rACLF, a recombinant snake venom metalloprotease, activates endothelial cells in vitro

Autor(es)

C. K. De Moraes ^[1] ; M. Fritzen ^[2] ; A. M. Chudzinski-Tavassi ^[3] ; H. S. Selistre-de-Araújo ^[4]

Afiliação do(s) autor(es)

^[1] Federal University of São Carlos. Department of Physiological Sciences - Brasil

^[2] Butantan Institute. Laboratory of Biochemistry and Biophysics - Brasil

^[3] Butantan Institute. Laboratory of Biochemistry and Biophysics - Brasil

^[4] Federal University of São Carlos. Department of Physiological Sciences - Brasil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Venomous Animals and Toxins including Tropical Diseases; v. 14, n. 1, p. 113-127, 2008-00-00.

Resumo

Snake venom metalloproteases (SVMPs) comprise a family of snake venom toxins responsible for most of local and systemic effects observed during envenomation by snakes from the Viperidae family. The vascular system and more specifically the endothelium seem to be the preferential targets of these proteins. This work describes the effects of rACLF, a recombinant SVMP from Agkistrodon contortrix laticinctus on human umbilical vein endothelial cells (HUVECs) in vitro. Our results showed that rACLF activates HUVECs by the release of mediators involved in inflammation and hemostasis such as prostacyclin and interleukin-8. We also demonstrated that rACLF increased the expression of ICAM-I and decay accelerating factor (DAF). Moreover, rACLF protects the HUVECs against apoptosis induced by serum deprivation. These results suggest that the endothelial cell activation induced by SVMPs may have a significant role in the development of the local inflammatory lesion observed in Viperidae envenomation. (AU)

• Processo FAPESP: 02/08043-6 - Estudo da atividade proteolítica da ACLF, uma metaloprotease recombinante, sobre componentes da matriz extracelular e expressão gênica
• Beneficiário: Caroline Krieger de Moraes
• Modalidade de apoio: Bolsas no Brasil - Doutorado