2,2′,4,4′-Tetrabromodiphenyl ether disrupts spermatogenesis, impairs mitochondrial function and induces apoptosis of early leptotene spermatocytes in rats

Huang, Shaoping; Cui, Yiqiang; Guo, Xuejiang; Wang, Lei; Li, Suying; Lu, Ying; Bi, Ye; Huang, Xiaoyan; Lin, Min; Xia, Yankai; Wang, Shoulin; Wang, Xinru; Zhou, Zuomin; Sha, Jiahao

doi:10.1016/j.reprotox.2015.01.009

Cited by 27 publications

(40 citation statements)

References 43 publications

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“…Our previous study showed that Sucla2 expression decreased in rat testes with failure of spermatogenesis, and decreased in mouse spermatogonia cell line (GC1 cells) with an increase in apoptotic cells; moreover, Sucla2 was strongly expressed in spermatocytes of stages VII-XII in rat spermatogenesis [8]. Yet, whether the expression of Sucla2 in mouse testes is similar to that in rat testes is unknown; also, the function of Sucla2 in the spermatocyte is still unclear.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, proteomic analysis showed that Sucla2 is related to capacitation of boar spermatozoa [7]. In a previous study, we found that the protein level of Sucla2 was decreased in testes of rats with spermatogenesis failure, and decreased in mouse spermatogonia cell line (GC1) with increased apoptosis after exposure to the endocrine disruptor BDE47; Sucla2 is located in germ cells and is highly expressed in VII-XII stages of rat spermatogenesis [8]. This previous study indicates that Sucla2 is important during spermatogenesis, and probably plays an important role in the proliferation and apoptosis of germ cells.…”

Section: Introductionmentioning

confidence: 95%

“…The mixture was shaken at 4°C for 1 h, and the insoluble matter was removed by centrifugation at 40,000 g and 4°C for 1 hour. Protein concentrations were determined by the Bradford method using BSA as the standard [8].…”

Section: Immunohistochemistry (Ihc)mentioning

confidence: 99%

“…MMP was detected by flow cytometry using JC-1 mitochondrial potential detection kit (C2006, Beyotime Biotech, Shanghai, China) as previously indicated [8]. In brief, GC2 cells after Sucla2-targeting SiRNA transfection were incubated with JC-1 dye for 15 min in DMEM at 37°C, and then subjected to flow cytometry.…”

Section: Detection Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 99%

“…The mixture was shaken at 4°C for 1 hour, and then centrifuged at 40,000 g for 1 hour at 4°C. The supernatant was subjected to ATP measurement by luminometric methods, using an ATP assay kit (s0026, Beyotime, Shanghai, China) and a luminometer (TD-20/20, Turner Designs, Sunnyvale, CA, USA) as previously described [8]. ATP levels were also normalized to protein level to exclude the effect of the weight of the cell proteins.…”

Section: Detection Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 99%

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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: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

Section: Immunohistochemistry (Ihc)mentioning

confidence: 99%

Section: Detection Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 99%

Section: Detection Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 99%

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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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Amodiaquine‐induced reproductive toxicity in adult male rats

Niu

Wei

et al. 2015

Molecular Reproduction Devel

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Amodiaquine (AQ) is routinely prescribed as an anti-malarial drug. Here, we evaluated AQ-induced toxicity in the male reproductive system. Eighty adult male Sprague-Dawley rats were randomly divided into four groups that received distilled water (control) or daily doses of 5 mg/kg body weight, 10 mg/kg, or 15 mg/kg AQ for 2 weeks. Testes morphology was analyzed using hematoxylin-and-eosin staining, terminal dUTP nicked-end labeling (TUNEL), and immunostaining whereas protein expression was determined by Western blotting. AQ dose-dependently led to abnormal spermatogenesis. Disruption of the blood-testis barrier and increased germ cell apoptosis were observed in all three AQ-treated groups. Interestingly, AQ-induced damage of spermatogenesis recovered over time, based on the survival of promyelocytic leukemia zinc-finger (PLZF)-positive, undifferentiated spermatogonia. Serum levels of luteinizing hormone and testosterone, as well as testicular testosterone levels, were not significantly altered in AQ-treated groups compared with controls. Collectively, our study suggests that AQ exerts substantial acute side effects on the reproductive systems of adult male rats by inducing the apoptosis of differentiating spermatogenic cells and disruption of blood-testis barrier function.

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Key proteins of proteome underlying sperm malformation of rats exposed to low fenvalerate doses are highly related to P53

Huang

et al. 2021

Environmental Toxicology

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Fenvalerate (Fen) is an endocrine disruptor, capable of interfering with the activity of estrogen and androgen. Our objective was to explore the molecular mechanisms of Fen on sperm in vivo. Adult male Sprague-Dawley rats were orally exposed to 0, 0.00625, 0.125, 2.5, 30 mg/kg/day Fen for 8 weeks. Sperm morphology, differential proteomics of sperm and testes, bioinformatic analysis, western blotting (WB), and RT-PCR were used to explore the mechanism of Fen on sperm. Data showed that low Fen doses significantly induced sperm malformations. In sperm proteomics, 47 differentially expressed (DE) proteins were enriched in biological processes (BPs) related to energy metabolism, response to estrogen, spermatogenesis; and enriched in cellular components (CCs) relating to energy-metabolism, sperm fibrous sheath and their outer dense fibers. In testicular proteomics, 56 DE proteins were highly associated with mRNA splicing, energy metabolism; and enriched in CCs relating to vesicles, myelin sheath, microtubules, mitochondria.WB showed that the expression of selected proteins was identical to their tendency in 2D gels. Literature indicates that key DE proteins in proteomic profiles (such as Trap1, Hnrnpa2b1, Hnrnpk, Hspa8, and Gapdh) are involved in P53-related processes or morphogenesis or spermatogenesis. Also, P53 mRNA and protein levels were significantly increased by Fen; bioinformatic re-analysis showed that 88.5% DE proteins and P53 formed a complex interacting network, and the key DE proteins were coenriched with P53-related BPs. Results indicate that key DE proteins of proteome underlying sperm malformations of rats exposed to low Fen doses are highly related to P53.

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2,2′,4,4′-Tetrabromodiphenyl ether disrupts spermatogenesis, impairs mitochondrial function and induces apoptosis of early leptotene spermatocytes in rats

Cited by 27 publications

References 43 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

Amodiaquine‐induced reproductive toxicity in adult male rats

Key proteins of proteome underlying sperm malformation of rats exposed to low fenvalerate doses are highly related to P53

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