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Ribonuclease L

December 15, 2023

Ribonuclease L or RNase L (for latent), known sometimes as ribonuclease 4 or 2'-5' oligoadenylate synthetase-dependent ribonuclease, is an interferon (IFN)-induced ribonuclease which, upon activation, destroys all RNA within the cell (both cellular and viral). RNase L is an enzyme that in humans is encoded by the RNASEL gene.[5]

RNASEL
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRNASEL, PRCA1, RNS4, ribonuclease L
External IDsOMIM: 180435 MGI: 1098272 HomoloGene: 8040 GeneCards: RNASEL
Orthologs
SpeciesHumanMouse
Entrez

6041

24014

Ensembl

ENSG00000135828

ENSMUSG00000066800

UniProt

Q05823

Q05921

RefSeq (mRNA)

NM_021133

NM_011882

RefSeq (protein)

NP_066956

NP_036012

Location (UCSC)Chr 1: 182.57 – 182.59 MbChr 1: 153.63 – 153.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

This gene encodes a component of the interferon-regulated 2'-5'oligoadenylate (2'-5'A) system that functions in the antiviral and antiproliferative roles of interferons. RNase L is activated by dimerization, which occurs upon 2'-5'A binding, and results in cleavage of all RNA in the cell. This can lead to activation of MDA5, an RNA helicase involved in the production of interferons.

Synthesis and activation edit

 
RNase L activation pathway-IFN factors bind the receptor and lead transcription and modifications of OAS. Viral dsRNA binds OAS, so that 2'-5'A is produced leading to the dimerization of RNase L. Activated RNase L cleaves all RNA in the cell, which can activate MDA5 leading to interferon production.

RNase L is present in very minute quantities during the normal cell cycle. When interferon binds to cell receptors, it activates transcription of around 300 genes to bring about the antiviral state. Among the enzymes produced is RNase L, which is initially in an inactive form. A set of transcribed genes codes for 2'-5' Oligoadenylate Synthetase (OAS).[6] The transcribed RNA is then spliced and modified in the nucleus before reaching the cytoplasm and being translated into an inactive form of OAS. The location of OAS in the cell and the length of the 2'-5' oligoadenylate depends on the post-transcriptional and post-translational modifications of OAS.[6]

OAS is only activated under a viral infection, when a tight binding of the inactive form of the protein with a viral dsRNA, consisting of the retrovirus' ssRNA and its complementary strand, takes place. Once active, OAS converts ATP to pyrophosphate and 2'-5'-linked oligoadenylates (2-5A), which are 5' end phosphorylated.[7] 2-5 A molecules then bind to RNase L, promoting its activation by dimerization. In its activated form RNase L cleaves all RNA molecules in the cell leading to autophagy and apoptosis. Some of the resulting RNA fragments can also further induce the production of IFN-β as noted in the Significance section.[8]

This dimerization and activation of RNase L can be recognized using Fluorescence Resonance Energy Transfer (FRET), as oligoribonucleotides containing a quencher and a fluorophore on opposite sites are added to a solution with inactive RNase L. The FRET signal is then recorded as the quencher and the fluorophore are very close to each other. Upon the addition of 2-5A molecules, RNase L becomes active, cleaving the oligoribonucleotides and interfering in the FRET signal.[9]

In vitro, RNase L can be inhibited by curcumin.[10]

Significance edit

RNase L is part of the body's innate immune defense, namely the antiviral state of the cell. When a cell is in the antiviral state, it is highly resistant to viral attacks and is also ready to undergo apoptosis upon successful viral infection. Degradation of all RNA within the cell (which usually occurs with cessation of translation activity caused by protein kinase R) is the cell's last stand against a virus before it attempts apoptosis.

Interferon beta (IFN-β), a type I interferon responsible for antiviral activity, is induced by RNase L and melanoma differentiation-associated protein 5 (MDA5) in the infected cell. The relationship between RNase L and MDA5 in the production of IFNs has been confirmed with siRNA tests silencing the expression of either molecule and noting a marked decline in IFN production.[11] MDA5, an RNA helicase, is known to be activated by complex high molecular weight dsRNA transcribed from the viral genome.[11][12] In a cell with RNase L, MDA5 activity may be further enhanced.[11] When active, RNase L cleaves and identifies viral RNA and feeds it into MDA5 activation sites, enhancing the production of IFN-β. The RNA fragments produced by RNase L have double stranded regions, as well as specific markers, that allow them to be identified by the RNase L and MDA5.[8] Some studies have suggested that high levels of RNase L may actually inhibit IFN-β production, but a clear linkage still exists between RNase L activity and IFN-β production.[8]

Furthermore, it has been shown that RNase L is involved in many diseases. In 2002, the "hereditary prostate cancer 1" locus (HPC1) was mapped to the RNASEL gene, indicating that mutations in this gene cause a predisposition to prostate cancer.[13][14][15] Impairments of the OAS/RNase L pathway in chronic fatigue syndrome (CFS) have been investigated.[16][17]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135828 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000066800 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Squire J, Zhou A, Hassel BA, Nie H, Silverman RH (January 1994). "Localization of the interferon-induced, 2-5A-dependent RNase gene (RNS4) to human chromosome 1q25". Genomics. 19 (1): 174–5. doi:10.1006/geno.1994.1033. PMID 7514564.
  6. ^ a b Sarkar SN, Pandey M, Sen GC (2005). "Assays for the Interferon-Induced Enzyme 2′,5′ Oligoadenylate Synthetases". Interferon Methods and Protocols. Methods in Molecular Medicine. Vol. 116. Human Press Inc. pp. 81–101. doi:10.1385/1-59259-939-7:081. ISBN 978-1-58829-418-0. PMID 16000856.
  7. ^ Liang SL, Quirk D, Zhou A (September 2006). "RNase L: its biological roles and regulation". IUBMB Life. 58 (9): 508–14. doi:10.1080/15216540600838232. PMID 17002978.
  8. ^ a b c Banerjee S, Chakrabarti A, Jha BK, Weiss SR, Silverman RH (February 2014). "Cell-type-specific effects of RNase L on viral induction of beta interferon". mBio. 5 (2): e00856-14. doi:10.1128/mBio.00856-14. PMC 3940032. PMID 24570368.
  9. ^ Thakur CS, Xu Z, Wang Z, Novince Z, Silverman RH (2005). "A Convenient and Sensitive Fluorescence Resonance Energy Transfer Assay for RNase L and 2′,5′ Oligoadenylates". Interferon Methods and Protocols. Methods in Molecular Medicine. Vol. 116. Human Press Inc. pp. 103–13. doi:10.1385/1-59259-939-7:103. ISBN 978-1-58829-418-0. PMID 16000857.
  10. ^ Gupta A, Rath PC (2014). "Curcumin, a natural antioxidant, acts as a noncompetitive inhibitor of human RNase L in presence of its cofactor 2-5A in vitro". BioMed Research International. 2014: 817024. doi:10.1155/2014/817024. PMC 4165196. PMID 25254215.
  11. ^ a b c Luthra P, Sun D, Silverman RH, He B (February 2011). "Activation of IFN-β expression by a viral mRNA through RNase L and MDA5". Proceedings of the National Academy of Sciences of the United States of America. 108 (5): 2118–23. Bibcode:2011PNAS..108.2118L. doi:10.1073/pnas.1012409108. PMC 3033319. PMID 21245317.
  12. ^ Pichlmair A, Schulz O, Tan CP, Rehwinkel J, Kato H, Takeuchi O, et al. (October 2009). "Activation of MDA5 requires higher-order RNA structures generated during virus infection". Journal of Virology. 83 (20): 10761–9. doi:10.1128/JVI.00770-09. PMC 2753146. PMID 19656871.
  13. ^ Smith JR, Freije D, Carpten J, Gronberg H, Xu J, Isaacs S, et al. (Nov 1996). "Major susceptibility locus for prostate cancer on chromosome 1 suggested by a genome-wide search". Science. 274 (5291): 1371–4. Bibcode:1996Sci...274.1371S. doi:10.1126/science.274.5291.1371. PMID 8910276. S2CID 42684655.
  14. ^ "Entrez Gene: RNASEL ribonuclease L (2',5'-oligoisoadenylate synthetase-dependent)".
  15. ^ Carpten J, Nupponen N, Isaacs S, Sood R, Robbins C, Xu J, et al. (February 2002). "Germline mutations in the ribonuclease L gene in families showing linkage with HPC1". Nature Genetics. 30 (2): 181–4. doi:10.1038/ng823. PMID 11799394. S2CID 2922306.
  16. ^ Nijs J, De Meirleir K (Nov–Dec 2005). "Impairments of the 2-5A synthetase/RNase L pathway in chronic fatigue syndrome". In Vivo. 19 (6): 1013–21. PMID 16277015.
  17. ^ Suhadolnik RJ, Peterson DL, O'Brien K, Cheney PR, Herst CV, Reichenbach NL, et al. (July 1997). "Biochemical evidence for a novel low molecular weight 2-5A-dependent RNase L in chronic fatigue syndrome". Journal of Interferon & Cytokine Research. 17 (7): 377–85. doi:10.1089/jir.1997.17.377. PMID 9243369.

Further reading edit

  • Urisman A, Molinaro RJ, Fischer N, Plummer SJ, Casey G, Klein EA, et al. (March 2006). "Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant". PLOS Pathogens. 2 (3): e25. doi:10.1371/journal.ppat.0020025. PMC 1434790. PMID 16609730.
  • Chakrabarti A, Jha BK, Silverman RH (January 2011). "New insights into the role of RNase L in innate immunity". Journal of Interferon & Cytokine Research. 31 (1): 49–57. doi:10.1089/jir.2010.0120. PMC 3021357. PMID 21190483.
  • Castelli J, Wood KA, Youle RJ (1999). "The 2-5A system in viral infection and apoptosis". Biomedicine & Pharmacotherapy. 52 (9): 386–90. doi:10.1016/S0753-3322(99)80006-7. PMID 9856285.
  • Leaman DW, Cramer H (July 1999). "Controlling gene expression with 2-5A antisense". Methods. 18 (3): 252–65. doi:10.1006/meth.1999.0782. PMID 10454983.
  • Silverman RH (February 2003). "Implications for RNase L in prostate cancer biology". Biochemistry. 42 (7): 1805–12. doi:10.1021/bi027147i. PMID 12590567.
  • Kieffer N, Schmitz M, Scheiden R, Nathan M, Faber JC (2006). "Involvement of the RNAse L gene in prostate cancer". Bulletin de la Société des Sciences Médicales du Grand-Duché de Luxembourg (1): 21–8. PMID 16869093.
  • Bisbal C, Silverman RH (2007). "Diverse functions of RNase L and implications in pathology". Biochimie. 89 (6–7): 789–98. doi:10.1016/j.biochi.2007.02.006. PMC 2706398. PMID 17400356.
  • Carter BS, Beaty TH, Steinberg GD, Childs B, Walsh PC (April 1992). "Mendelian inheritance of familial prostate cancer". Proceedings of the National Academy of Sciences of the United States of America. 89 (8): 3367–71. Bibcode:1992PNAS...89.3367C. doi:10.1073/pnas.89.8.3367. PMC 48868. PMID 1565627.
  • Dong B, Xu L, Zhou A, Hassel BA, Lee X, Torrence PF, Silverman RH (May 1994). "Intrinsic molecular activities of the interferon-induced 2-5A-dependent RNase". The Journal of Biological Chemistry. 269 (19): 14153–8. doi:10.1016/S0021-9258(17)36767-4. PMID 7514601.
  • Bisbal C, Martinand C, Silhol M, Lebleu B, Salehzada T (June 1995). "Cloning and characterization of a RNAse L inhibitor. A new component of the interferon-regulated 2-5A pathway". The Journal of Biological Chemistry. 270 (22): 13308–17. doi:10.1074/jbc.270.22.13308. PMID 7539425.
  • Zhou A, Hassel BA, Silverman RH (March 1993). "Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action". Cell. 72 (5): 753–65. doi:10.1016/0092-8674(93)90403-D. PMID 7680958.
  • Hassel BA, Zhou A, Sotomayor C, Maran A, Silverman RH (August 1993). "A dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon". The EMBO Journal. 12 (8): 3297–304. doi:10.1002/j.1460-2075.1993.tb05999.x. PMC 413597. PMID 7688298.
  • Smith JR, Freije D, Carpten JD, Grönberg H, Xu J, Isaacs SD, et al. (November 1996). "Major susceptibility locus for prostate cancer on chromosome 1 suggested by a genome-wide search". Science. 274 (5291): 1371–4. Bibcode:1996Sci...274.1371S. doi:10.1126/science.274.5291.1371. PMID 8910276. S2CID 42684655.
  • Egesten A, Dyer KD, Batten D, Domachowske JB, Rosenberg HF (October 1997). "Ribonucleases and host defense: identification, localization and gene expression in adherent monocytes in vitro". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1358 (3): 255–60. doi:10.1016/S0167-4889(97)00081-5. PMID 9366257.
  • Eeles RA, Durocher F, Edwards S, Teare D, Badzioch M, Hamoudi R, et al. (March 1998). "Linkage analysis of chromosome 1q markers in 136 prostate cancer families. The Cancer Research Campaign/British Prostate Group U.K. Familial Prostate Cancer Study Collaborators". American Journal of Human Genetics. 62 (3): 653–8. doi:10.1086/301745. PMC 1376940. PMID 9497242.
  • Dong B, Silverman RH (January 1999). "Alternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase L". Nucleic Acids Research. 27 (2): 439–45. doi:10.1093/nar/27.2.439. PMC 148198. PMID 9862963.
  • Carpten JD, Makalowska I, Robbins CM, Scott N, Sood R, Connors TD, et al. (February 2000). "A 6-Mb high-resolution physical and transcription map encompassing the hereditary prostate cancer 1 (HPC1) region". Genomics. 64 (1): 1–14. doi:10.1006/geno.1999.6051. PMID 10708513.
  • Zhou A, Nie H, Silverman RH (November 2000). "Analysis and origins of the human and mouse RNase L genes: mediators of interferon action". Mammalian Genome. 11 (11): 989–92. doi:10.1007/s003350010194. PMID 11063255. S2CID 35650613.
  • Dong B, Niwa M, Walter P, Silverman RH (March 2001). "Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p". RNA. 7 (3): 361–73. doi:10.1017/S1355838201002230. PMC 1370093. PMID 11333017.

External links edit

December 15, 2023
ribonuclease, rnase, latent, known, sometimes, ribonuclease, oligoadenylate, synthetase, dependent, ribonuclease, interferon, induced, ribonuclease, which, upon, activation, destroys, within, cell, both, cellular, viral, rnase, enzyme, that, humans, encoded, r. Ribonuclease L or RNase L for latent known sometimes as ribonuclease 4 or 2 5 oligoadenylate synthetase dependent ribonuclease is an interferon IFN induced ribonuclease which upon activation destroys all RNA within the cell both cellular and viral RNase L is an enzyme that in humans is encoded by the RNASEL gene 5 RNASELAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1WDY 4G8K 4G8L 4OAU 4OAVIdentifiersAliasesRNASEL PRCA1 RNS4 ribonuclease LExternal IDsOMIM 180435 MGI 1098272 HomoloGene 8040 GeneCards RNASELGene location Human Chr Chromosome 1 human 1 Band1q25 3Start182 573 634 bp 1 End182 589 256 bp 1 Gene location Mouse Chr Chromosome 1 mouse 2 Band1 1 G3Start153 625 172 bp 2 End153 639 967 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inamniotic fluidpalpebral conjunctivagerminal epitheliumbloodvisceral pleurajejunal mucosaparietal pleurabronchial epithelial cellseminal vesiculacorpus epididymisTop expressed inleft colonileumintestinal villusjejunumbloodduodenumganglionic eminencePaneth cellmedial ganglionic eminencegastric mucosaMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding protein kinase activity rRNA binding metal ion binding endoribonuclease activity ribonuclease activity protein binding RNA binding nuclease activity ribonucleoprotein complex binding endonuclease activity hydrolase activity ATP binding identical protein bindingCellular componentcytoplasm cytosol nuclear matrix mitochondrial matrix mitochondrion cellular componentBiological processregulation of mRNA stability nucleic acid phosphodiester bond hydrolysis mRNA processing protein phosphorylation negative regulation of viral genome replication RNA phosphodiester bond hydrolysis defense response to virus type I interferon signaling pathway rRNA processing fat cell differentiation positive regulation of transcription by RNA polymerase II RNA phosphodiester bond hydrolysis endonucleolytic regulation of type I interferon mediated signaling pathway positive regulation of glucose importSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez604124014EnsemblENSG00000135828ENSMUSG00000066800UniProtQ05823Q05921RefSeq mRNA NM 021133NM 011882RefSeq protein NP 066956NP 036012Location UCSC Chr 1 182 57 182 59 MbChr 1 153 63 153 64 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThis gene encodes a component of the interferon regulated 2 5 oligoadenylate 2 5 A system that functions in the antiviral and antiproliferative roles of interferons RNase L is activated by dimerization which occurs upon 2 5 A binding and results in cleavage of all RNA in the cell This can lead to activation of MDA5 an RNA helicase involved in the production of interferons Contents 1 Synthesis and activation 2 Significance 3 References 4 Further reading 5 External linksSynthesis and activation edit nbsp RNase L activation pathway IFN factors bind the receptor and lead transcription and modifications of OAS Viral dsRNA binds OAS so that 2 5 A is produced leading to the dimerization of RNase L Activated RNase L cleaves all RNA in the cell which can activate MDA5 leading to interferon production RNase L is present in very minute quantities during the normal cell cycle When interferon binds to cell receptors it activates transcription of around 300 genes to bring about the antiviral state Among the enzymes produced is RNase L which is initially in an inactive form A set of transcribed genes codes for 2 5 Oligoadenylate Synthetase OAS 6 The transcribed RNA is then spliced and modified in the nucleus before reaching the cytoplasm and being translated into an inactive form of OAS The location of OAS in the cell and the length of the 2 5 oligoadenylate depends on the post transcriptional and post translational modifications of OAS 6 OAS is only activated under a viral infection when a tight binding of the inactive form of the protein with a viral dsRNA consisting of the retrovirus ssRNA and its complementary strand takes place Once active OAS converts ATP to pyrophosphate and 2 5 linked oligoadenylates 2 5A which are 5 end phosphorylated 7 2 5 A molecules then bind to RNase L promoting its activation by dimerization In its activated form RNase L cleaves all RNA molecules in the cell leading to autophagy and apoptosis Some of the resulting RNA fragments can also further induce the production of IFN b as noted in the Significance section 8 This dimerization and activation of RNase L can be recognized using Fluorescence Resonance Energy Transfer FRET as oligoribonucleotides containing a quencher and a fluorophore on opposite sites are added to a solution with inactive RNase L The FRET signal is then recorded as the quencher and the fluorophore are very close to each other Upon the addition of 2 5A molecules RNase L becomes active cleaving the oligoribonucleotides and interfering in the FRET signal 9 In vitro RNase L can be inhibited by curcumin 10 Significance editRNase L is part of the body s innate immune defense namely the antiviral state of the cell When a cell is in the antiviral state it is highly resistant to viral attacks and is also ready to undergo apoptosis upon successful viral infection Degradation of all RNA within the cell which usually occurs with cessation of translation activity caused by protein kinase R is the cell s last stand against a virus before it attempts apoptosis Interferon beta IFN b a type I interferon responsible for antiviral activity is induced by RNase L and melanoma differentiation associated protein 5 MDA5 in the infected cell The relationship between RNase L and MDA5 in the production of IFNs has been confirmed with siRNA tests silencing the expression of either molecule and noting a marked decline in IFN production 11 MDA5 an RNA helicase is known to be activated by complex high molecular weight dsRNA transcribed from the viral genome 11 12 In a cell with RNase L MDA5 activity may be further enhanced 11 When active RNase L cleaves and identifies viral RNA and feeds it into MDA5 activation sites enhancing the production of IFN b The RNA fragments produced by RNase L have double stranded regions as well as specific markers that allow them to be identified by the RNase L and MDA5 8 Some studies have suggested that high levels of RNase L may actually inhibit IFN b production but a clear linkage still exists between RNase L activity and IFN b production 8 Furthermore it has been shown that RNase L is involved in many diseases In 2002 the hereditary prostate cancer 1 locus HPC1 was mapped to the RNASEL gene indicating that mutations in this gene cause a predisposition to prostate cancer 13 14 15 Impairments of the OAS RNase L pathway in chronic fatigue syndrome CFS have been investigated 16 17 References edit a b c GRCh38 Ensembl release 89 ENSG00000135828 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000066800 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Squire J Zhou A Hassel BA Nie H Silverman RH January 1994 Localization of the interferon induced 2 5A dependent RNase gene RNS4 to human chromosome 1q25 Genomics 19 1 174 5 doi 10 1006 geno 1994 1033 PMID 7514564 a b Sarkar SN Pandey M Sen GC 2005 Assays for the Interferon Induced Enzyme 2 5 Oligoadenylate Synthetases Interferon Methods and Protocols Methods in Molecular Medicine Vol 116 Human Press Inc pp 81 101 doi 10 1385 1 59259 939 7 081 ISBN 978 1 58829 418 0 PMID 16000856 Liang SL Quirk D Zhou A September 2006 RNase L its biological roles and regulation IUBMB Life 58 9 508 14 doi 10 1080 15216540600838232 PMID 17002978 a b c Banerjee S Chakrabarti A Jha BK Weiss SR Silverman RH February 2014 Cell type specific effects of RNase L on viral induction of beta interferon mBio 5 2 e00856 14 doi 10 1128 mBio 00856 14 PMC 3940032 PMID 24570368 Thakur CS Xu Z Wang Z Novince Z Silverman RH 2005 A Convenient and Sensitive Fluorescence Resonance Energy Transfer Assay for RNase L and 2 5 Oligoadenylates Interferon Methods and Protocols Methods in Molecular Medicine Vol 116 Human Press Inc pp 103 13 doi 10 1385 1 59259 939 7 103 ISBN 978 1 58829 418 0 PMID 16000857 Gupta A Rath PC 2014 Curcumin a natural antioxidant acts as a noncompetitive inhibitor of human RNase L in presence of its cofactor 2 5A in vitro BioMed Research International 2014 817024 doi 10 1155 2014 817024 PMC 4165196 PMID 25254215 a b c Luthra P Sun D Silverman RH He B February 2011 Activation of IFN b expression by a viral mRNA through RNase L and MDA5 Proceedings of the National Academy of Sciences of the United States of America 108 5 2118 23 Bibcode 2011PNAS 108 2118L doi 10 1073 pnas 1012409108 PMC 3033319 PMID 21245317 Pichlmair A Schulz O Tan CP Rehwinkel J Kato H Takeuchi O et al October 2009 Activation of MDA5 requires higher order RNA structures generated during virus infection Journal of Virology 83 20 10761 9 doi 10 1128 JVI 00770 09 PMC 2753146 PMID 19656871 Smith JR Freije D Carpten J Gronberg H Xu J Isaacs S et al Nov 1996 Major susceptibility locus for prostate cancer on chromosome 1 suggested by a genome wide search Science 274 5291 1371 4 Bibcode 1996Sci 274 1371S doi 10 1126 science 274 5291 1371 PMID 8910276 S2CID 42684655 Entrez Gene RNASEL ribonuclease L 2 5 oligoisoadenylate synthetase dependent Carpten J Nupponen N Isaacs S Sood R Robbins C Xu J et al February 2002 Germline mutations in the ribonuclease L gene in families showing linkage with HPC1 Nature Genetics 30 2 181 4 doi 10 1038 ng823 PMID 11799394 S2CID 2922306 Nijs J De Meirleir K Nov Dec 2005 Impairments of the 2 5A synthetase RNase L pathway in chronic fatigue syndrome In Vivo 19 6 1013 21 PMID 16277015 Suhadolnik RJ Peterson DL O Brien K Cheney PR Herst CV Reichenbach NL et al July 1997 Biochemical evidence for a novel low molecular weight 2 5A dependent RNase L in chronic fatigue syndrome Journal of Interferon amp Cytokine Research 17 7 377 85 doi 10 1089 jir 1997 17 377 PMID 9243369 Further reading editUrisman A Molinaro RJ Fischer N Plummer SJ Casey G Klein EA et al March 2006 Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant PLOS Pathogens 2 3 e25 doi 10 1371 journal ppat 0020025 PMC 1434790 PMID 16609730 Chakrabarti A Jha BK Silverman RH January 2011 New insights into the role of RNase L in innate immunity Journal of Interferon amp Cytokine Research 31 1 49 57 doi 10 1089 jir 2010 0120 PMC 3021357 PMID 21190483 Castelli J Wood KA Youle RJ 1999 The 2 5A system in viral infection and apoptosis Biomedicine amp Pharmacotherapy 52 9 386 90 doi 10 1016 S0753 3322 99 80006 7 PMID 9856285 Leaman DW Cramer H July 1999 Controlling gene expression with 2 5A antisense Methods 18 3 252 65 doi 10 1006 meth 1999 0782 PMID 10454983 Silverman RH February 2003 Implications for RNase L in prostate cancer biology Biochemistry 42 7 1805 12 doi 10 1021 bi027147i PMID 12590567 Kieffer N Schmitz M Scheiden R Nathan M Faber JC 2006 Involvement of the RNAse L gene in prostate cancer Bulletin de la Societe des Sciences Medicales du Grand Duche de Luxembourg 1 21 8 PMID 16869093 Bisbal C Silverman RH 2007 Diverse functions of RNase L and implications in pathology Biochimie 89 6 7 789 98 doi 10 1016 j biochi 2007 02 006 PMC 2706398 PMID 17400356 Carter BS Beaty TH Steinberg GD Childs B Walsh PC April 1992 Mendelian inheritance of familial prostate cancer Proceedings of the National Academy of Sciences of the United States of America 89 8 3367 71 Bibcode 1992PNAS 89 3367C doi 10 1073 pnas 89 8 3367 PMC 48868 PMID 1565627 Dong B Xu L Zhou A Hassel BA Lee X Torrence PF Silverman RH May 1994 Intrinsic molecular activities of the interferon induced 2 5A dependent RNase The Journal of Biological Chemistry 269 19 14153 8 doi 10 1016 S0021 9258 17 36767 4 PMID 7514601 Bisbal C Martinand C Silhol M Lebleu B Salehzada T June 1995 Cloning and characterization of a RNAse L inhibitor A new component of the interferon regulated 2 5A pathway The Journal of Biological Chemistry 270 22 13308 17 doi 10 1074 jbc 270 22 13308 PMID 7539425 Zhou A Hassel BA Silverman RH March 1993 Expression cloning of 2 5A dependent RNAase a uniquely regulated mediator of interferon action Cell 72 5 753 65 doi 10 1016 0092 8674 93 90403 D PMID 7680958 Hassel BA Zhou A Sotomayor C Maran A Silverman RH August 1993 A dominant negative mutant of 2 5A dependent RNase suppresses antiproliferative and antiviral effects of interferon The EMBO Journal 12 8 3297 304 doi 10 1002 j 1460 2075 1993 tb05999 x PMC 413597 PMID 7688298 Smith JR Freije D Carpten JD Gronberg H Xu J Isaacs SD et al November 1996 Major susceptibility locus for prostate cancer on chromosome 1 suggested by a genome wide search Science 274 5291 1371 4 Bibcode 1996Sci 274 1371S doi 10 1126 science 274 5291 1371 PMID 8910276 S2CID 42684655 Egesten A Dyer KD Batten D Domachowske JB Rosenberg HF October 1997 Ribonucleases and host defense identification localization and gene expression in adherent monocytes in vitro Biochimica et Biophysica Acta BBA Molecular Cell Research 1358 3 255 60 doi 10 1016 S0167 4889 97 00081 5 PMID 9366257 Eeles RA Durocher F Edwards S Teare D Badzioch M Hamoudi R et al March 1998 Linkage analysis of chromosome 1q markers in 136 prostate cancer families The Cancer Research Campaign British Prostate Group U K Familial Prostate Cancer Study Collaborators American Journal of Human Genetics 62 3 653 8 doi 10 1086 301745 PMC 1376940 PMID 9497242 Dong B Silverman RH January 1999 Alternative function of a protein kinase homology domain in 2 5 oligoadenylate dependent RNase L Nucleic Acids Research 27 2 439 45 doi 10 1093 nar 27 2 439 PMC 148198 PMID 9862963 Carpten JD Makalowska I Robbins CM Scott N Sood R Connors TD et al February 2000 A 6 Mb high resolution physical and transcription map encompassing the hereditary prostate cancer 1 HPC1 region Genomics 64 1 1 14 doi 10 1006 geno 1999 6051 PMID 10708513 Zhou A Nie H Silverman RH November 2000 Analysis and origins of the human and mouse RNase L genes mediators of interferon action Mammalian Genome 11 11 989 92 doi 10 1007 s003350010194 PMID 11063255 S2CID 35650613 Dong B Niwa M Walter P Silverman RH March 2001 Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p RNA 7 3 361 73 doi 10 1017 S1355838201002230 PMC 1370093 PMID 11333017 External links editribonuclease L human at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Ribonuclease L amp oldid 1186804788, wikipedia, wiki, book, books, library,

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