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Oxidative stress leads to pancreatic dysfunction

Discussion in 'The Gut: De Meirleir & Maes; H2S; Leaky Gut' started by Suzy, Jan 6, 2010.

  1. Suzy

    Suzy Guest

    This will be interesting for those , like me, tht have poor pancreatic function. The catalase part is really interesting b/c it detoxifies hydrogen peroxide and hydrogen peroxide is being found in excess amounts in patients with vitiligo , which I have.

    Superoxide dismutase and catalase: a possible role in established pancreatitis.
    Guice KS, Miller DE, Oldham KT, Townsend CM Jr, Thompson JC.

    The mechanism of cerulein-induced acute pancreatitis may involve the production of free radicals in excess of the capacity of endogenous intracellular scavengers. These radicals destroy the cellular membranes, releasing digestive enzymes and cellular proteins into the interstitium. Thereafter, a cascade of events, including polymorphonuclear infiltration and complement activation, leads to pancreatic destruction. The present study demonstrates that superoxide dismutase and catalase reduce the ultrastructural and biochemical injury associated with cerulein-induced acute pancreatitis in rats. Pretreatment with superoxide dismutase and catalase 30 minutes before injury did not appear to be protective, presumably because the half-life of intravenous superoxide dismutase is only 6 minutes. This and similar studies suggest a potential clinical role for free radical scavengers in acute established pancreatitis.
  2. Suzy

    Suzy Guest

    And this shows the importance of catalase in removing hydrogen peroxide. Glutathione peroxidase is much less efficient. So, if your catalase is not funcitioning properly, for whatever reason, I imagine a buildup of hydrogen peroxide will occur, even if glutathoien is normal.

    Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
    Auteur(s) / Author(s)
    Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)
    Univ. Genoa, ist. nazionale ric. cancro and ist. oncologia clin. sper., Genoa, ITALIE

    Rsum / Abstract
    Purified enzymes were mixed to form a cell-free system that simulated the conditions for removal of hydrogen peroxide within human erythrocytes. Human glutathione peroxidase disposed of hydrogen peroxide (H2O2) at a rate that was only 17% of the rate at which human catalase simultaneously removed hydrogen peroxide. The relative rates observed were in agreement with the relative rates predicted from the kinetic constants of the two enzymes. These results confirm two earlier studies on intact erythrocytes, which refuted the notion that glutathione peroxidase is the primary enzyme for removal of hydrogen peroxide within erythrocytes. The present findings differ from the results with intact cells, however, in showing that glutathione peroxidase accounts for even less than 50% of the removal of hydrogen peroxide. A means is proposed for calculating the relative contribution of glutathione peroxidase and catalase in other cells and species. The present results raise the possibility that the major function of glutathione peroxidase may be the disposal of organic peroxides rather than the removal of hydrogen peroxide.
  3. JanisB

    JanisB Senior Member

    Central Ohio
    So Suzy, do you know if taking catalase and SOD (Biotics Research makes a powder called Dismuzyme that contains it) can actually help repair damage?

    I too am finding mild pancreatic issues on my healing journey, perhaps a side effect of stress from chelation.
  4. George

    George Guest

    Thanks for the post Suzy, this looks really interesting.
  5. Suzy

    Suzy Guest

    I'm not sure Janis, this is allnew to me in the last couple of days. I've been taking antioxidants and Rich's protocol and my vitiligo is not budging so had to search for more answers. I'll check out that powder. Have you heard anything , good or bad, about it ?

  6. JanisB

    JanisB Senior Member

    Central Ohio
    I took it once (they promote it for hepatitis) and didn't feel any difference.
  7. Sunday

    Sunday Senior Member

    I'm going to put in a quote from RichvanK here, something he said on another thread. (Don't know the official way to do quotes and don't have the brains to learn today, so it's a cut-and-paste.)

    You might be interested to know that Dr. Kunin told me that he thinks that normal pancreatic digestive enzymes are capable of breaking down biofilm. As I posted on another thread, he also enlightened me to the fact that the secretion of digestive enzymes by the pancreas is dependent on methylation. Putting these two together would say that the methylation problem is what allows the biofilms to form, and it suggests that if methylation is fixed, maybe the biofilms will be broken down, perhaps restoring good gut function. I realize that I have made some leaps in logic here, but please just consider this an unproven hypothesis!



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