atrolysin A

contains zinc; consider also other atrolysin records

Also Known As:

Crotalus atrox alpha-proteinase; Crotalus atrox metalloproteinase; Crotalus atrox protease; Ht-a proteolytic toxin; hemorrhagic proteinase (Crotalus)

Networked: 2 relevant articles (0 outcomes, 0 trials/studies)

1.	Osteosarcoma (Osteogenic Sarcoma) 10/01/2005 - "The cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A was shown to inhibit collagen-stimulated platelet aggregation and to interact with MG-63 osteosarcoma cells via integrin alpha2beta1 to inhibit adhesion to collagen I. In addition, we demonstrate by solid-phase binding assays that atrolysin A binds to collagen I and to vWF (von Willebrand factor) via exosites in the cysteine-rich domain. "
2.	Hemorrhage 09/01/2007 - "These included collagen VI, fibronectin, fibulin 2 and annexin V. Of particular interest was the observation of collagen VI and annexin V in that the release of these substrates could play a role in altering hemostasis and promote hemorrhage caused by the more typical actions of atrolysin A. "

1.	Collagen
2.	Metalloproteases (Metalloproteinases)
3.	Integrin alpha2beta1
4.	Annexin A5
5.	von Willebrand Factor
6.	Fibronectins (Fibronectin)
7.	Cysteine (L-Cysteine)
8.	fibulin 2