Mitochondria, Energetics, Epigenetics, and Cellular Responses to Stress

Shaughnessy, Daniel T.; McAllister, Kimberly A.; Worth, Leroy; Haugen, Astrid C.; Meyer, Joel N.; Domann, Frederick E.; Houten, Bennett Van; Mostoslavsky, Raúl; Bultman, Scott J.; Baccarelli, Andrea; Begley, Thomas J.; Sobol, Robert W.; Hirschey, Matthew D.; Ideker, Trey; Santos, Janine H.; Copeland, William C.; Tice, Raymond R.; Balshaw, David M.; Tyson, Frederick L.

doi:10.1289/ehp.1408418

Cited by 228 publications

(173 citation statements)

References 103 publications

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“…Mitochondria are multitasking organelles [28], and many environmental and stress stimuli can cause mitochondrial dysfunction [29,30], thereby affecting spermatogenesis [31][32][33][34]. The present study is a follow-up to our previous works, which showed that Sucla2 expression decreased in testes and GC1 cells with increasing apoptotic cells after exposure to endocrine disruptor BDE47 [8].…”

Section: Discussionsupporting

confidence: 73%

Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells

Huang

Wang

2016

Folia Histochem Cytobiol.

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Introduction. Sucla2, a b subunit of succinyl coenzyme A synthase, is located in the mitochondrial matrix. Sucla2 catalyzes the reversible synthesis of succinate and adenosine triphosphate (ATP) in the tricarboxylic acid cycle. Sucla2 expression was found to be correlated with the capacitation of boar spermatozoa. We have previously reported that Sucla2 was decreased in the testes of rats with spermatogenesis failure after exposure to endocrine disruptor BDE47. Yet, the expression model of Sucla2 in spermatogenesis and the function of Sucla2 in spermatogenic cells are still unclear. Our objective was to explore the localization of Sucla2 during mouse spermatogenesis and its function in the mouse spermatocyte line (GC2). Material and methods. The localization of Sucla2 in the mouse testis was explored through immunohistochemistry (IHC). Sucla2 was knocked down in GC2 cells and its expression was detected by Western blot (WB) to verify the efficiency of the siRNA transfection. Mitochondrial membrane potential (MMP), apoptosis and ROS of GC2 were detected by flow cytometry. ATP production was measured by the luminometric method and the presence of Bcl2 of GC2 was detected by WB. Results. Sucla2 is highly expressed in all germ cells but not in interstitial cells. Coarse Sucla2 signals are found in spermatocytes in stages VII-XII of mouse spermatogenesis. In GC2 cells, knockdown of Sucla2 decreased cell viability and MMP, induced apoptosis of GC2 cells, decreased ATP production, and Bcl2 expression, and increased ROS levels. Conclusions. Sucla2 is related to the developmental stages of mouse spermatogenesis. Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis via decreased mitochondrial function of the cells.

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Section: Discussionsupporting

confidence: 73%

Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells

Huang

Wang

2016

Folia Histochem Cytobiol.

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“…Mitochondria are dynamic organelles involved in a wide range of processes, such as ATP generation, cell death, immune signaling, chemotaxis, and calcium homeostasis (48). These organelles also play a central role in phospholipid metabolism and lipid exchange with the ER (49,50).…”

Section: Resultsmentioning

confidence: 99%

Neospora caninum Recruits Host Cell Structures to Its Parasitophorous Vacuole and Salvages Lipids from Organelles

et al. 2015

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Toxoplasma gondii and Neospora caninum, which cause the diseases toxoplasmosis and neosporosis, respectively, are two closely related apicomplexan parasites. They have similar heteroxenous life cycles and conserved genomes and share many metabolic features. Despite these similarities, T. gondii and N. caninum differ in their transmission strategies and zoonotic potential. Comparative analyses of the two parasites are important to identify the unique biological features that underlie the basis of host preference and pathogenicity. T. gondii and N. caninum are obligate intravacuolar parasites; in contrast to T. gondii, events that occur during N. caninum infection remain largely uncharacterized. We examined the capability of N. caninum (Liverpool isolate) to interact with host organelles and scavenge nutrients in comparison to that of T. gondii (RH strain). N. caninum reorganizes the host microtubular cytoskeleton and attracts endoplasmic reticulum (ER), mitochondria, lysosomes, multivesicular bodies, and Golgi vesicles to its vacuole though with some notable differences from T. gondii. For example, the host ER gathers around the N. caninum parasitophorous vacuole (PV) but does not physically associate with the vacuolar membrane; the host Golgi apparatus surrounds the N. caninum PV but does not fragment into ministacks. N. caninum relies on plasma lipoproteins and scavenges cholesterol from NPC1-containing endocytic organelles. This parasite salvages sphingolipids from host Golgi Rab14 vesicles that it sequesters into its vacuole. Our data highlight a remarkable degree of conservation in the intracellular infection program of N. caninum and T. gondii. The minor differences between the two parasites related to the recruitment and rearrangement of host organelles around their vacuoles likely reflect divergent evolutionary paths.

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“…Considering its importance in modulating growth factor downstream pathways, we surmised that AQP8-dependent H 2 O 2 transport could be fine-tuned during stress conditions known to entail the production of ROS (51,52). Accordingly, we found that diverse cellular stresses reversibly inhibit AQP8-dependent transport, impacting cell growth and survival.…”

Section: Innovationmentioning

confidence: 96%

Stress Regulates Aquaporin-8 Permeability to Impact Cell Growth and Survival

Medraño-Fernández

Bestetti

Bertolotti

et al. 2016

Antioxidants & Redox Signaling

109

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Aquaporin-8 (AQP8) allows the bidirectional transport of water and hydrogen peroxide across biological membranes. Depending on its concentration, H 2 O 2 exerts opposite roles, amplifying growth factor signaling in physiological conditions, but causing severe cell damage when in excess. Thus, H 2 O 2 permeability is likely to be tightly controlled in living cells. Aims: In this study, we investigated whether and how the transport of H 2 O 2 through plasma membrane AQP8 is regulated, particularly during cell stress. Results: We show that diverse cellular stress conditions, including heat, hypoxia, and ER stress, reversibly inhibit the permeability of AQP8 to H 2 O 2 and water. Preventing the accumulation of intracellular reactive oxygen species (ROS) during stress counteracts AQP8 blockade. Once inhibition is established, AQP8-dependent transport can be rescued by reducing agents. Neither H 2 O 2 nor water transport is impaired in stressed cells expressing a mutant AQP8, in which cysteine 53 had been replaced by serine. Cells expressing this mutant are more resistant to stress-, drug-, and radiation-induced growth arrest and death. Innovation and Conclusion: The control of AQP8-mediated H 2 O 2 transport provides a novel mechanism to regulate cell signaling and survival during stress. Antioxid.

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Mitochondria, Energetics, Epigenetics, and Cellular Responses to Stress

Cited by 228 publications

References 103 publications

Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells

Knockdown of Sucla2 decreases the viability of mouse spermatocytes by inducing apoptosis through injury of the mitochondrial function of cells

Neospora caninum Recruits Host Cell Structures to Its Parasitophorous Vacuole and Salvages Lipids from Organelles

Stress Regulates Aquaporin-8 Permeability to Impact Cell Growth and Survival

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