Collagen type XVIII endostatin release

Stable Identifier
Reaction [transition]
Homo sapiens
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Collagen type XVIII is a heparan sulfate proteoglycan associated with the basement membranes of almost all epithelia and endothelia. It has a large C-terminal noncollagenous domain. Mouse knockouts suggest that it may have a role in maintaining the structural integrity of the extracellular matrix (Utriainen et al. 2004).

Proteolytic cleavage of the C-terminal noncollagenous domain by matrix metalloproteinases (Heljasvaara et al. 2005) releases 18 to 38 kDa C-terminal proteolytic fragments, collectively named endostatin. They have anti-angiogenic activity (O'Reilly et al. 1997, Ständker et al. 1997) and suppress primary tumor and metastasis growth in experimental animal models (Ortega & Werb 2002). It is not clear whether this collagen subtype forms supramolecular assemblies (Myllyharju & Kivirikko, 2004) but thought likely, via a similar mechanism to the related collagen XV (Hurskainen et al. 2010).

Endostatin-like fragments are released from collagen type XVIII by MMP 7 (Lin et al. 2001), 3, 9, 12, 13 (Ferreras et al. 2000) and 20 (Heljasvaara et al. 2005). Several cathepsins and elastase can bring about endostatin release (Ferreras et al. 2000, Felbor et al. 2000).
Literature References
PubMed ID Title Journal Year
15950618 Generation of biologically active endostatin fragments from human collagen XVIII by distinct matrix metalloproteases

Sorsa, T, Rehn, M, Pihlajaniemi, T, Nyberg, P, Salo, T, Heikkilä, P, Heljasvaara, R, Parikka, M, Luostarinen, J

Exp Cell Res 2005
11119712 Generation and degradation of human endostatin proteins by various proteinases

Delaissé, J, Ferreras, M, Felbor, U, Lenhard, T, Olsen, BR

FEBS Lett. 2000
Catalyst Activity

serine-type endopeptidase activity of Endostatin-releasing proteases [extracellular region]

Orthologous Events
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