Nitrogen Monoxide (NO) Storage and Transport by Dinitrosyl-Dithiol-Iron Complexes: Long-lived NO That Is Trafficked by Interacting Proteins
Nitrogen monoxide (NO) markedly affects intracellular iron metabolism, and recent studies have shown that molecules traditionally involved in drug resistance, namely GST and MRP1 (multidrug resistance-associated protein 1), are critical molecular players in this process. This is mediated by interact...
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| Veröffentlicht in: | The Journal of biological chemistry 2012-03, Vol.287 (10), p.6960-6968 |
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| creator | Suryo Rahmanto, Yohan Kalinowski, Danuta S. Lane, Darius J.R. Lok, Hiu Chuen Richardson, Vera Richardson, Des R. |
| description | Nitrogen monoxide (NO) markedly affects intracellular iron metabolism, and recent studies have shown that molecules traditionally involved in drug resistance, namely GST and MRP1 (multidrug resistance-associated protein 1), are critical molecular players in this process. This is mediated by interaction of these proteins with dinitrosyl-dithiol-iron complexes (Watts, R. N., Hawkins, C., Ponka, P., and Richardson, D. R. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 7670–7675; Lok, H. C., Suryo Rahmanto, Y., Hawkins, C. L., Kalinowski, D. S., Morrow, C. S., Townsend, A. J., Ponka, P., and Richardson, D. R. (2012) J. Biol. Chem. 287, 607–618). These complexes are bioavailable, have a markedly longer half-life compared with free NO, and form in cells after an interaction between iron, NO, and glutathione. The generation of dinitrosyl-dithiol-iron complexes acts as a common currency for NO transport and storage by MRP1 and GST P1-1, respectively. Understanding the biological trafficking mechanisms involved in the metabolism of NO is vital for elucidating its many roles in cellular signaling and cytotoxicity and for development of new therapeutic targets. |
| doi_str_mv | 10.1074/jbc.R111.329847 |
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This is mediated by interaction of these proteins with dinitrosyl-dithiol-iron complexes (Watts, R. N., Hawkins, C., Ponka, P., and Richardson, D. R. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 7670–7675; Lok, H. C., Suryo Rahmanto, Y., Hawkins, C. L., Kalinowski, D. S., Morrow, C. S., Townsend, A. J., Ponka, P., and Richardson, D. R. (2012) J. Biol. Chem. 287, 607–618). These complexes are bioavailable, have a markedly longer half-life compared with free NO, and form in cells after an interaction between iron, NO, and glutathione. The generation of dinitrosyl-dithiol-iron complexes acts as a common currency for NO transport and storage by MRP1 and GST P1-1, respectively. Understanding the biological trafficking mechanisms involved in the metabolism of NO is vital for elucidating its many roles in cellular signaling and cytotoxicity and for development of new therapeutic targets.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.R111.329847</identifier><identifier>PMID: 22262835</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Biological Transport, Active - physiology ; Glutathione - metabolism ; Glutathione S-Transferase pi - metabolism ; Humans ; Iron ; Iron Compounds - metabolism ; Iron Metabolism ; Metals ; Minireviews ; Multidrug Resistance-Associated Proteins - metabolism ; Nitric Oxide - metabolism ; Nitrogen Oxides - metabolism ; Protein-Metal Ion Interaction ; Signal Transduction - physiology ; Transport Metals</subject><ispartof>The Journal of biological chemistry, 2012-03, Vol.287 (10), p.6960-6968</ispartof><rights>2012 © 2012 ASBMB. 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This is mediated by interaction of these proteins with dinitrosyl-dithiol-iron complexes (Watts, R. N., Hawkins, C., Ponka, P., and Richardson, D. R. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 7670–7675; Lok, H. C., Suryo Rahmanto, Y., Hawkins, C. L., Kalinowski, D. S., Morrow, C. S., Townsend, A. J., Ponka, P., and Richardson, D. R. (2012) J. Biol. Chem. 287, 607–618). These complexes are bioavailable, have a markedly longer half-life compared with free NO, and form in cells after an interaction between iron, NO, and glutathione. The generation of dinitrosyl-dithiol-iron complexes acts as a common currency for NO transport and storage by MRP1 and GST P1-1, respectively. Understanding the biological trafficking mechanisms involved in the metabolism of NO is vital for elucidating its many roles in cellular signaling and cytotoxicity and for development of new therapeutic targets.</description><subject>Animals</subject><subject>Biological Transport, Active - physiology</subject><subject>Glutathione - metabolism</subject><subject>Glutathione S-Transferase pi - metabolism</subject><subject>Humans</subject><subject>Iron</subject><subject>Iron Compounds - metabolism</subject><subject>Iron Metabolism</subject><subject>Metals</subject><subject>Minireviews</subject><subject>Multidrug Resistance-Associated Proteins - metabolism</subject><subject>Nitric Oxide - metabolism</subject><subject>Nitrogen Oxides - metabolism</subject><subject>Protein-Metal Ion Interaction</subject><subject>Signal Transduction - physiology</subject><subject>Transport Metals</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUFvEzEQhS0EomnhzA35Bhw2tb3rjZdDJZSWEikkVQkSN8vrnd24bOxgO1HzG_jT9SqlggNzGWn85hvrPYTeUDKmZFKc39V6fEspHeesEsXkGRpRIvIs5_THczQihNGsYlycoNMQ7kiqoqIv0QljrGQi5yP0e2Gidx1Y_NVZd28awO8Xyw_4W3RedYCVbfDKKxu2zkdcH_ClscNGOPTZpYlr4_ps5p3FU7fZ9nAP4SOeO9tlvdlDgxdLvFqriGdhoLSt0T_TNGFmNoJXOhrb4RvvIhgbXqEXreoDvH7sZ-j756vV9Es2X17Ppp_mmS4KFrMaqCAVaeuyqQVAqaBgnFBeq1ITKqhueDVRPCd1y7UuSEUJG-aMc94wLfIzdHHkbnf1BhoNNnrVy603G-UP0ikj_32xZi07t5fJ5JwLlgDvHgHe_dpBiHJjgoa-VxbcLsiKlZwUVPCkPD8qdbIseGifrlAihwRlSlAOCcpjgmnj7d-fe9L_iSwJqqMAkkV7A14GbcBqaIwHHWXjzH_hD7sZrJE</recordid><startdate>20120302</startdate><enddate>20120302</enddate><creator>Suryo Rahmanto, Yohan</creator><creator>Kalinowski, Danuta S.</creator><creator>Lane, Darius J.R.</creator><creator>Lok, Hiu Chuen</creator><creator>Richardson, Vera</creator><creator>Richardson, Des R.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120302</creationdate><title>Nitrogen Monoxide (NO) Storage and Transport by Dinitrosyl-Dithiol-Iron Complexes: Long-lived NO That Is Trafficked by Interacting Proteins</title><author>Suryo Rahmanto, Yohan ; 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| subjects | Animals Biological Transport, Active - physiology Glutathione - metabolism Glutathione S-Transferase pi - metabolism Humans Iron Iron Compounds - metabolism Iron Metabolism Metals Minireviews Multidrug Resistance-Associated Proteins - metabolism Nitric Oxide - metabolism Nitrogen Oxides - metabolism Protein-Metal Ion Interaction Signal Transduction - physiology Transport Metals |
| title | Nitrogen Monoxide (NO) Storage and Transport by Dinitrosyl-Dithiol-Iron Complexes: Long-lived NO That Is Trafficked by Interacting Proteins |
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