NSA9, a human prothrombin kringle-2-derived peptide, acts as an inhibitor of kringle-2-induced activation in EOC2 microglia. BMB reports [BMB Rep] Journal article | | Title | NSA9, a human prothrombin kringle-2-derived peptide, acts as an inhibitor of kringle-2-induced activation in EOC2 microglia. | | Author(s) | Kim JY, Kim TH, Kim SS | | Institution | Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea kimss518@yonsei.ac.kr. | | Source | BMB Rep 2009 Jun 30; 42(6):380-6. | | Abstract | In neurodegenerative diseases, such as Alzheimerapostrophes and Parkinsonapostrophes, microglial cell activation is thought to contribute to CNS injury by producing neurotoxic compounds. Prothrombin and kringle-2 increase levels of NO and the mRNA expression of iNOS, IL-1beta, and TNF-alpha in microglial cells. In contrast, the human prothrombin kringle-2 derived peptide NSA9 inhibits NO release and the production of pro-inflammatory cytokines such as IL-1beta, TNF-alpha, and IL-6 in LPS-activated EOC2 microglia. In this study, we investigated the anti-inflammatory effects of NSA9 in human prothrombin- and kringle-2-stimulated EOC2 microglia. Treatment with 20-100 muM of NSA9 attenuated both prothrombin- and kringle-2-induced microglial activation. NO production induced by MAPKs and NF-kappaB was similarly reduced by inhibitors of ERK (PD98059), p38 (SB203580), NF-kappaB (N-acetylcysteine), and NSA9. These results suggest that NSA9 acts independently as an inhibitor of microglial activation and that its effects in EOC2 microglia are not influenced by the presence of kringle-2. [BMB reports 2009; 42(6): 380-386]. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 19558798 |
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