Release of endostatin-like peptides

Stable Identifier
R-HSA-2213200
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Collagens XV and XVIII are basement membrane associated collagens that can be cleaved to generate the antiangiogenic peptides restin (endostatin-XV) and endostatin (endostatin-XVIII), respectively (O'Reilly et al. 1997, Ramachandran et al. 1997, Sasaki et al. 2000). Endostatin fragments of differing molecular size (14-30 kDa) have been identified in vivo. Furthermore the C-terminal domains of several other collagens (IV, VIII, XIX) have anti-angiogenic and anti-tumoral activities (Ricard-Blum & Ballut 2011). Several proteases are able to generate endostatin from collagen XVIII including MMP-3, -7, -9, -13 and -20 and cathepsins B, V, S and L (Heljasvaara et al. 2005, Ma et al. 2007, Veillard et al. 2011). Endostatin inhibits proliferation of endothelial cells, angiogenesis and tumor growth in vivo (O'Reilly et al. 1997).

Literature References
PubMed ID Title Journal Year
9008168 Endostatin: an endogenous inhibitor of angiogenesis and tumor growth

O'Reilly, MS, Boehm, T, Shing, Y, Fukai, N, Vasios, G, Lane, WS, Flynn, E, Birkhead, JR, Olsen, BR, Folkman, J

Cell 1997
10966814 Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity

Sasaki, T, Larsson, H, Tisi, D, Claesson-Welsh, L, Hohenester, E, Timpl, R

J Mol Biol 2000
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
endopeptidase activity of Endostatin releasing proteases [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
Cite Us!