The Impact of Peroxisomes on Cellular Aging and Death

Manivannan, Selvambigai; Scheckhuber, Christian Q.; Veenhuis, Marten; Klei, Ida J. van der

doi:10.3389/fonc.2012.00050

Cited by 47 publications

(25 citation statements)

References 75 publications

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“…Hydrogen peroxide (H 2 O 2 ) is a ubiquitous cellular oxidant that is mostly produced by the peroxisome (Manivannan et al, 2012) and high cellular level of H 2 O 2 is well-known to oxidize the lipids on the biological membrane and consequently compromises the membrane integrity (Johnson et al, 2005;Repetto et al, 2012). (Sharma et al, 2001;Leuratti et al, 2002;Alzoghaibi et al, 2007).…”

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 99%

Benzo(a)pyrene induces oxidative stress, pro-inflammatory cytokines, expression of nuclear factor-kappa B and deregulation of wnt/beta-catenin signaling in colons of BALB/c mice

Ajayi

Adedara

Farombi

2016

Food and Chemical Toxicology

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Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 99%

Benzo(a)pyrene induces oxidative stress, pro-inflammatory cytokines, expression of nuclear factor-kappa B and deregulation of wnt/beta-catenin signaling in colons of BALB/c mice

Ajayi

Adedara

Farombi

2016

Food and Chemical Toxicology

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“…As a result, the damage that occurs within the mitochondrion is not isolated, but impacts the rest of the cell by increasing the overall amount of reactive oxygen species, protein oxidation, lipid peroxidation, and DNA damage (Balaban, Nemoto & Finkel, 2005). A similar relationship, involving the spread of oxidative damage, is believed to occur between peroxisomes and the cell (Manivannan et al , 2012). …”

Section: The Interaction Between Mitochondria and Peroxisomesmentioning

confidence: 96%

“…This results in the formation of a seemingly healthier peroxisome at the expense of a more highly damaged one. Consequently, the division of an already damaged organelle may temporarily alleviate cellular stress, but eventually the damaged peroxisomes, if not cleared, will outweigh the formation of healthy ones (Manivannan et al , 2012). …”

Section: Peroxisomes Lonp2 Aging and Diseasementioning

confidence: 99%

The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1

2016

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Peroxisomes are ubiquitous eukaryotic organelles with the primary role of breaking down very long- and branched-chain fatty acids for subsequent β-oxidation in the mitochondrion. Like mitochondria, peroxisomes are major sites for oxygen utilization and potential contributors to cellular oxidative stress. The accumulation of oxidatively damaged proteins, which often develop into inclusion bodies (of oxidized, aggregated, and cross-linked proteins) within both mitochondria and peroxisomes, results in loss of organelle function that may contribute to the aging process. Both organelles possess an isoform of the Lon protease that is responsible for degrading proteins damaged by oxidation. While the importance of mitochondrial Lon (LonP1) in relation to oxidative stress and aging has been established, little is known regarding the role of LonP2 and aging-related changes in the peroxisome. Recently, peroxisome dysfunction has been associated with aging-related diseases indicating that peroxisome maintenance is a critical component of ‘healthy aging’. Although mitochondria and peroxisomes are both needed for fatty acid metabolism, little work has focused on understanding the relationship between these two organelles including how age-dependent changes in one organelle may be detrimental for the other. Herein, we summarize findings that establish proteolytic degradation of damaged proteins by the Lon protease as a vital mechanism to maintain protein homeostasis within the peroxisome. Due to the metabolic coordination between peroxisomes and mitochondria, understanding the role of Lon in the aging peroxisome may help to elucidate cellular causes for both peroxisome and mitochondrial dysfunction.

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“…The peroxisome is important for b-oxidation of fatty acids that produce oxygen radicals and hydroperoxides (Manivannan et al 2012). In addition, ROS are generated from peroxisomes that are defective in either form or function.…”

Section: Internal Sources Of Rosmentioning

confidence: 99%

Programmed Cell Death Initiation and Execution in Budding Yeast

Strich

2015

Genetics

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Apoptosis or programmed cell death (PCD) was initially described in metazoans as a genetically controlled process leading to intracellular breakdown and engulfment by a neighboring cell . This process was distinguished from other forms of cell death like necrosis by maintenance of plasma membrane integrity prior to engulfment and the well-defined genetic system controlling this process. Apoptosis was originally described as a mechanism to reshape tissues during development. Given this context, the assumption was made that this process would not be found in simpler eukaryotes such as budding yeast. Although basic components of the apoptotic pathway were identified in yeast, initial observations suggested that it was devoid of prosurvival and prodeath regulatory proteins identified in mammalian cells. However, as apoptosis became extensively linked to the elimination of damaged cells, key PCD regulatory proteins were identified in yeast that play similar roles in mammals. This review highlights recent discoveries that have permitted information regarding PCD regulation in yeast to now inform experiments in animals.

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The Impact of Peroxisomes on Cellular Aging and Death

Cited by 47 publications

References 75 publications

Benzo(a)pyrene induces oxidative stress, pro-inflammatory cytokines, expression of nuclear factor-kappa B and deregulation of wnt/beta-catenin signaling in colons of BALB/c mice

Benzo(a)pyrene induces oxidative stress, pro-inflammatory cytokines, expression of nuclear factor-kappa B and deregulation of wnt/beta-catenin signaling in colons of BALB/c mice

The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1

Programmed Cell Death Initiation and Execution in Budding Yeast

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