Aspirin′s active metabolite salicylic acid targets high mobility group box 1 to modulate inflammatory responses

Molecular Medicine

Volumn 21, Issue , 2015, Pages 526-535

  Choi, Hyong Woo ^a   Tian, Miaoying ^a,f   Song, Fei ^b   Venereau, Emilie ^d   Preti, Alessandro ^d   Park, Sang Wook ^a,g   Hamilton, Keith ^b   Swapna, G V T ^b   Manohar, Murli ^a   Moreau, Magali ^a   Agresti, Alessandra ^d   Gorzanelli, Andrea ^d   De Marchis, Francesco ^d   Wang, Huang ^b   Antonyak, Marc ^e   Micikas, Robert J ^a   Gentile, Daniel R ^a,h   Cerione, Richard A ^e   Schroeder, Frank C ^a   Montelione, Gaetano T ^b,c   Bianchi, Marco E ^d   Klessig, Daniel F ^a   more..

^a Boyce Thompson Institute for Plant Research   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^d VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^e Department of Obstetrics Gynecology   (United States)

^f UNIVERSITY OF HAWAII   (United States)

^g AUBURN UNIVERSITY   (United States)

^h UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOOXYGENASE 2; HIGH MOBILITY GROUP B1 PROTEIN; SALICYLIC ACID; SALICYLIC ACID DERIVATIVE; ACETYLSALICYLIC ACID;

3T3 CELL LINE; ANIMAL CELL; ARTICLE; BINDING SITE; CHEMOTAXIS; CONTROLLED STUDY; DRUG POTENCY; DRUG TARGETING; HELA CELL LINE; HUMAN; HUMAN CELL; INFLAMMATION; MOLECULAR CLONING; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INDUCTION; PROTEIN PURIFICATION; BIOSYNTHESIS; CHEMISTRY; GENETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE; PATHOLOGY;

ASPIRIN; CYCLOOXYGENASE 2; HMGB1 PROTEIN; HUMANS; INFLAMMATION; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SALICYLIC ACID;

EID: 84942431410     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/molmed.2015.00148     Document Type: Article

References (41)

1. Vane J. (1971) Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nat. New Biol. 231:232-5.
2. Weissmann G. (1991) Aspirin. Sci. Am. 264:84-90.
3. Vlot AC, Dempsey DA, Klessig DF. (2009) Salicylic Acid, a multifaceted hormone to combat disease. Annu. Rev. Phytopathol. 47:177-206.
4. Aboelsoud N. (2010) Herbal medicine in ancient Egypt. J. Med. Plants Res. 4:82-6.
5. Mitchell AG, Broadhead JF. (1967) Hydrolysis of solubilized aspirin. J. Pharm. Sci. 56:1261-6.
6. Rowland PM, Riegelman S, Harris PA, Sholkoff SD, Eyring EJ. (1967) Kinetics of acetylsalicylic acid disposition in man. Nature 215:413-4.
7. Ekinci D. (2011) Salicylic acid derivatives: synthesis, features and usage as therapeutic tools. Expert Opin. Ther. Pat. 21:1831-41.
8. Rothwell PM, et al. (2010) Long-term effect of aspirin on colorectal cancer incidence and mortality: 20-year follow-up of five randomised trials. Lancet. 376:1741-50.
9. Armitage J, et al. (2012) Aspirin for the older person: report of a meeting at the Royal Society of Medicine, London, 3rd November 2011. Ecancermedicalscience. 6:245.
10. Costello PB, Caruana JA, Green FA. (1984) The relative roles of hydrolases of the erythrocyte and other tissues in controlling aspirin survival in vivo. Arthritis Rheum. 27:422-6.
11. Tian M, et al. (2012) The combined use of photoaffinity labeling and surface plasmon resonance- based technology identifies multiple salicylic acid-binding proteins. Plant J. 72:1027-38.
12. Manohar M, et al. (2015) Identification of multiple salicylic acid-binding proteins using two high throughput screens. Front. Plant Sci. 5:777.
13. Lotze MT, Tracey KJ. (2005) High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat. Rev. Immunol. 5:331-42.
14. Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. (2010) Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. J. Mol. Biol. 403:706-22.
15. Celona B, et al. (2011) Substantial histone reduction modulates genomewide nucleosomal occupancy and global transcriptional output. PLoS Biol. 9:e1001086.
16. Andersson U, Tracey KJ. (2011) HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29:139-62.
17. Venereau E, et al. (2012) Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J. Exp. Med. 209:1519-28.
18. Yang H, et al. (2015) MD-2 is required for disulfide HMGB1-dependent TLR4 signaling. J. Exp. Med. 212:5-14.
19. Schiraldi M, et al. (2012) HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4. J. Exp. Med. 209:551-63.
20. Yang H, Ochani M, Li J. (2004) Reversing established sepsis with antagonists of endogenous high-mobility group box 1. Proc. Natl. Acad. Sci. U. S. A. 101:296-301.
21. Schierbeck H, et al. (2011) Monoclonal anti- HMGB1 (high mobility group box chromosomal protein 1) antibody protection in two experimental arthritis models. Mol. Med. 17:1039-44.
22. Porto A, et al. (2006) Smooth muscle cells in human atherosclerotic plaques secrete and proliferate in response to high mobility group box 1 protein. FASEB J. 20:2565-6.
23. Choi YR, et al. (2003) Overexpression of high mobility group box 1 in gastrointestinal stromal tumors with KIT mutation. Cancer Res. 63:2188-93.
24. Tang D, Kang R, Zeh HJ, Lotze MT. (2010) Highmobility group box 1 and cancer. Biochim. Biophys. Acta. 1799:131-40.
25. Jube S, et al. (2012) Cancer cell secretion of the DAMP protein HMGB1 supports progression in malignant mesothelioma. Cancer Res. 72:3290-301.
26. Ohndorf U, Rould M, He Q, Pabo C, Lippard S. (1999) Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature. 399:708-12.
27. Xiao R, et al. (2010) The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium. J. Struct. Biol. 172:21-33.
28. Acton TB, et al. (2011) Preparation of protein samples for NMR structure, function, and smallmolecule screening studies. Methods Enzymol. 493:21-60.
29. Farmer B 2nd, et al. (1996) Localizing the NADP+ binding site on the MurB enzyme by NMR. Nat. Struct. Biol 3:995-7.
30. Biamonti C, Rios C, Lyons B, Montelione G. (1994) Multidimensional NMR experiments and analysis techniques for determining homo- and heteronuclear scalar coupling constants in proteins and nucleic acids. Adv. Biophys. Chem. 4:51-120.
31. Moseley HNB, Monleon D, Montelione GT. (2001) Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 339:91-108.
32. Mollica L, et al. (2007) Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities. Chem. Biol. 14:431-41.
33. Sitia G, Iannacone M, Müller S, Bianchi ME, Guidotti LG. (2007) Treatment with HMGB1 inhibitors diminishes CTL-induced liver disease in HBV transgenic mice. J. Leukoc. Biol. 81:100-7.
34. Weidner C, et al. (2012) Amorfrutins are potent antidiabetic dietary natural products. Proc. Natl. Acad. Sci. U. S. A. 109:7257-62.
35. Mayer M, Meyer B. (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 123:6108-17.
36. Grosdidier A, Zoete V, Michielin O. (2011) Swiss- Dock, a protein-small molecule docking web service based on EADock DSS. Nucleic Acids Res. 39:W270-7.
37. Silver RM, et al. (1995) Bacterial lipopolysaccharide- mediated fetal death. Production of a newly recognized form of inducible cyclooxygenase (COX-2) in murine decidua in response to lipopolysaccharide. J. Clin. Invest. 95:725-31.
38. Hwang D. (2001) Modulation of the expression of cyclooxygenase-2 by fatty acids mediated through toll-like receptor 4-derived signaling pathways. FASEB J. 15:2556-64.
39. Proost J, Imhoff G Van, Wesseling H. (1983) Plasma levels of acetylsalicylic acid and salicylic acid after oral ingestion of plain and buffered acetylsalicylic acid in relation to bleeding time and thrombocyte function. Pharm. Weekbl. Sci. 5:22-7.
40. Mitchell JA, Saunders M, Barnes PJ, Newton R, Belvisi MG. (1997) Sodium salicylate inhibits cyclo-oxygenase-2 activity independently of transcription factor (nuclear factor fB) activation: role of arachidonic acid. Mol. Pharmacol. 912:907-12.
41. Yang H, et al. (2015) Aspirin delays mesothelioma growth by inhibiting HMGB1-mediated tumor progression. Cell Death Dis. 6:e1786.