The peroxisome: an update on mysteries

Islinger, Markus; Grille, Sandra; Fahimi, H. Dariush; Schrader, Michael

doi:10.1007/s00418-012-0941-4

Cited by 195 publications

(99 citation statements)

References 334 publications

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“…Interestingly, mitochondrial and peroxisomal fission machineries share some core components, such as FIS1 homolog (reviewed in Ref. 81), the expression of which in human sperm is shown in the present study for the first time. Moreover, there is active vesicular trafficking between mitochondria and peroxisomes.…”

Section: Discussionmentioning

confidence: 67%

Human Sperm Tail Proteome Suggests New Endogenous Metabolic Pathways

Amaral

Castillo

Estanyol

et al. 2013

Molecular & Cellular Proteomics

207

177

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Proteomic studies are contributing greatly to our understanding of the sperm cell, and more detailed descriptions are expected to clarify additional cellular and molecular sperm attributes. The aim of this study was to characterize the subcellular proteome of the human sperm tail and, hopefully, identify less concentrated proteins (not found in whole cell proteome studies). Specifically, we were interested in characterizing the sperm metabolic proteome and gaining new insights into the sperm metabolism issue. Sperm were isolated from normozoospermic semen samples and depleted of any contaminating leukocytes. Tail fractions were obtained by means of sonication followed by sucrose-gradient ultracentrifugation, and their purity was confirmed via various techniques. Liquid chromatography and tandem mass spectrometry of isolated sperm tail peptides resulted in the identification of 1049 proteins, more than half of which had not been previously described in human sperm. The categorization of proteins according to their function revealed two main groups: proteins related to metabolism and energy production (26%), and proteins related to sperm tail structure and motility (11%). Interestingly, a great proportion of the metabolic proteome (24%) comprised enzymes involved in lipid metabolism, including enzymes for mitochondrial beta-oxidation. Unexpectedly, we also identified various peroxisomal proteins, some of which are known to be involved in the oxidation of very long chain fatty acids. Analysis of our data using Reactome suggests that both mitochondrial and peroxisomal pathways might indeed be active in sperm, and that the use of fatty acids as fuel might be more preponderant than previously thought. In addition, incubation of sperm with the fatty acid oxidation inhibitor etomoxir resulted in a significant decrease in sperm motility. Contradicting a common concept in the literature, we suggest that the male gamete might have the capacity to obtain energy from endogenous pools, and thus to adapt to putative exogenous fluctuations. Molecular &

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Section: Discussionmentioning

confidence: 67%

Human Sperm Tail Proteome Suggests New Endogenous Metabolic Pathways

Amaral

Castillo

Estanyol

et al. 2013

Molecular & Cellular Proteomics

207

177

View full text Add to dashboard Cite

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“…It is not surprising therefore that malfunction of peroxisomes leads to peroxisome-specific diseases (Braverman et al, 2013;Weller et al, 2003) and contributes to the pathology of Alzheimer's and Parkinson's diseases, aging, cancer, type 2 diabetes and heart failure (Beach et al, 2012;Colasante et al, 2015;Fransen et al, 2013;Islinger et al, 2012;Trompier et al, 2014). A useful distinction divides peroxisomal diseases into two groups: those in which single enzymatic functions are defective, and those where peroxisome biogenesis is defective per se.…”

Section: Introductionmentioning

confidence: 99%

Pex35 is a regulator of peroxisome abundance

Yofe

Soliman

Chuartzman

et al. 2017

Journal of Cell Science

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Peroxisomes are cellular organelles with vital functions in lipid, amino acid and redox metabolism. The cellular formation and dynamics of peroxisomes are governed by PEX genes; however, the regulation of peroxisome abundance is still poorly understood. Here, we use a high-content microscopy screen in Saccharomyces cerevisiae to identify new regulators of peroxisome size and abundance. Our screen led to the identification of a previously uncharacterized gene, which we term PEX35, which affects peroxisome abundance. PEX35 encodes a peroxisomal membrane protein, a remote homolog to several curvature-generating human proteins. We systematically characterized the genetic and physical interactome as well as the metabolome of mutants in PEX35, and we found that Pex35 functionally interacts with the vesicle-budding-inducer Arf1. Our results highlight the functional interaction between peroxisomes and the secretory pathway.

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“…Despite their simple architecture, peroxisomes are important organelles that display an unprecedented diversity of functions depending on metabolic needs and external stimuli (8). They are crucial in man, manifested by the presence various inherited disorders (i.e.…”

mentioning

confidence: 99%

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Bartoszewska

Williams

Kikhney

et al. 2012

Journal of Biological Chemistry

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Background: A putative Lon protease has been identified in peroxisomes of various species (Pln). Results: Pln is an ATP-dependent protease that digests unfolded substrates e.g. oxidatively damaged catalase-peroxidase, and displays chaperone-like activity, circumventing accumulation of protein aggregates in peroxisomes that compromise organelle function. Conclusion: Pln is a bifunctional protein with chaperone and protease activities. Significance: Pln is crucial for peroxisome proteostasis.

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The peroxisome: an update on mysteries

Cited by 195 publications

References 334 publications

Human Sperm Tail Proteome Suggests New Endogenous Metabolic Pathways

Human Sperm Tail Proteome Suggests New Endogenous Metabolic Pathways

Pex35 is a regulator of peroxisome abundance

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

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