Vertebrate Secretory (RNase A) Ribonucleases and Host Defense
作者： Helene F. Rosenberg
DOI: 10.1007/978-3-642-21078-5_2
关键词:
摘要: Bovine pancreatic ribonuclease, also known as RNase A, is the prototype of an extensive, multi-lineage family vertebrate secretory proteins that share elements structure and catalytic activity despite substantial functional divergence. In this review, we feature A its members are implicated in promoting host defense – activities include sustaining mucosal barriers, well participating various aspects innate acquired immunity explore relationships linking gene evolution, enzymatic activity, physiologic function.
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Shida Yousefi, Jeffrey A Gold, Nicola Andina, James J Lee, Ann M Kelly, Evelyne Kozlowski, Inès Schmid, Alex Straumann, Janine Reichenbach, Gerald J Gleich, Hans-Uwe Simon, Catapult-like release of mitochondrial DNA by eosinophils contributes to antibacterial defense Nature Medicine. ,vol. 14, pp. 949- 953 ,(2008) , 10.1038/NM.1855
Dalia Maor, Michael R. Mardiney, Paul B. Chretien, ALTERATION OF HUMAN SERUM RIBONUCLEASE ACTIVITY IN MALIGNANCY CRC critical reviews in clinical laboratory sciences. ,vol. 10, pp. 89- 111 ,(1979) , 10.3109/10408367909149733
Jianzhi Zhang, Kimberly D Dyer, Helene F Rosenberg, Human RNase 7: a new cationic ribonuclease of the RNase A superfamily Nucleic Acids Research. ,vol. 31, pp. 602- 607 ,(2003) , 10.1093/NAR/GKG157
G.W. Welling, G.Leijenaar-Van Den Berg, B. Van Dijk, A. Van Den Berg, G. Groen, W. Gaastra, M. Emmens, J.J. Beintema, Evolution of mammalian pancreatic ribonucleases Biosystems. ,vol. 6, pp. 239- 245 ,(1975) , 10.1016/0303-2647(75)90067-2
De Yang, Helene F. Rosenberg, Qian Chen, Kimberly D. Dyer, Kahori Kurosaka, Joost J. Oppenheim, Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells Blood. ,vol. 102, pp. 3396- 3403 ,(2003) , 10.1182/BLOOD-2003-01-0151
Marc Torrent, Beatriz G. de la Torre, Victòria M. Nogués, David Andreu, Ester Boix, Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment. Biochemical Journal. ,vol. 421, pp. 425- 434 ,(2009) , 10.1042/BJ20082330
G J Gleich, D A Loegering, Immunobiology of Eosinophils Annual Review of Immunology. ,vol. 2, pp. 429- 459 ,(1984) , 10.1146/ANNUREV.IY.02.040184.002241
L R Pease, R L Barker, D A Loegering, R M Ten, K J Hamann, G J Gleich, Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. Journal of Immunology. ,vol. 143, pp. 952- 955 ,(1989)
Tara L. Garvey, Kimberly D. Dyer, John A. Ellis, Cynthia A. Bonville, Barbara Foster, Calman Prussin, Andrew J. Easton, Joseph B. Domachowske, Helene F. Rosenberg, Inflammatory Responses to Pneumovirus Infection in IFN-αβR Gene-Deleted Mice Journal of Immunology. ,vol. 175, pp. 4735- 4744 ,(2005) , 10.4049/JIMMUNOL.175.7.4735
Soochin Cho, Jianzhi Zhang, Zebrafish Ribonucleases Are Bactericidal: Implications for the Origin of the Vertebrate RNase A Superfamily Molecular Biology and Evolution. ,vol. 24, pp. 1259- 1268 ,(2007) , 10.1093/MOLBEV/MSM047