Effect of resveratrol on Sertoli cell proliferation

Gorga, Agostina; Rindone, Gustavo Marcelo; Regueira, Mariana; Pellizzari, Eliana Herminia; Camberos, María del Carmen; Cigorraga, Selva Beatriz; Riera, María Fernanda; Galardo, Maria Noel Lujan; Meroni, Silvina Beatriz

doi:10.1002/jcb.27350

Cited by 6 publications

(3 citation statements)

References 54 publications

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“…On the other hand, the cell cycle inhibitor p21 is involved in cell cycle arrest and in the maturation of Sertoli cells. Retinoic acid, the thyroid hormones, and signaling proteins such as AMPK and Sirtuin 1 increase p21 expression as part of their anti‐proliferative action 24,40,41 . In the present study, we show that Sertoli cells isolated from metformin‐treated animals present reduced Ccnd1 and Ccne2 mRNA levels and increased Cdkn1a mRNA levels.…”

Section: Discussionsupporting

confidence: 56%

Postnatal metformin treatment alters rat Sertoli cell proliferation and daily sperm production

et al. 2021

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Background The direct correlation between Sertoli cell number and sperm production capacity highlights the importance of deciphering external factors that modify Sertoli cell proliferation. A growing body of evidence in vitro suggests that metformin, the main pharmacological agent for type 2 diabetes treatment in children, exerts anti‐proliferative effects on Sertoli cells. Objective The aims of this study were to investigate the effect of metformin administration during postnatal period on Sertoli cell proliferation and on cell cycle regulators expression and to analyze the impact of this treatment on the sperm production capacity in adulthood. Materials and Methods Sprague Dawley rat pups were randomly divided into two groups: MET (receiving daily 200 mg/kg metformin, from Pnd3 to Pnd7 inclusive) and control (receiving vehicle). BrdU incorporation was measured to assess proliferation. Gene expression analyses were performed in Sertoli cells isolated from animals of both groups. Daily sperm production and sperm parameters were measured in adult male rats (Pnd90) that received neonatal treatment. Results MET group exhibited a significant decrease in BrdU incorporation in Sertoli cells. Concordantly, MET group showed a reduction in cyclin D1 and E2 expression and an increase in p21 expression in Sertoli cells. In addition, metformin‐treated animals displayed lower values of daily sperm production on Pnd90. Discussion and Conclusion These results suggest that metformin treatment may lead to a decrease in Sertoli cell proliferation, a concomitant altered expression of cell cycle regulators and ultimately, a reduction in daily sperm production in adult animals.

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Section: Discussionsupporting

confidence: 56%

Postnatal metformin treatment alters rat Sertoli cell proliferation and daily sperm production

et al. 2021

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“…Activation of SIRT1 decreased cyclin D1 and D2 levels and increased p21Cip1 mRNA levels. SIRT1 activation also decreased c-Myc transcriptional activity (189). Remarkably, TH regulate SIRT1 expression and activity in different experimental models (190–192).…”

Section: Main Factors Involved In Cessation Of Proliferation and In Mmentioning

confidence: 99%

Molecular Mechanisms and Signaling Pathways Involved in Sertoli Cell Proliferation

et al. 2019

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Sertoli cells are somatic cells present in seminiferous tubules which have essential roles in regulating spermatogenesis. Considering that each Sertoli cell is able to support a limited number of germ cells, the final number of Sertoli cells reached during the proliferative period determines sperm production capacity. Only immature Sertoli cells, which have not established the blood-testis barrier, proliferate. A number of hormonal cues regulate Sertoli cell proliferation. Among them, FSH, the insulin family of growth factors, activin, and cytokines action must be highlighted. It has been demonstrated that cAMP/PKA, ERK1/2, PI3K/Akt, and mTORC1/p70SK6 pathways are the main signal transduction pathways involved in Sertoli cell proliferation. Additionally, c-Myc and hypoxia inducible factor are transcription factors which participate in the induction by FSH of various genes of relevance in cell cycle progression. Cessation of proliferation is a pre-requisite to Sertoli cell maturation accompanied by the establishment of the blood-testis barrier. With respect to this barrier, the participation of androgens, estrogens, thyroid hormones, retinoic acid and opioids has been reported. Additionally, two central enzymes that are involved in sensing cell energy status have been associated with the suppression of Sertoli cell proliferation, namely AMPK and Sirtuin 1 (SIRT1). Among the molecular mechanisms involved in the cessation of proliferation and in the maturation of Sertoli cells, it is worth mentioning the up-regulation of the cell cycle inhibitors p21Cip1, p27Kip, and p19INK4, and of the gap junction protein connexin 43. A decrease in Sertoli cell proliferation due to administration of certain therapeutic drugs and exposure to xenobiotic agents before puberty has been experimentally demonstrated. This review focuses on the hormones, locally produced factors, signal transduction pathways, and molecular mechanisms controlling Sertoli cell proliferation and maturation. The comprehension of how the final number of Sertoli cells in adulthood is established constitutes a pre-requisite to understand the underlying causes responsible for the progressive decrease in sperm production that has been observed during the last 50 years in humans.

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“…Liu et al reported that the administration of resveratrol could ameliorate Microcystin‐leucine arginine‐induced Sertoli cell apoptosis (Liu et al, 2018). Noteworthy, Sirt1‐knockout animals are infertile (Gorga et al, 2018). Also, the deficiency of SIRT1 in yak testis caused the impairment of testicular development (Yin et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Cordycepin, a major bioactive component ofCordyceps militaris, ameliorates diabetes‐induced testicular damage through the Sirt1/Foxo3a pathway

Huang

Zhou

et al. 2021

Andrologia

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Diabetes‐induced male dysfunction is considered as a worldwide challenge, and testicular damage mainly caused by oxidative stress is its most common manifestation. Cordycepin, a natural antioxidant, has been used in the treatment of diabetic complications. However, the protective action and underlying mechanism of cordycepin on hyperglycaemia‐induced testicular damage are unclear. This study aimed to investigate the protective effects and molecular mechanisms of cordycepin against diabetes‐induced testicular damage. The type 2 diabetes model was established in C57BL/6 male mice via high‐fat diet for 4 weeks and injected intraperitoneally with 50 mg/kg/day streptozotocin for five consecutive days. Then mice were treated with cordycepin (10 and 20 mg/kg, respectively) for 8 weeks. At the end of experiment, biochemical indicators, microstructure of testicular tissue, sperm morphology, TUNEL staining and protein expressions were evaluated. In the present study, cordycepin alleviated the testicular damage, restored disruption of the blood‐testis barrier, and improved spermatogenic function via the antiapoptotic and antioxidant capacity. Mechanistically, cordycepin significantly enhanced SIRT1 expression and triggered the activity of Foxo3a, further to induce the expression of its downstream antioxidant enzymes, including Mn‐SOD and CAT. These findings indicated that cordycepin could improve hyperglycaemia‐induced testicular damage by regulating downstream antioxidant enzymes activity through the SIRT1/Foxo3a signalling pathway.

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Effect of resveratrol on Sertoli cell proliferation

Cited by 6 publications

References 54 publications

Postnatal metformin treatment alters rat Sertoli cell proliferation and daily sperm production

Postnatal metformin treatment alters rat Sertoli cell proliferation and daily sperm production

Molecular Mechanisms and Signaling Pathways Involved in Sertoli Cell Proliferation

Cordycepin, a major bioactive component ofCordyceps militaris, ameliorates diabetes‐induced testicular damage through the Sirt1/Foxo3a pathway

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