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Artykuły w czasopismach na temat „Sertoli cells Physiology”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 28 stycznia 2023

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1

de, Kretser DM. "Germ cell-Sertoli cell interactions." Reproduction, Fertility and Development 2, no. 3 (1990): 225. http://dx.doi.org/10.1071/rd9900225.

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The interactions between the Sertoli cells and germ cells are progressively becoming an important part of testicular physiology. This paper explores the cytological basis for these interactions, detailing the cyclic changes in the Sertoli cells in concert with the stages of the seminiferous cycle and the nature of the blood-testis barrier. These cytological changes are correlated with a number of variations in the function of Sertoli cells. The mechanisms by which germ cells and Sertoli cells interact are explored and can be divided into those using cell-to-cell contact and others utilizing pa

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2

Maqdasy, Salwan, Fatim-Zohra El Hajjaji, Marine Baptissart, Emilie Viennois, Abdelkader Oumeddour, Florence Brugnon, Amalia Trousson та ін. "Identification of the Functions of Liver X Receptor-β in Sertoli Cells Using a Targeted Expression-Rescue Model". Endocrinology 156, № 12 (24 вересня 2015): 4545–57. http://dx.doi.org/10.1210/en.2015-1382.

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Liver X receptors (LXRs) are key regulators of lipid homeostasis and are involved in multiple testicular functions. The Lxrα−/−;Lxrβ−/− mice have illuminated the roles of both isoforms in maintenance of the epithelium in the seminiferous tubules, spermatogenesis, and T production. The requirement for LXRβ in Sertoli cells have been emphasized by early abnormal cholesteryl ester accumulation in the Lxrβ−/− and Lxrα−/−;Lxrβ−/− mice. Other phenotypes, such as germ cell loss and hypogonadism, occur later in life in the Lxrα−/−;Lxrβ−/− mice. Thus, LXRβ expression in Sertoli cells seems to be essent

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3

Pelletier, R. Marc, Casimir D. Akpovi, Li Chen, Robert Day, and María L. Vitale. "CX43 expression, phosphorylation, and distribution in the normal and autoimmune orchitic testis with a look at gap junctions joining germ cell to germ cell." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 300, no. 1 (January 2011): R121—R139. http://dx.doi.org/10.1152/ajpregu.00500.2010.

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Spermatogenesis requires connexin 43 (Cx43).This study examines normal gene transcription, translation, and phosphorylation of Cx43 to define its role on germ cell growth and Sertoli cell's differentiation, and identifies abnormalities arising from spontaneous autoimmune orchitis (AIO) in mink, a seasonal breeder and a natural model for autoimmunity. Northern blot analysis detected 2.8- and a 3.7-kb Cx43 mRNA bands in seminiferous tubule-enriched fractions. Cx43 mRNA increased in seminiferous tubule-enriched fractions throughout development and then seasonally with the completion of spermatoge

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4

Benahmed, M., J. Reventos, E. Tabone, and J. M. Saez. "Cultured Sertoli cell-mediated FSH stimulatory effect on Leydig cell steroidogenesis." American Journal of Physiology-Endocrinology and Metabolism 248, no. 2 (February 1, 1985): E176—E181. http://dx.doi.org/10.1152/ajpendo.1985.248.2.e176.

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To determine the precise role of Sertoli cells in the stimulating effects of follicle stimulating hormone (FSH) on Leydig cell activity, porcine purified Leydig and Sertoli cells were cultured separately or together in a chemically defined medium in the absence or presence of porcine, FSH 50 ng/ml. Leydig cell activity was evaluated using two parameters: human chorionic gonadotropin (hCG) binding sites; and hCG-stimulated cAMP production and testosterone secretion. First, it was found that FSH increases Leydig cell activity in crude Leydig cell preparations (40–60% of Leydig cells), whereas it

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5

Froment, P., M. Vigier, D. Nègre, I. Fontaine, J. Beghelli, F. L. Cosset, M. Holzenberger, and P. Durand. "Inactivation of the IGF-I receptor gene in primary Sertoli cells highlights the autocrine effects of IGF-I." Journal of Endocrinology 194, no. 3 (September 2007): 557–68. http://dx.doi.org/10.1677/joe-07-0258.

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IGF-I regulates pituitaryand gonadal functions, and is pivotal for sexual development and fertility in mammalian species. To better understand the function of autocrine IGF-I in Sertoli cell physiology, we established a system for Cre-mediated conditional inactivation of the IGF-I receptor (IGF-IR) in cultured Sertoli cells. We show here that loss of IGF-IR decreased the number of viable Sertoli cells as a consequence of diminished Sertoli cell proliferation and increased Sertoli cell death. Furthermore, the lack of IGF-IR altered the morphology of cultured Sertoli cells and decreased lactate

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6

Renier, G., J. Gaulin, W. Gibb, R. Collu, and J. R. Ducharme. "Effect of catecholamines on porcine Sertoli and Leydig cells in primary culture." Canadian Journal of Physiology and Pharmacology 65, no. 10 (October 1, 1987): 2053–58. http://dx.doi.org/10.1139/y87-321.

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The accumulation by purified immature porcine Leydig and Sertoli cells of cyclic adenosine 3′,5′-monophosphate in the presence of 1-methyl-3-isobuthylxathine was studied and their respective testosterone and 17β-estradiol production in response to catecholamines was assessed in vitro. These substances increased both basal and FSH-stimulated cyclic adenosine 3′,5′-monophosphate accumulation in Sertoli cells. In contrast, catecholamines slightly enhanced basal cyclic adenosine 3′,5′-monophosphate production but inhibited its human chorionic gonadotropin-stimulated accumulation by Leydig cells. C

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7

Moroi, Seiji, Mitinori Saitou, Kazushi Fujimoto, Akira Sakakibara, Mikio Furuse, Osamu Yoshida, and Shoichiro Tsukita. "Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes." American Journal of Physiology-Cell Physiology 274, no. 6 (June 1, 1998): C1708—C1717. http://dx.doi.org/10.1152/ajpcell.1998.274.6.c1708.

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Occludin is the only integral membrane protein identified to date as a component of tight junctions (TJs). Here, we examined the distribution and expression of occludin in murine testis bearing well-developed TJ. In the adult mouse testis, occludin was concentrated at TJ strands, which are located at the most basal regions of lateral membranes of Sertoli cells. In immunoblotting, occludin showed a characteristic multiple banding pattern, suggesting that occludin is highly phosphorylated in the testis. In 1-wk-old mouse testis, occludin was distributed diffusely at the lateral membranes of Sert

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8

Fantoni, G., P. L. Morris, G. Forti, G. B. Vannelli, C. Orlando, T. Barni, R. Sestini, G. Danza, and M. Maggi. "Endothelin-1: a new autocrine/paracrine factor in rat testis." American Journal of Physiology-Endocrinology and Metabolism 265, no. 2 (August 1, 1993): E267—E274. http://dx.doi.org/10.1152/ajpendo.1993.265.2.e267.

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Cultured Sertoli cells of 20-day-old rats were found to produce and release endothelin-1-like immunoreactivity (ET-1-LI) under follicle-stimulating hormone control. The elution profile of ET-1-LI from extracts of spent Sertoli cell culture medium corresponds to that of synthetic ET-1, suggesting a testicular production of authentic ET-1. In contrast, the conditioned medium from rat Leydig cells did not contain ET-1-LI. Immunohistochemical studies confirmed that, in 20-day-old rats, the positive staining was confined to some Sertoli cells, whereas interstitial cells were negative. In the adult

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9

Allan, Charles M., Patrick Lim, Mathew Robson, Jenny Spaliviero, and David J. Handelsman. "Transgenic mutant D567G but not wild-type human FSH receptor overexpression provides FSH-independent and promiscuous glycoprotein hormone Sertoli cell signaling." American Journal of Physiology-Endocrinology and Metabolism 296, no. 5 (May 2009): E1022—E1028. http://dx.doi.org/10.1152/ajpendo.90941.2008.

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We have characterized the in vivo actions of human wild-type FSH receptor (FSHR) overexpressed in Sertoli cells of transgenic (Tg) mice ( TgFSHRwt) compared with transgenic overexpression of the human activated mutant FSHR*D567G ( TgFSHR*D567G). Testicular TgFSHRwt expression significantly elevated specific FSH binding (>2-fold, P < 0.01) relative to nontransgenic testes, similar to increased FSH binding in TgFSHR*D567G testes. Isolated TgFSHRwt Sertoli cells exhibited higher FSH-stimulated cAMP levels compared with non- Tg or TgFSHR*D567G cells but did not display the elevated FSH-indep

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10

Riera, María F., María N. Galardo, Eliana H. Pellizzari, Silvina B. Meroni, and Selva B. Cigorraga. "Molecular mechanisms involved in Sertoli cell adaptation to glucose deprivation." American Journal of Physiology-Endocrinology and Metabolism 297, no. 4 (October 2009): E907—E914. http://dx.doi.org/10.1152/ajpendo.00235.2009.

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Sertoli cells provide the physical support and the necessary environment for germ cell development. Among the products secreted by Sertoli cells, lactate, the preferred energy substrate for spermatocytes and spermatids, is present. Considering the essential role of lactate on germ cell metabolism, it is supposed that Sertoli cells must ensure its production even in adverse conditions, such as those that would result from a decrease in glucose levels in the extracellular milieu. The aim of the present study was to investigate 1) a possible effect of glucose deprivation on glucose uptake and on

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11

Kongmanas, Kessiri, Arpornrad Saewu, Wongsakorn Kiattiburut, Mark A. Baker, Kym F. Faull, Dylan Burger, and Nongnuj Tanphaichitr. "Accumulation of Seminolipid in Sertoli Cells Is Associated with Increased Levels of Reactive Oxygen Species and Male Subfertility: Studies in Aging Arsa Null Male Mice." Antioxidants 10, no. 6 (June 4, 2021): 912. http://dx.doi.org/10.3390/antiox10060912.

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Seminolipid (also known as sulfogalactosylglycerolipid-SGG), present selectively in male germ cells, plays important roles in spermatogenesis and sperm–egg interaction. The proper degradation of SGG in apoptotic germ cells is also as important. Sertoli cells first phagocytose apoptotic germ cells, then Sertoli lysosomal arylsulfatase A (ARSA) desulfates SGG, the first step of SGG degradation. We have reported that aging male Arsa−/− mice become subfertile with SGG accumulation in Sertoli cell lysosomes, typical of a lysosomal storage disorder (LSD). Since reactive oxygen species (ROS) levels a

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12

Kato, Ryo, Tomoji Maeda, Toshihiro Akaike, and Ikumi Tamai. "Characterization of novel Na+-dependent nucleobase transport systems at the blood-testis barrier." American Journal of Physiology-Endocrinology and Metabolism 290, no. 5 (May 2006): E968—E975. http://dx.doi.org/10.1152/ajpendo.00160.2005.

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In the testis, nucleosides and nucleobases are important substrates of the salvage pathway for nucleotide biosynthesis, and one of the roles of Sertoli cells is to provide nutrients and metabolic precursors to spermatogenic cells located within the blood-testis barrier (BTB). We have already shown that concentrative and equilibrative nucleoside transporters are expressed and are functional in primary-cultured rat Sertoli cells as a BTB model, but little is known about nucleobase transport at the BTB or about the genes encoding specific nucleobase transporters in mammalian cells. In the present

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13

Eusebi, Fabrizio, Francesca Grassi, Guiseppe Fratamico, Susanna Dolci, Marco Conti, and Mario Stefanini. "Cell-to-cell communication in cultured Sertoli cells." Pfl�gers Archiv European Journal of Physiology 404, no. 4 (August 1985): 382–84. http://dx.doi.org/10.1007/bf00585353.

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Domanskyi, Andrii, Fu-Ping Zhang, Mirja Nurmio, Jorma J. Palvimo, Jorma Toppari, and Olli A. Jänne. "Expression and localization of androgen receptor-interacting protein-4 in the testis." American Journal of Physiology-Endocrinology and Metabolism 292, no. 2 (February 2007): E513—E522. http://dx.doi.org/10.1152/ajpendo.00287.2006.

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Androgen receptor-interacting protein 4 (ARIP4) belongs to the SNF2 family of proteins involved in chromatin remodeling, DNA excision repair, and homologous recombination. It is a DNA-dependent ATPase, binds to DNA and mononucleosomes, and interacts with androgen receptor (AR) and modulates AR-dependent transactivation. We have examined in this study the expression and cellular localization of ARIP4 during postnatal development of mouse testis. ARIP4 was detected by immunohistochemistry in Sertoli cell nuclei at all ages studied, starting on day 5, and exhibited the highest expression level in

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15

Veitinger, Sophie, Thomas Veitinger, Silvia Cainarca, Daniela Fluegge, Corinna H. Engelhardt, Stefan Lohmer, Hanns Hatt, et al. "Purinergic signalling mobilizes mitochondrial Ca2+in mouse Sertoli cells." Journal of Physiology 589, no. 21 (October 28, 2011): 5033–55. http://dx.doi.org/10.1113/jphysiol.2011.216309.

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16

Cheng, C. Yan, and Dolores D. Mruk. "Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development." Physiological Reviews 82, no. 4 (January 10, 2002): 825–74. http://dx.doi.org/10.1152/physrev.00009.2002.

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Spermatogenesis is an intriguing but complicated biological process. However, many studies since the 1960s have focused either on the hormonal events of the hypothalamus-pituitary-testicular axis or morphological events that take place in the seminiferous epithelium. Recent advances in biochemistry, cell biology, and molecular biology have shifted attention to understanding some of the key events that regulate spermatogenesis, such as germ cell apoptosis, cell cycle regulation, Sertoli-germ cell communication, and junction dynamics. In this review, we discuss the physiology and biology of junc

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17

Oliveira, P. F., M. Sousa, A. Barros, T. Moura, and A. Rebelo da Costa. "Intracellular pH regulation in human Sertoli cells: role of membrane transporters." REPRODUCTION 137, no. 2 (February 2009): 353–59. http://dx.doi.org/10.1530/rep-08-0363.

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Sertoli cells are responsible for regulating a wide range of processes that lead to the differentiation of male germ cells into spermatozoa. Intracellular pH (pHi) is an important parameter in cell physiology regulating namely cell metabolism and differentiation. However, pHi regulation mechanisms in Sertoli cells have not yet been systematically elucidated. In this work, pHi was determined in primary cultures of human Sertoli cells. Sertoli cells were exposed to weak acids, which caused a rapid acidification of the intracellular milieu. pHi then recovered by a mechanism that was shown to be p

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18

Deng, Qiong, Chihua He, Yong Wu, Jianwen Zhang, Ying Zhang, Zhu Wang, Hui Liang, and Fei Yang. "CSN6 and Rab34 Are Involved in Androgen Receptor Trafficking in Mouse Testicular Sertoli Cells." Cellular Physiology and Biochemistry 47, no. 6 (2018): 2360–68. http://dx.doi.org/10.1159/000491608.

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Background/Aims: Androgen and its receptor (AR) play an important role in maintaining spermatogenesis and male fertility. Our previous studies showed that testosterone at a physiological concentration induces cytoplasmic AR translocation to the Sertoli cell plasma membrane of within 5 minutes. Methods: In this study, mass spectrometry (MS) and bioinformatic analyses were applied to identify candidate proteins mediating AR trafficking. The candidate proteins were knocked down by shRNA transfection. Results: Nine candidate proteins were identified by MS. The data was verified by co-immunoprecipi

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Trejo, Raquel, Alicia Valadéz-Salazar, and Graciela Delhumeau. "Effects of quercetin on rat testis aerobic glycolysis." Canadian Journal of Physiology and Pharmacology 73, no. 11 (November 1, 1995): 1605–15. http://dx.doi.org/10.1139/y95-722.

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Lactate production by testicular fragments and isolated germinal cells at various stages of spermatogenesis was studied in aerobic and anerobic conditions. Several ATPase inhibitors were used to determine the role of ATPase activities in the control of aerobic lactate production. Aerobic glycolysis reached a high level in spermatogonia plus Sertoli cell and in primary spermatocyte populations. The activity was twice that found in early spermatids. Neither Na+–K+ ATPase nor mitochondrial F1 ATPase seemed to participate directly in the control of aerobic glycolysis. The uncoupling of oxidative p

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Wen, Qing, Elizabeth I. Tang, Wing-yee Lui, Will M. Lee, Chris K. C. Wong, Bruno Silvestrini, and C. Yan Cheng. "Dynein 1 supports spermatid transport and spermiation during spermatogenesis in the rat testis." American Journal of Physiology-Endocrinology and Metabolism 315, no. 5 (November 1, 2018): E924—E948. http://dx.doi.org/10.1152/ajpendo.00114.2018.

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In the mammalian testis, spermatogenesis is dependent on the microtubule (MT)-specific motor proteins, such as dynein 1, that serve as the engine to support germ cell and organelle transport across the seminiferous epithelium at different stages of the epithelial cycle. Yet the underlying molecular mechanism(s) that support this series of cellular events remain unknown. Herein, we used RNAi to knockdown cytoplasmic dynein 1 heavy chain (Dync1h1) and an inhibitor ciliobrevin D to inactivate dynein in Sertoli cells in vitro and the testis in vivo, thereby probing the role of dynein 1 in spermato

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PELTO-HUIKKO, M., R. SCHULTZ, J. KOISTINAHO, and T. HÖKFELT. "Immunocytochemical demonstratin of c-fos protein in sertoli cells and germ cells in rat testis." Acta Physiologica Scandinavica 141, no. 2 (February 1991): 283–84. http://dx.doi.org/10.1111/j.1748-1716.1991.tb09080.x.

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Deng, Qiong, Zeng Zhang, Yong Wu, Wang-yang Yu, Jianwen Zhang, Zhi-mao Jiang, Ying Zhang, Hui Liang, and Yao-ting Gui. "Non-Genomic Action of Androgens is Mediated by Rapid Phosphorylation and Regulation of Androgen Receptor Trafficking." Cellular Physiology and Biochemistry 43, no. 1 (2017): 223–36. http://dx.doi.org/10.1159/000480343.

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Background: Testosterone is critical for maintaining spermatogenesis and male fertility. The accomplishment of these processes requires the synergistic actions of the classical and non-classical signaling pathways of androgens. Methods: A murine testicular Sertoli cell line, TM4 cell was used to examine androgen actions in Sertoli cells. Western blot analysis and immunofluorescence assay were employed to study the testosterone-induced Androgen receptor (AR) translocation. Protein phosphorylation antibody array was applied to identify the phosphorylation sites under testosterone treatment, and

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Ko, W. H., H. C. Chan, S. B. Chew, and P. Y. D. Wong. "Regulated anion secretion in cultured epithelia from Sertoli cells of immature rats." Journal of Physiology 512, no. 2 (October 1998): 471–80. http://dx.doi.org/10.1111/j.1469-7793.1998.471be.x.

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Frungieri, Mónica B., Ricardo S. Calandra, Artur Mayerhofer, and María E. Matzkin. "Cyclooxygenase and prostaglandins in somatic cell populations of the testis." REPRODUCTION 149, no. 4 (April 2015): R169—R180. http://dx.doi.org/10.1530/rep-14-0392.

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Prostaglandins (PGs) are synthesized through the action of the rate-limiting enzyme cyclooxygenase (COX) and further specific enzymes. The development ofCox-deficient mice in the 1990s gave insights into the reproductive roles of PGs. FemaleCox-knockout mice were subfertile or infertile. Interestingly, fertility was not affected in male mice deficient inCox, suggesting that PGs may not be critical for the functioning of the testis. However, this conclusion has recently been challenged by observations of important roles for PGs in both physiological and pathological processes in the testis. The

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Qian, Xiaojing, Dolores D. Mruk, Elissa W. P. Wong, and C. Yan Cheng. "Breast cancer resistance protein regulates apical ectoplasmic specialization dynamics stage specifically in the rat testis." American Journal of Physiology-Endocrinology and Metabolism 304, no. 7 (April 1, 2013): E757—E769. http://dx.doi.org/10.1152/ajpendo.00645.2012.

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Drug transporters determine the bioavailability of drugs in the testis behind the blood-testis barrier (BTB). Thus, they are crucial for male contraceptive development if these drugs (e.g., adjudin) exert their effects behind the BTB. Herein breast cancer resistance protein (Bcrp), an efflux drug transporter, was found to be expressed by both Sertoli and germ cells. Interestingly, Bcrp was not a component of the Sertoli cell BTB. Instead, it was highly expressed by peritubular myoid cells at the tunica propria and also endothelial cells of the microvessels in the interstitium at all stages of

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Yan, Ming, Linxi Li, Baiping Mao, Huitao Li, Stephen Y. T. Li, Dolores Mruk, Bruno Silvestrini, Qingquan Lian, Renshan Ge, and C. Yan Cheng. "mTORC1/rpS6 signaling complex modifies BTB transport function: an in vivo study using the adjudin model." American Journal of Physiology-Endocrinology and Metabolism 317, no. 1 (July 1, 2019): E121—E138. http://dx.doi.org/10.1152/ajpendo.00553.2018.

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Studies have shown that the mTORC1/rpS6 signaling cascade regulates Sertoli cell blood-testis barrier (BTB) dynamics. For instance, specific inhibition of mTORC1 by treating Sertoli cells with rapamycin promotes the Sertoli cell barrier, making it “tighter.” However, activation of mTORC1 by overexpressing a full-length rpS6 cDNA clone (i.e., rpS6-WT, wild type) in Sertoli cells promotes BTB remodeling, making the barrier “leaky.” Also, there is an increase in rpS6 and p-rpS6 (phosphorylated and activated rpS6) expression at the BTB in testes at stages VIII–IX of the epithelial cycle, and it co

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Oliveira, P. F., M. Sousa, A. Barros, T. Moura, and A. Rebelo da Costa. "Membrane Transporters and Cytoplasmatic pH Regulation on Bovine Sertoli Cells." Journal of Membrane Biology 227, no. 1 (December 3, 2008): 49–55. http://dx.doi.org/10.1007/s00232-008-9139-z.

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Rocha, A. B., F. C. R. Guma, E. A. Casali, G. S. Scherer, M. A. Elena, and E. A. Bernard. "Influence of the Biomatrix on the Response of Sertoli Cells to FSH." Archives of Physiology and Biochemistry 105, no. 5 (January 1997): 473–77. http://dx.doi.org/10.1076/apab.105.5.473.3288.

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Pelletier, R. Marc, Suk Ran Yoon, Casimir D. Akpovi, Emil Silvas, and María Leiza Vitale. "Defects in the regulatory clearance mechanisms favor the breakdown of self-tolerance during spontaneous autoimmune orchitis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 296, no. 3 (March 2009): R743—R762. http://dx.doi.org/10.1152/ajpregu.90751.2008.

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We identified aberrations leading to spontaneous autoimmune orchitis (AIO) in mink, a seasonal breeder and natural model for autoimmunity. This study provides evidence favoring the view that a malfunction of the clearance mechanisms for apoptotic cell debris arising from imbalances in phagocyte receptors or cytokines acting on Sertoli cells constitutes a major factor leading to breakdown of self-tolerance during spontaneous AIO. Serum anti-sperm antibody titers measured by ELISA reflected spermatogenic activity without causing immune inflammatory responses. Orchitic mink showed excess antibody

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Vigodner, Margarita, Tomomoto Ishikawa, Peter N. Schlegel, and Patricia L. Morris. "SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis." American Journal of Physiology-Endocrinology and Metabolism 290, no. 5 (May 2006): E1022—E1033. http://dx.doi.org/10.1152/ajpendo.00527.2005.

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Sumoylation affects multiple cellular events, including chromatin inactivation and transcriptional repression. Our data provide the first characterization of small ubiquitin-related modifier-1 (SUMO-1) expression during human spermatogenesis by the use of high-resolution cellular SUMO-1 bioimaging. During human meiotic prophase, SUMO-1 localizes to sex chromosomes and centromeric and pericentromeric chromatin. As human spermatocytes progress toward the end of prophase in meiosis I, SUMO-1 is no longer detected within the sex body and pericentromeric heterochromatin but localizes exclusively to

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Lasala, Celina, Helena F. Schteingart, Nassim Arouche, Patricia Bedecarrás, Romina P. Grinspon, Jean-Yves Picard, Nathalie Josso, Nathalie di Clemente, and Rodolfo A. Rey. "SOX9 and SF1 are involved in cyclic AMP-mediated upregulation of anti-Müllerian gene expression in the testicular prepubertal Sertoli cell line SMAT1." American Journal of Physiology-Endocrinology and Metabolism 301, no. 3 (September 2011): E539—E547. http://dx.doi.org/10.1152/ajpendo.00187.2011.

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In Sertoli cells, anti-Müllerian hormone (AMH) expression is upregulated by FSH via cyclic AMP (cAMP), although no classical cAMP response elements exist in the AMH promoter. The response to cAMP involves NF-κB and AP2; however, targeted mutagenesis of their binding sites in the AMH promoter do not completely abolish the response. In this work we assessed whether SOX9, SF1, GATA4, and AP1 might represent alternative pathways involved in cAMP-mediated AMH upregulation, using real-time RT-PCR (qPCR), targeted mutagenesis, luciferase assays, and immunocytochemistry in the Sertoli cell line SMAT1.

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Brauchi, Sebastian, Maria C. Rauch, Ivan E. Alfaro, Christian Cea, Ilona I. Concha, Dale J. Benos, and Juan G. Reyes. "Kinetics, molecular basis, and differentiation of l-lactate transport in spermatogenic cells." American Journal of Physiology-Cell Physiology 288, no. 3 (March 2005): C523—C534. http://dx.doi.org/10.1152/ajpcell.00448.2003.

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Round spermatid energy metabolism is closely dependent on the presence of l-lactate in the external medium. This l-lactate has been proposed to be supplied by Sertoli cells in the seminiferous tubules. l-Lactate, in conjunction with glucose, modulates intracellular Ca2+ concentration in round spermatids and pachytene spermatocytes. In spite of this central role of l-lactate in spermatogenic cell physiology, the mechanism of l-lactate transport, as well as possible differentiation during spermatogenesis, has not been studied in these cells. By measuring radioactive l-lactate transport and intra

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Casali, E. A., T. R. da Silva, D. P. Gelain, G. R. R. F. Kaiser, A. M. O. Battastini, J. J. F. Sarkis, and E. A. Bernard. "Ectonucleotidase activities in Sertoli cells from immature rats." Brazilian Journal of Medical and Biological Research 34, no. 10 (October 2001): 1247–56. http://dx.doi.org/10.1590/s0100-879x2001001000003.

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Fenton, R. A., G. J. Cooper, I. D. Morris, and C. P. Smith. "Coordinated expression of UT-A and UT-B urea transporters in rat testis." American Journal of Physiology-Cell Physiology 282, no. 6 (June 1, 2002): C1492—C1501. http://dx.doi.org/10.1152/ajpcell.00567.2001.

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The blood-seminiferous tubule barrier is responsible for maintaining the unique microenvironment conducive to spermatogenesis. A key feature of the blood-testis barrier is selective permeability to solutes and water transport, conferred by the Sertoli cells of the seminiferous tubules (SMTs). Movement of fluid into the lumen of the seminiferous tubule is crucial to spermatogenesis. By Northern analysis, we have shown that 4.0-, 3.3-, 2.8-, and ∼1.7-kb UT-A mRNA transcripts and a 3.8-kb UT-B mRNA transcript are detected within rat testis. Western analysis revealed the expression of both charact

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35

Christiansen, T., B. Korsgaard, and A. Jespersen. "Effects of nonylphenol and 17 beta-oestradiol on vitellogenin synthesis, testicular structure and cytology in male eelpout Zoarces viviparus." Journal of Experimental Biology 201, no. 2 (January 15, 1998): 179–92. http://dx.doi.org/10.1242/jeb.201.2.179.

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Nonylphenol has been found to be oestrogenic in fish and may influence the reproductive system of male fish. In the present study, the effects of low (10 microg g-1 week-1) and high (100 microg g-1 week-1) doses of nonylphenol and of 17 beta-oestradiol on the synthesis of vitellogenin and on testicular structure and cytology were investigated in male eelpout Zoarces viviparus during active spermatogenesis (May) and late spermatogenesis (June). Twenty-five days after injection, a significant dose-dependent increase in the plasma vitellogenin concentration, measured by enzyme-linked immunosorben

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Yoon, Kyung-Ae, Young-Mi Chae, and Je-Yoel Cho. "FGF2 stimulates SDF-1 expression through theErmtranscription factor in Sertoli cells." Journal of Cellular Physiology 220, no. 1 (July 2009): 245–56. http://dx.doi.org/10.1002/jcp.21759.

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Leichtmann-Bardoogo, Yael, Lyora A. Cohen, Avital Weiss, Britta Marohn, Stephanie Schubert, Andreas Meinhardt, and Esther G. Meyron-Holtz. "Compartmentalization and regulation of iron metabolism proteins protect male germ cells from iron overload." American Journal of Physiology-Endocrinology and Metabolism 302, no. 12 (June 15, 2012): E1519—E1530. http://dx.doi.org/10.1152/ajpendo.00007.2012.

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The universal importance of iron, its high toxicity, and complex chemistry present a challenge to biological systems in general and to protected compartments in particular. The high mitotic rate and avid mitochondriogenesis of developing male germ cells imply high iron requirements. Yet access to germ cells is tightly regulated by the blood-testis barrier that protects the meiotic and postmeiotic germ cells. To elucidate how iron is supplied to developing male germ cells, we analyzed iron deposition and iron transport proteins in testes of mice with iron overload and with genetic ablation of t

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Tung, Pierre S., and Irving B. Fritz. "Role of laminin in the Morphogenetic cascade during Coculture of sertoli cells with peritubular cells." Journal of Cellular Physiology 161, no. 1 (October 1994): 77–88. http://dx.doi.org/10.1002/jcp.1041610111.

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Akerstrom, V. L., and M. R. Walters. "Physiological effects of 1,25-dihydroxyvitamin D3 in TM4 Sertoli cell line." American Journal of Physiology-Endocrinology and Metabolism 262, no. 6 (June 1, 1992): E884—E890. http://dx.doi.org/10.1152/ajpendo.1992.262.6.e884.

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1,25-Dihydroxyvitamin D3 [1,25(OH)2D3] receptors have been previously described in Sertoli cells. This study was performed to assess biological activity of the receptor in the mouse Sertoli cell line TM4. A 2-h preincubation with 0.01-25 nM 1,25(OH)2D3 resulted in a dose-dependent rapid uptake of 45Ca2+ within 5 min of addition of the isotope to the cells (27 +/- 8%, n = 4 experiments; P less than 0.05). This response was specific for 1,25(OH)2D3, in that it was not induced by 25-hydroxyvitamin D3, estradiol, cortisol, R 5020 (promegestone), or testosterone. However, a combination of testoster

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Bernardino, Raquel, David Carrageta, Ana Silva, Giuseppe Calamita, Marco Alves, Graça Soveral, and Pedro Oliveira. "Estrogen Modulates Glycerol Permeability in Sertoli Cells through Downregulation of Aquaporin-9." Cells 7, no. 10 (September 28, 2018): 153. http://dx.doi.org/10.3390/cells7100153.

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High 17β-Estradiol (E2) levels are known to cause alterations of spermatogenesis and environments throughout the male reproductive tract. Sertoli cells (SCs) ensure an adequate environment inside the seminiferous tubule. Glycerol stands as essential for the maintenance of blood–testis barrier created by SCs, however, the role of E2 in this process is not known. Herein, we hypothesized that the effect of E2 on glycerol permeability in mouse SCs (mSCs) could be mediated by aquaglyceroporins. The expression of aquaglyceroporins was assessed by RT-PCR and qRT-PCR. Glycerol permeability was evaluat

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Huynh, S., H. Oulhaj, J. Bocquet та A. Nouvelot. "Metabolic utilization of linoleate and α-linolenate in cultured Sertoli cells". Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 99, № 2 (січень 1991): 265–70. http://dx.doi.org/10.1016/0305-0491(91)90039-g.

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Fiorini, Celine, Xavier Decrouy, Norah Defamie, Dominique Segretain та Georges Pointis. "Opposite regulation of connexin33 and connexin43 by LPS and IL-1α in spermatogenesis". American Journal of Physiology-Cell Physiology 290, № 3 (березень 2006): C733—C740. http://dx.doi.org/10.1152/ajpcell.00106.2005.

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The gap junction proteins, connexins (Cxs), are present in the testis, and among them, Cx43 play an essential role in spermatogenesis. In the present study, we investigated the testicular expression and regulation of another Cx, Cx33, previously described as a negative regulator of gap junction communication. Cx33 mRNA was present in testis and undetectable in heart, liver, ovary, and uterus. In the mature testis, Cx33 was specifically immunolocalized in the basal compartment of the seminiferous tubules, whereas Cx43 was present in both seminiferous tubule and interstitial compartments. During

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Cameron, D. F., J. Rountree, R. E. Schultz, D. Repetta, and F. T. Murray. "Sustained hyperglycemia results in testicular dysfunction and reduced fertility potential in BBWOR diabetic rats." American Journal of Physiology-Endocrinology and Metabolism 259, no. 6 (December 1, 1990): E881—E889. http://dx.doi.org/10.1152/ajpendo.1990.259.6.e881.

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Rats with short-term diabetes show a greater than 50% reduction of serum testosterone and increased lipid in Leydig cells but normal testicular structure. The purpose of this study was to determine the extent of testicular pathology (morphology index), integrity of the blood-testis barrier, daily sperm production (DSP), number of Leydig cells per testis (LC/T), and total trunk testosterone (TTT) in diabetic rats (BBWORdp) with long-term hyperglycemia (300-350 mg/dl for greater than 180 days) and to evaluate its effects on fertility potential. Results were compared with similarly aged normoglyc

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Niu, Qiaoge, Maosheng Cao, Chenfeng Yuan, Yuwen Huang, Zijiao Zhao, Boqi Zhang, Xin Wang, et al. "Effect of nerve growth factor on the proliferation in newborn bovine testicular Sertoli cells." Reproduction 160, no. 3 (September 2020): 405–15. http://dx.doi.org/10.1530/rep-19-0601.

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Nerve growth factor (NGF) has been proved to play important roles in male reproductive physiology, but the molecular mechanisms of NGF action remain unclear. In this study, the effects of NGF on the growth of newborn bovine testicular Sertoli (NBS) cells and the related signaling pathways were investigated. The NBS cells were treated in vitro with NGF (100 ng/mL) for 18 h. The expression levels of cell proliferation related genes, INHBB, and cytoplasmic specialization related gene were determined using real-time PCR and Western blot. The roles of PI3K/AKT and MAPK/ERK pathways in NGF-induced c

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Kishi, Hisashi, Mariko Itoh, Sachiko Wada, Yoko Yukinari, Yumiko Tanaka, Natsuko Nagamine, Wanzhu Jin, Gen Watanabe, and Kazuyoshi Taya. "Inhibin is an important factor in the regulation of FSH secretion in the adult male hamster." American Journal of Physiology-Endocrinology and Metabolism 278, no. 4 (April 1, 2000): E744—E751. http://dx.doi.org/10.1152/ajpendo.2000.278.4.e744.

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We investigated the importance of inhibin and testosterone in the regulation of gonadotropin secretion in adult male golden hamsters ( Mesocricetus auratus). After castration, plasma concentrations of inhibin and testosterone were reduced to undetectable, whereas plasma follicle-stimulating hormone (FSH) and luteinizing hormone (LH) were increased. After hemicastration, plasma FSH and LH increased moderately and plasma inhibin decreased to one-half its initial level. Plasma testosterone levels in hemicastrated animals decreased 3 h after hemicastration but returned to those in sham-operated an

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Dias, Tania Rodrigues, Raquel Lages Bernardino, Marco Gouveia Alves, Joaquina Silva, Alberto Barros, Mário Sousa, Susana Casal, Branca Maria Silva, and Pedro Fontes Oliveira. "L-theanine modulates human Sertoli cells metabolic and mitochondrial function while maintaining redox homeostasis." Free Radical Biology and Medicine 120 (May 2018): S150. http://dx.doi.org/10.1016/j.freeradbiomed.2018.04.496.

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Michailidis, Georgios, Maria Anastasiadou, Edith Guibert, and Pascal Froment. "Activation of innate immune system in response to lipopolysaccharide in chicken Sertoli cells." REPRODUCTION 148, no. 3 (September 2014): 259–70. http://dx.doi.org/10.1530/rep-14-0064.

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Sertoli cells (SCs) play an important physiological role in the testis, as they support, nourish, and protect the germ cells. As protection of the developing spermatozoa is an emerging aspect of reproductive physiology, this study examined the expression pattern of innate immune-related genes, including avian β-defensins (AvBDs), Toll-like receptors (TLRs), and cytokines, and investigated the time course of an inflammatory response in rooster SCs triggered by exposure to the bacterial endotoxin lipopolysaccharide (LPS). SCs were isolated from 6-week-old chicken, culturedin vitro, and stimulate

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Abdullah, Munir, James A. Crowell, Laura L. Tres, and Abraham L. Kierszenbaum. "Fetuin: A serum component associated with rat sertoli and spermatogenic cells in coculture." Journal of Cellular Physiology 127, no. 3 (June 1986): 463–72. http://dx.doi.org/10.1002/jcp.1041270317.

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Mitic, Laura L., Christina M. Van Itallie, and James M. Anderson. "Molecular Physiology and Pathophysiology of Tight Junctions I. Tight junction structure and function: lessons from mutant animals and proteins." American Journal of Physiology-Gastrointestinal and Liver Physiology 279, no. 2 (August 1, 2000): G250—G254. http://dx.doi.org/10.1152/ajpgi.2000.279.2.g250.

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Tight junctions form the major paracellular barrier in epithelial tissues. Barrier-sealing properties are quite variable among cell types in terms of electrical resistance, solute and water flux, and charge selectivity. A molecular explanation for this variability appears closer following identification of the transmembrane proteins occludin and members of the claudin multigene family. For example, the human phenotype of mutations in claudin-16 suggests that it creates a channel that allows magnesium to diffuse through renal tight junctions. Similarly, a mouse knockout of claudin-11 reveals it

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Heindel, JerroldJ, CassandraJ Powell, CarlS Paschall, Akira Arimura, and MichaelD Culler. "PACAP stimulates cAMP accumulation and secretory function in cultured rat sertoli cells." Regulatory Peptides 37, no. 3 (February 1992): 333. http://dx.doi.org/10.1016/0167-0115(92)90645-b.

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