Myxoma viral serpin, Serp-1, inhibits human monocyte adhesion through regulation of actin-binding protein filamin B.
Serp-1 is a secreted myxoma viral serine protease inhibitor (serpin) with proven, highly effective, anti-inflammatory defensive activity during host cell infection, as well as potent immunomodulatory activity in a wide range of animal disease models. Serp-1 binds urokinase-type plasminogen activator (uPA) and the tissue-type PA, plasmin, and factor Xa, requiring uPA receptor (uPAR) for anti-inflammatory activity. To define Serp-1-mediated effects on inflammatory cell activation, we examined the association of Serp-1 with monocytes and T cells, effects on cellular migration, and the role of uPAR-linked integrins and actin-binding proteins in Serp-1 cellular responses. Our results show that Serp-1 associates directly with activated monocytes and T lymphocytes, in part through interaction with uPAR (P
Published In/Presented At
Viswanathan, K., Richardson, J., Togonu-Bickersteth, B., Dai, E., Liu, L., Vatsya, P., Sun, Y. M., Yu, J., Munuswamy-Ramanujam, G., Baker, H., & Lucas, A. R. (2009). Myxoma viral serpin, Serp-1, inhibits human monocyte adhesion through regulation of actin-binding protein filamin B. Journal of leukocyte biology, 85(3), 418–426. https://doi.org/10.1189/jlb.0808506
Medicine and Health Sciences
Department of Medicine