30 Jul 2012
The cyclic nature of PRX (see Appendix I) promoted incorporation of the ur-mitochondrium into the cell . A matching of supply and demand of ATP into a 24 hour cycle .
PRX invited Mitochondria into the cell , but the spin of mitochondria has ruled since . Melatonin as a Terminator anti-oxidant determines the frequency of the system . Which eventually ties it to the Terran day-night system
Spin-Mirror neuron networks .
Mitochondrial spins are connected to neural mirror-network spins via quantal connections .
Think two chain links spinning around themselves and also rotating around their circumference in harmony . This has a natural resonance with mitochondria . There is a mutual interaction . This is an old harmony wanting to reassert itself .
You have old , well-established neural mirror neuron networks just waiting for the right spins .
The normal system results from random distribution of mitochondrial spin . Some direction gives rise to the standard distribution curve of rapid result initially , tapering off .
Every memory changes over time .
Inhibitory role of peroxiredoxin II (Prx II) on cellular senescence.
Han YH, Kim HS, Kim JM, Kim SK, Yu DY, Moon EY.
Laboratory of Human Genomics, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 52 Oun-Dong, Yusong, Taejeon 305-806, Korea.
• FEBS Lett. 2005 Sep 12;579(22):5112.
Reactive oxygen species (ROS) were generated in all oxygen-utilizing organisms. Peroxiredoxin II (Prx II) as one of antioxidant enzymes may play a protective role against the oxidative damage caused by ROS. In order to define the role of Prx II in organismal aging, we evaluated cellular senescence in Prx II(-/-) mouse embryonic fibroblast (MEF). As compared to wild type MEF, cellular senescence was accelerated in Prx II(-/-) MEF. Senescence-associated (SA)-beta-galactosidase (Gal)-positive cell formation was about 30% higher in Prx II(-/-) MEF. N-Acetyl-l-cysteine (NAC) treatment attenuated SA-beta-Gal-positive cell formation. Prx II(-/-) MEF exhibited the higher G2/M (41%) and lower S (1.6%) phase cells as compared to 24% and 7.3% [corrected] in wild type MEF, respectively. A high increase in the p16 and a slight increase in the p21 and p53 levels were detected in PrxII(-/-) MEF cells. The cellular senescence of Prx II(-/-) MEF was correlated with the organismal aging of Prx II(-/-) mouse skin. While extracellular signal-regulated kinase (ERK) and p38 activation was detected in Prx II(-/-) MEF, ERK and c-Jun N-terminal kinase (JNK) activation was detected in Prx II(-/-) skin. These results suggest that Prx II may function as an enzymatic antioxidant to prevent cellular senescence and skin aging.
[PubMed - indexed for MEDLINE]
Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver.
Bae SH, Sung SH, Cho EJ, Lee SK, Lee HE, Woo HA, Yu DY, Kil IS, Rhee SG.
Department of Life Science, Division of Life and Pharmaceutical Sciences, Ewha Womans University, Seoul, Korea. firstname.lastname@example.org
Peroxiredoxins (Prxs) are peroxidases that catalyze the reduction of reactive oxygen species (ROS). The active site cysteine residue of members of the 2-Cys Prx subgroup (Prx I to IV) of Prxs is hyperoxidized to cysteine sulfinic acid (Cys-SO(2) ) during catalysis with concomitant loss of peroxidase activity. Reactivation of the hyperoxidized Prx is catalyzed by sulfiredoxin (Srx). Ethanol consumption induces the accumulation of cytochrome P450 2E1 (CYP2E1), a major contributor to ethanol-induced ROS production in the liver. We now show that chronic ethanol feeding markedly increased the expression of Srx in the liver of mice in a largely Nrf2-dependent manner. Among Prx I to IV, only Prx I was found to be hyperoxidized in the liver of ethanol-fed wildtype mice, and the level of Prx I-SO(2) increased to ≈30% to 50% of total Prx I in the liver of ethanol-fed Srx(-/-) mice. This result suggests that Prx I is the most active 2-Cys Prx in elimination of ROS from the liver of ethanol-fed mice and that, despite the up-regulation of Srx expression by ethanol, the capacity of Srx is not sufficient to counteract the hyperoxidation of Prx I that occurs during ROS reduction. A protease protection assay revealed that a large fraction of Prx I is located together with CYP2E1 at the cytosolic side of the endoplasmic reticulum membrane. The selective role of Prx I in ROS removal is thus likely attributable to the proximity of Prx I and CYP2E1. CONCLUSION: The pivotal functions of Srx and Prx I in protection of the liver in ethanol-fed mice was evident from the severe oxidative damage observed in mice lacking either Srx or Prx I.