A hydrogen peroxide safety valve: The reversible phosphorylation of catalase from the freeze-tolerant North American wood frog, Rana sylvatica

Dawson, Neal J.; Storey, Kenneth B.

doi:10.1016/j.bbagen.2015.12.007

Cited by 40 publications

(39 citation statements)

References 58 publications

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“…Found that wood frog catalase could be activated by phosphorylation of serine and thyrosine of the catalase protein. They are suggesting that researchers should explore the activation of catalase enzyme by phosphorylation in other catalases especially in human catalase enzyme [12]. Veal E et al, reported on the hydrogen peroxide signaling which could be enhanced in catalase deficiency [1].…”

Section: Resultsmentioning

confidence: 99%

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Blood Catalase Activities, Catalase Gene Polymorphisms and Acatalasemia Mutations in Hungarian Patients with Diabetes Mellitus

Góth¹

2016

Glob J Obes Diabetes Metab Syndr

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Introduction: Catalase decomposes hydrogen peroxide into oxygen and water. Its low concentration could be involved in signaling while its high concentration is toxic.Aim: This short review discusses the association of blood catalase and diabetes mellitus in Hungarian diabetic patients.Results: Several cohort studies showed decreased blood catalase activity in type 2 diabetes and in gestational diabetes.Among the catalase gene polymorphisms rs769217 showed a weak association with type 1 diabetes. Regarding rs1001179 polymorphism patients with TT genotype have a risk for lower life expectancy.In acatalasemics the frequency of diabetes mellitus is higher (P˂0.001) than in the Hungarian population. 11 of 12 known Hungarian acatalasemia mutations are found in diabetic patients. Acatalasemia may be associated with a higher risk for diabetes mellitus especially for its type 2 form.Acatalasemia mutations could explain the decreased (˂50%) blood catalase activities only in 17.4% of the cases. Conclusions:Blood catalase activity is decreased in type 2 and gestional diabetes. Patients with inherited catalase deficiency and known acatalasemia mutation are at higher risk of diabetes mellitus.The lifelong effect of oxidative damage on the oxidant sensitive, insulin producing pancreatic beta-cells could contribute to the manifestation of diabetes mellitus especially to type 2 form. Acatalasemia mutations could explain the reason for the catalase decrease while for the other (82.6 %) cases it remains unsolved.The decreased blood catalase activity in type 2 and gestational diabetes rather due to regulatory mechanisms than to the catalase gene mutations. Diabetes mellitus is a metabolic disorder characterized by hyperglycemia and either insufficiency of insulin secretion or diminished insulin sensitivity. Gestational diabetes occurs with variable severity in 3%-5% of all pregnancies. It is related to oxidative stress and impaired antioxidant defense [5]. Furthermore, Hur et al., conducted a web-based search for genes associated with reactive oxygen species and diabetes mellitus. This search showed that among the targets insulin was the first and catalase the second [6].There are several reports on decreased blood catalase activities in diseases of Hungarian subjects [7][8][9][10]. The main reasons for the blood catalase decrease might be caused by gene polymorphisms and mutations as well as regulatory mechanisms [11,12].

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Section: Resultsmentioning

confidence: 99%

“…The main reasons for the blood catalase decrease might be caused by gene polymorphisms and mutations as well as regulatory mechanisms [11,12].…”

Section: Discussionmentioning

confidence: 99%

Blood Catalase Activities, Catalase Gene Polymorphisms and Acatalasemia Mutations in Hungarian Patients with Diabetes Mellitus

Góth¹

2016

Glob J Obes Diabetes Metab Syndr

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“…CAT is a high activity enzyme in cells and is often regarded as being paired with SOD in antioxidant defense since it can catabolize the H 2 O 2 product of SOD. Purified CAT from skeletal muscle of frozen frogs showed a significantly higher V max activity (1.48‐fold) and a significantly lower K m H 2 O 2 (0.64‐fold) as compared with control CAT, indicating an enhanced functionality of the enzyme in frozen muscle. CAT from frozen frogs also showed higher protein phosphorylation (1.73‐fold) that included both enhanced phosphoserine (1.60‐fold) and phosphotyrosine (1.27‐fold) contents, compared to controls.…”

Section: Antioxidant Enzymes: New Evidence Of Control By Post‐translamentioning

confidence: 93%

“…However, antioxidant enzymes have received relatively little attention in this regard even though it is clear that coordinated responses by antioxidant defenses to environmental stress would be adaptive in many situations. Recent work on superoxide dismutase (SOD) and catalase (CAT) purified from skeletal muscle of control (5 °C) versus frozen (24 h at −3 °C) wood frogs has given first indications that PTMs provide a mechanism for adaptive regulation of antioxidant enzymes to environmental stress

SOD : 2 {O_{2}}^{•}^{-} + 2 H^{+} \to H_{2} O_{2} + O_{2}

CAT : 2 H_{2} O_{2} \to 2 H_{2} normalO + O_{2}

…”

Section: Antioxidant Enzymes: New Evidence Of Control By Post‐translamentioning

confidence: 99%

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Mitochondria, metabolic control and microRNA: Advances in understanding amphibian freeze tolerance

Storey

2019

BioFactors

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Winter survival for many animal species depends freeze tolerance, a capacity to endure the conversion of as much as 65–70% of total body water into extracellular ice while reorganizing metabolism to provide cells with cryoprotection against insults that include prolonged ischemia and hyperosmotic stress. Natural freeze tolerance involves not just de novo preservation mechanisms such as synthesis of high levels of cryoprotectants or novel proteins that manage ice formation, but also requires attention to and co‐ordination of many cellular processes. The present review examines recent studies of the freeze‐tolerant wood frog (Rana sylvatica) that probed previously unexplored areas of metabolic adaptation for freezing survival, with a particular emphasis on mitochondria. Post‐translational controls on enzyme function play a prominent role in resculpting metabolic responses of the wood frog to freezing including reversible phosphorylation control over fuel processing at the pyruvate dehydrogenase locus and modulation of antioxidant defense enzymes (Mn‐SOD, catalase). Enzymes involved in mitochondrial nitrogen metabolism (glutamate dehydrogenase, carbamoyl phosphate synthetase) are also differentially regulated during freezing but by different post‐translational modifications including ADP‐ribosylation, lysine acetylation or glutarylation. The action of microRNAs in mediating post‐translational controls on gene expression aid the suppression of energy‐expensive (cell cycle) or destructive (apoptosis) processes in the frozen state while also providing storage of transcripts that will be immediately available for repair or reactivation of metabolic processes after thawing. The effects of low temperature in strengthening mRNA–microRNA interactions can also provide a passive mechanism of metabolic suppression in the frozen state.

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Solving Donor Organ Shortage with Insights from Freeze Tolerance in Nature

Luu¹,

Storey²

2018

BioEssays

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The North American wood frog, Rana sylvatica, endures seasonal whole-body freezing during the winter and thawing during the spring without sustaining any apparent damage from ice or oxidative stress. Strategies from these frogs may solve the shortage of human donor organs, which is a multidisciplinary problem that can be alleviated by eliminating geographical boundaries. Rana sylvatica deploys an array of molecular and physiological responses, such as glucose production and microRNA regulation, to help it survive the cold. These strategies have been adapted in the lab to impart cryotolerance in liver cells, and the non-freezing supercooled storage of transplantable rat livers - milestones that have advanced the field toward cryopreserving human donor organs in the clinic. In this review, a case is presented for the use of non-coding RNAs to decrease oxidative damage of donor organs by activating endogenous antioxidant systems prior to procurement.

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A hydrogen peroxide safety valve: The reversible phosphorylation of catalase from the freeze-tolerant North American wood frog, Rana sylvatica

Cited by 40 publications

References 58 publications

Blood Catalase Activities, Catalase Gene Polymorphisms and Acatalasemia Mutations in Hungarian Patients with Diabetes Mellitus

Blood Catalase Activities, Catalase Gene Polymorphisms and Acatalasemia Mutations in Hungarian Patients with Diabetes Mellitus

Mitochondria, metabolic control and microRNA: Advances in understanding amphibian freeze tolerance

Solving Donor Organ Shortage with Insights from Freeze Tolerance in Nature

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