Secluding few lines on physiological interactions triggered by reducers

  • Authors

    • Muhammad Torequl Islam LecturerDepartment of PharmacySouthern University BangladeshMehedibag-4000, Chittagong
    2017-01-23
    https://doi.org/10.14419/ijm.v5i1.7036
  • Redox-Reaction, Physiological Role, Biological Interactions.
  • Abstract

    Nowadays, we are very much concerned about the physiological contributions of oxidative species (e.g. - free radicals, reactive species). These include reactive oxygen/nitrogen species (ROS/RNS), vastly under continuous study in the medical concerns, emphasized on normal physiological as well as pathophysiological conditions. Being oxidizer, they have enforced us to search substances or conditions capability to counteract them, called the reducers. Doubtless, redox reaction has numerous roles in a biological system; despite we badly count the effects of ROS. This paper depicts some important interactions related to the reduction effects on the biological systems.

  • References

    1. [1] Sena LA, Chandel NS. Physiological roles of mitochondrial reactive oxygen species. Mol Cell 2012; 48:158-167. https://doi.org/10.1016/j.molcel.2012.09.025.

      [2] Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002; 82:47-95. https://doi.org/10.1152/physrev.00018.2001.

      [3] Kamata H, Hirata H. Redox regulation of cellular signalling. Cell Signal 1999; 11:1-14. https://doi.org/10.1016/S0898-6568(98)00037-0.

      [4] Haghdoost S, Czene S, Naslund I, Skog S, Harms-Ringdahl M. Extracellular 8-oxo-dG as a sensitive parameter for oxidative stress in vivo and in vitro. Free Radic Res 2005; 39:153-162. https://doi.org/10.1080/10715760500043132.

      [5] DeNicola GM. Karreth FA, Humpton TJ, Gopinathan A, Wei C, Frese K, et al. Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature 2011; 475:106-109. https://doi.org/10.1038/nature10189.

      [6] Van Remmen H, Ikeno Y, Hamilton M, Pahlavani M, Wolf N, Thorpe SR, et al. Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging. Physiol Genom 2003; 16:29-37. https://doi.org/10.1152/physiolgenomics.00122.2003.

      [7] Schriner SE, Linford NJ, Martin GM, Treuting P, Ogburn CE, Emond M, et al. Extension of murine life span by overexpression of catalase targeted to mitochondria. Sci 2005; 308:1909-1911. https://doi.org/10.1126/science.1106653.

      [8] Yang W, Li J, Hekimi SA. Measurable increase in oxidative damage due to reduction in superoxide detoxification fails to shorten the life span of long-lived mitochondrial mutants of Caenorhabditis elegans. Genetics 2007; 177:2063-2074. https://doi.org/10.1534/genetics.107.080788.

      [9] Islam MT, Streck L, Paz MFCJ, Sousa JMC, Alencar MVOB, Mata AMOF, et al. Preparation of phytol-loaded nanoemulsion and screening for antioxidant capacity. Int Arch Med 2016; 9:1-15. https://doi.org/10.3823/1941.

      [10] Islam MT, Ali ES, Sousa JMC, Santos JVO, Paz MFCJ, Lima RMT, et al. Physiological contributions of reactive oxygen species. Photon eBooks. Ed. I, Nov 2016. Pages 1-13. UBN: 015-A94510112030.

      [11] Kehrer JP. The Haber-Weiss reaction and mechanisms of toxicity. Toxicol 2000; 149:43-50. https://doi.org/10.1016/S0300-483X(00)00231-6.

      [12] Brigelius-Flohe R. Glutathione peroxidases and redox-regulated transcription factors. Biol Chem 2006; 387:1329-1335. https://doi.org/10.1515/BC.2006.166.

      [13] Lee SR, Kwon KS, Kim SR, Rhee SG. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 1998; 273:15366-15372. https://doi.org/10.1074/jbc.273.25.15366.

      [14] Nakamura H, Nakamura K, Yodoi J. Redox regulation of cellular activation. Annu Rev Immunol 1997; 15:351-369. https://doi.org/10.1146/annurev.immunol.15.1.351.

      [15] Holmgren A, Aslund F. Glutaredoxin. Methods Enzymol 1995; 252:283-292. https://doi.org/10.1016/0076-6879(95)52031-7.

      [16] Rhee SG, Yang K-S, Kang SW, Woo HA, Chang T-S. Controlled elimination of intracellular H2O2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid Redox Signal 2005; 7:619-626. https://doi.org/10.1089/ars.2005.7.619.

      [17] Wood ZA, Schroder E, Robin Harris J, Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci 2003; 28:32-40. https://doi.org/10.1016/S0968-0004(02)00003-8.

      [18] Pinchuk I, Schnitzer E, Lichtenberg D. Kinetic analysis of copper-induced peroxidation of LDL. Biochim Biophys Acta 1998; 1389:155-172. https://doi.org/10.1016/S0005-2760(97)00139-2.

      [19] Awasthi YC, Sharma R, Cheng JZ, Yang Y, Sharma A, Singhal SS, et al. Role of 4-hydroxynonenal in stress-mediated apoptosis signaling. Mol Aspects Med 2003; 24:219-230. https://doi.org/10.1016/S0098-2997(03)00017-7.

      [20] Breen AP, Murphy JA. Reactions of oxyl radicals with DNA. Free Radic Biol Med 1995; 18:1033-1077. https://doi.org/10.1016/0891-5849(94)00209-3.

      [21] Haddad JJ. Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors. Cell Signal 2002; 14:879-897. https://doi.org/10.1016/S0898-6568(02)00053-0.

      [22] Turpaev KT. Reactive oxygen species and regulation of gene expression. Biochemistry (Moscow) 2002; 67:281-292. https://doi.org/10.1023/A:1014819832003.

      [23] Drazic A, Winter J. The physiological role of reversible methionine oxidation. Biochim Biophys Acta 2014; 1844:1367-1382. https://doi.org/10.1016/j.bbapap.2014.01.001.

      [24] Bhaskar PT, Hay N. The two TORCs and Akt. Dev Cell 2007; 12:487-502. https://doi.org/10.1016/j.devcel.2007.03.020.

      [25] Rahman I, Marwick J, Kirkham P. Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem Pharmacol 2004; 68:1255-1267. https://doi.org/10.1016/j.bcp.2004.05.042.

      [26] Heneberg P, Draber P. Regulation of cys-based protein tyrosine phosphatases via reactive oxygen and nitrogen species in mast cells and basophils. Curr Med Chem 2005; 12:1859-1871. https://doi.org/10.2174/0929867054546636.

      [27] Edgar RS, Green EW, Zhao Y, van Ooijen G, Olmedo M, Qin X, et al. Peroxiredoxins are conserved markers of circadian rhythms. Nature 2012; 485:459-464. https://doi.org/10.1038/nature11088.

      [28] Lee C, Lee SM, Mukhopadhyay P, Kim SJ, Lee SC, Ahn WS, et al. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nature Struct Mol Biol 2004; 11:1179-1185. https://doi.org/10.1038/nsmb856.

      [29] Putker M, Madl T, Vos HR, de Ruiter H, Visscher M, van den Berg MC, et al. Redox-dependent control of FOXO/ DAF 16 by transportin 1. Mol Cell 2013; 49:730-742. https://doi.org/10.1016/j.molcel.2012.12.014.

      [30] Taguchi K, Motohashi H, Yamamoto M. Molecular mechanisms of the Keap1–Nrf2 pathway in stress response and cancer evolution. Genes Cells 2011; 16:123-140. https://doi.org/10.1111/j.1365-2443.2010.01473.x.

      [31] Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 2007; 26:1749-1760. https://doi.org/10.1038/sj.emboj.7601623.

      [32] Zhang Y, Choksi S, Chen K, Pobezinskaya Y, Linnoila I, Liu ZG. ROS play a critical role in the differentiation of alternatively activated macrophages and the occurrence of tumor-associated macrophages. Cell Res 2013; 23:898-914. https://doi.org/10.1038/cr.2013.75.

      [33] Liu J, Cao L, Chen J, Song S, Lee IH, Quijano C, et al. Bmi1 regulates mitochondrial function and the DNA damage response pathway. Nature 2009; 459:387-392. https://doi.org/10.1038/nature08040.

      [34] Chatoo W, Abdouh M, David J, Champagne M-P, Ferreira J, Rodier F, et al. The polycomb group gene Bmi1 regulates antioxidant defenses in neurons by repressing p53 pro-oxidant activity. J Neurosci 2009; 29:529-542. https://doi.org/10.1523/JNEUROSCI.5303-08.2009.

      [35] Li TS, Marban E. Physiological levels of reactive oxygen species are required to maintain genomic stability in stem cells. Stem Cells 2010; 28:1178-1185. https://doi.org/10.1002/stem.438.

  • Downloads

  • How to Cite

    Islam, M. T. (2017). Secluding few lines on physiological interactions triggered by reducers. International Journal of Medicine, 5(1), 28-31. https://doi.org/10.14419/ijm.v5i1.7036

    Received date: 2016-12-03

    Accepted date: 2017-01-11

    Published date: 2017-01-23