert, 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