Draft:Regnase-1
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- Comment: This article is too short to give the reader an understanding of the topic. To start, it does not state what regnase-1 is, simply how it was found. Also, the cited sources appear to be primary research, not yet validated by other studies, so, per WP:MEDRS, these are not acceptable sources. WikiDan61ChatMe!ReadMe!! 19:46, 29 January 2024 (UTC)
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Regnase-1 (MCPIP-1, ZC3H12A) is a protien that was first discovered in human peripheral blood monocytes treated the chemotactic protein MCP-1[1]. The protein contains an N-terminal domain, a PilT N-terminus like (PIN) domain, a zinc finger domain, a ubiquitin domain and a C-terminal domain. Two emerging functions of this protein include RNase-cleaving activity (PIN domain) and the control of ubiquitination. Regnase-1 also has implications in cell differentiation, apoptosis, and regulating inflammation[2].
Regulation of inflammation[edit]
NFκB is well known to induce proinflammatory cytokines. Pattern recognition receptors (PRRs) induce NFκB activation via mechanisms that utilize ubiquitylation of RIP1 and TRAF6. Recent studies have shown that Regnase-1 disrupts this ubiquitylation thereby blocking activation of NFκB and its downstream cytokines[3].
Regulation of apoptosis[edit]
References[edit]
- ^ Zhou, L; Azfer, A; Niu, J; Graham, S; Choudhury, M; Adamski, F; Younce, C; Binkley, P; Kolattukudy, PE (2006). "Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction". Circ Res. 98 (9): 1177–85. doi:10.1161/01.RES.0000220106.64661.71. PMC 1523425. PMID 16574901.
- ^ Jin, Z; Zheng, E; Sareli, C; Kolattukudy, PE; Niu, J (2021). "Monocyte Chemotactic Protein-Induced Protein 1 (MCPIP-1): A Key Player of Host Defense and Immune Regulation". Front Immunol. 12: 727–861. doi:10.3389/fimmu.2021.727861. PMC 8519509. PMID 34659213.
- ^ Liang, J; Saad, Y; Lei, T; Wang, J; Qi, D; Yang, Q; Kolattukudy, PE; Fu, M (2010). "MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling". J Exp Med. 207 (13): 2959–73. doi:10.1084/jem.20092641. PMC 3005225. PMID 21115689.