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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
editNFκB 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
editReferences
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.