Hereditary catalase deficiencies and increased risk of diabetes

Góth, László; Eaton, John W.

doi:10.1016/s0140-6736(00)03238-4

Cited by 166 publications

(104 citation statements)

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“…The evidence is mounting -peroxisome redox balance is a major determinant of cell stress and the presence or absence of cell pathology. Perhaps it is not surprising then that epidemiological studies suggest a very strong link exists between diminishing cellular catalase levels and the onset of degenerative disease [24] .…”

Section: Genetic Diseasementioning

confidence: 99%

Peroxisomes, oxidative stress, and inflammation

Terlecky

Terlecky²,

Giordano³

2012

WJBC

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Peroxisomes are intracellular organelles mediating a wide variety of biosynthetic and biodegradative reactions. Included among these are the metabolism of hydrogen peroxide and other reactive species, molecules whose levels help define the oxidative state of cells. Loss of oxidative equilibrium in cells of tissues and organs potentiates inflammatory responses which can ultimately trigger human disease. The goal of this article is to review evidence for connections between peroxisome function, oxidative stress, and inflammation in the context of human health and degenerative disease. Dysregulated points in this nexus are identified and potential remedial approaches are presented.

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Section: Genetic Diseasementioning

confidence: 99%

Peroxisomes, oxidative stress, and inflammation

Terlecky

Terlecky²,

Giordano³

2012

WJBC

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“…The lack of peroxiredoxin II was also shown to result in haemolytic anaemia [150]. On the other hand, patients having hereditary catalase deficiencies were also shown to be victims of oxidative stress and presented a high prevalence of diabetes [151]. Gaetani et al [152] also demonstrated that catalase is essential for the removal of H 2 O 2 from RBCs, having an activity six times higher than glutathione peroxidase.…”

Section: Red Blood Cellsmentioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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Protein oxidation mechanisms result in a wide array of modifications, from backbone cleavage or protein crosslinking to more subtle modifications such as side chain oxidations. Protein oxidation occurs as part of normal regulatory processes, as a defence mechanism against oxidative stress, or as a deleterious processes when antioxidant defences are overcome. Because blood is continually exposed to reactive oxygen and nitrogen species, blood proteomics should inherently adopt redox proteomic strategies. In this review, we recall the biochemical basis of protein oxidation, review the proteomic methodologies applied to analyse redox modifications, and highlight some physiological and in vitro responses to oxidative stress of various blood components.

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“…Described strain differences in rat islet sensitivity to IL-1β and nitric oxide might be due to different capacities to mount a free radical defence [14]. Hereditary catalase deficiencies and polymorphisms in the MnSOD gene are reported to increase the risk for Type I diabetes [79,80,81].…”

Section: Cellular Defence (Two Proteins)mentioning

confidence: 99%

IL-1β induced protein changes in diabetes prone BB rat islets of Langerhans identified by proteome analysis

Sparre

Bjerre-Christensen

Larsen³

et al. 2002

Diabetologia

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Aims/hypothesis. Type I (insulin-dependent) diabetes mellitus is characterized by selective destruction of the insulin producing beta cells. Interleukin-1β (IL-1β) modulates the beta-cell function, protein synthesis, energy production and causes apoptosis. We have previously shown changes in the expression of 82 out of 1 815 protein spots detected by two dimensional gel electrophoresis in IL-1β exposed diabetes prone Bio Breeding (BB-DP) rat islets of Langerhans in vitro. The aim of this study was to identify the proteins in these 82 spots by mass spectrometry and compare these changes with those seen in IL-1β exposed Wistar Furth (WF) rat islets. Methods. The 82 protein spots, that changed expression after IL-1β exposure, were all re-identified on preparative gels of 200 000 neonatal WF rat islets, cut out and subjected to mass spectrometry for identification.Results. Forty-five different proteins were identified from 51 spots and grouped according to function: (i) energy transduction and redox potentials; (ii) glycolytic and Krebs cycle enzymes; (iii) protein, DNA and RNA synthesis, chaperoning and protein folding; (iv) signal transduction, regulation, differentiation and apoptosis; (v) cellular defence; and (vi) other functions. Comparison of IL-1β exposed BB-DP and WF islets showed common changes in 14 proteins and several proteins influencing similar pathways, suggesting that similar routes in the two strains lead to beta-cell destruction. Conclusion/interpretation. We demonstrate that proteome analysis is a powerful tool to identify proteins and pathways in BB-DP rat islets exposed to IL-1β. [Diabetologia (2002) 45:1550-1561

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Hereditary catalase deficiencies and increased risk of diabetes

Cited by 166 publications

References 1 publication

Peroxisomes, oxidative stress, and inflammation

Peroxisomes, oxidative stress, and inflammation

Oxidation of proteins: Basic principles and perspectives for blood proteomics

IL-1β induced protein changes in diabetes prone BB rat islets of Langerhans identified by proteome analysis

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