Relevant bibliographies by topics / Sertoli cells Physiology

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Academic literature on the topic 'Sertoli cells Physiology'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 January 2023

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Journal articles on the topic "Sertoli cells Physiology"

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 paracrine factors.
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2

Maqdasy, Salwan, Fatim-Zohra El Hajjaji, Marine Baptissart, Emilie Viennois, Abdelkader Oumeddour, Florence Brugnon, Amalia Trousson, et al. "Identification of the Functions of Liver X Receptor-β in Sertoli Cells Using a Targeted Expression-Rescue Model." Endocrinology 156, no. 12 (September 24, 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 essential for normal testicular physiology. To decipher the roles of LXRβ within the Sertoli cells, we generated Lxrα−/−;Lxrβ−/−:AMH-Lxrβ transgenic mice, which reexpress Lxrβ in Sertoli cells in the context of Lxrα−/−;Lxrβ−/− mice. In addition to lipid homeostasis, LXRβ is necessary for maintaining the blood-testis barrier and the integrity of the germ cell epithelium. LXRβ is also implicated in the paracrine action of Sertoli cells on Leydig cells to modulate T synthesis. The Lxrα−/−;Lxrβ−/− and Lxrα−/−;Lxrβ−/−:AMH-Lxrβ mice exhibit lipid accumulation in germ cells after the Abcg8 down-regulation, suggesting an intricate LXRβ-dependent cooperation between the Sertoli cells and germ cells to ensure spermiogenesis. Further analysis revealed also peritubular smooth muscle defects (abnormal lipid accumulation and disorganized smooth muscle actin) and spermatozoa stagnation in the seminiferous tubules. Together the present work elucidates specific roles of LXRβ in Sertoli cell physiology in vivo beyond lipid homeostasis.
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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 spermatogenesis. Cx43 protein levels increased transiently during the colonization of the tubules by the early-stage spermatocytes. Cx43 phosphorylated (PCx43) and nonphosphorylated (NPCx43) in Ser368 decreased during the periods of completion of meiosis and Sertoli cell differentiation, while Cx43 mRNA remained elevated throughout. PCx43 labeled chiefly the plasma membrane except by stage VII when vesicles were also labeled in Sertoli cells. Vesicles and lysosomes in Sertoli cells and the Golgi apparatus in the round spermatids were NPCx43 positive. A decrease in Cx43 gene expression was matched by a Cx43 protein increase in the early, not the late, phase of AIO. Total Cx43 and PCx43 decreased with the advance of orchitis. The study makes a novel finding of gap junctions connecting germ cells. The data indicate that Cx43 protein expression and phosphorylation in Ser368 are stage-specific events that may locally influence the acquisition of meiotic competence and the Sertoli cell differentiation in normal testis. AIO modifies Cx43 levels, suggesting changes in Cx43-mediated intercommunication and spermatogenic activity in response to cytokines imbalances in Sertoli cells.
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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 exerts no effect on purified Leydig cells (greater than 90% of Leydig cells). Second, FSH stimulates the activity of Leydig cells cocultured with Sertoli cells, whereas it remains without effect on purified Leydig cells cultured alone. This stimulating effect of FSH on Leydig cell activity is dependent on the Sertoli cell number in the coculture. These data 1) show that the stimulating effect of FSH on Leydig cell function is mediated by Sertoli cells and 2) support the concept of local control of Leydig cell function originating from Sertoli cells.
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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 and transferrin secretions. Collectively, our data indicate that autocrine IGF-I contributes significantly to Sertoli cell homeostasis. The described in vitro system for loss-of-function analysis of the IGF-IR can be readily transposed to study the role of other intratesticular growth factors involved in spermatogenesis.
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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. Catecholamines had no effect on basal and stimulated testosterone release by these cells, while dopamine inhibited 17β-estradiol synthesis by Sertoli cells. Using various α- and β-adrenergic agonists and antagonists, β-receptors, likely of the β1-subtype, were shown to be present in both cell lines. Taken together these data suggest the presence of a cyclic adenosine 3′,5′-monophosphate-linked adrenergic receptor in porcine Leydig and Sertoli cells, the role of which remains to be determined.
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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 Sertoli cells, and even at this stage, highly phosphorylated occludin was detected. With development, occludin gradually became concentrated at the most basal regions of Sertoli cells. The same results were obtained in rat, but unexpectedly occludin was not detected in human or guinea pig Sertoli cells by immunofluorescence microscopy as well as by immunoblotting. Inasmuch as TJs are also well developed in Sertoli cells of these species, we concluded that, at least in the testes of these species, there are some Sertoli cell-specific isoforms of occludin or other TJ-associated integral membrane proteins that differ from occludin.
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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 rat testis the positivity was not limited to the tubular compartment (Sertoli cells) but was also present in the interstitium. A high concentration (13 pmol/mg protein) of high-affinity (dissociation constant = 0.6 nM) 125I-labeled ET-1 binding sites was present in Leydig cells. These sites bind ET-1 and ET-2 with 1,000-fold higher affinity than ET-3, suggesting that they correspond to the subtype ETA of the ET receptors. Specific 125I-ET-1 binding sites are present also in Sertoli cells but are 50-fold less concentrated than in Leydig cells. Our results suggest an autocrine/paracrine role for ET-1 in rat testis.
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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-independent basal cAMP levels found in TgFSHR*D567G Sertoli cells. Furthermore, Sertoli cell overexpression of TgFSHR*D567G but not TgFSHRwt allowed promiscuous cAMP responses to human chorionic gonadotropin (300 IU/ml) and TSH (30 mIU/ml), demonstrating increased constitutive signaling and altered glycoprotein hormone specificity via the intracellular D567G substitution rather than FSHR overexpression. Despite elevating Sertoli cell FSH sensitivity, overexpression of TgFSHRwt had no detectable effect upon normal testis function and did not stimulate Sertoli and germ cell development in testes of gonadotropin-deficient hypogonadal ( hpg) mice, in contrast to the increased meiotic and postmeiotic germ cell development in TgFSHR*D567G hpg testes. Increased steroidogenic potential of TgFSHR*D567G hpg testes was demonstrated by elevated Cyp11a1 and Star expression, which was not detected in TgFSHRwt hpg testes. Androgen-regulated and Sertoli cell-specific Rhox5 gene expression was increased in TgFSHR*D567G but not TgFSHRwt hpg testes, providing evidence of elevated LH-independent androgen activity due to mutant FSHR*D567G. Hence, transgenic FSHR overexpression in Sertoli cells revealed that the D567G mutation confers autonomous signaling and steroidogenic activity in vivo as well as promiscuous glycoprotein hormone receptor activation, independently of FSHR overexpression alone.
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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 the expression of glucose transporters in rat Sertoli cells and 2) the participation of different signal transduction pathways in the above-mentioned regulation. Results obtained show that decreasing glucose levels in Sertoli cell culture medium provokes 1) an increase in glucose uptake accompanied by only a slight decrease in lactate production, 2) an increase in GLUT1 and a decrease in GLUT3 expression, and 3) an activation of AMP-activated protein kinase (AMPK)-, phosphatidylinositol 3-kinase (PI3K)/PKB-, and p38 MAPK-dependent pathways. Additionally, by using specific inhibitors of these pathways, a possible participation of AMPK- and p38MAPK-dependent pathways in the regulation of glucose uptake and GLUT1 expression is shown. These results suggest that Sertoli cells adapt to conditions of glucose deprivation to ensure an adequate lactate concentration in the microenvironment where germ cell development occurs.
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Dissertations / Theses on the topic "Sertoli cells Physiology"

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Hayes, Marianne Kay. "Bovine testicular cells in vitro: establishment of primary cultures and investigations of secretory functions : a thesis presented for the degree of Doctor of Philosophy in the University of Adelaide." Title page, contents and summary only, 1986. http://web4.library.adelaide.edu.au/theses/09PH/09phh4178.pdf.

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Includes bibliographical references (leaves 98-128). Investigates protein secretion by bovine Sertoli cells in culture. Cultures were obtained from bulls at all stages of post natal development and from sexually mature animals.
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Wong, Chui-shan, and 黃翠珊. "Interactions of multiple proteins during specialized junctions formation in the rat seminiferous epithelium." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1999. http://hub.hku.hk/bib/B31221907.

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Harstine, Bo R. "Novel Approaches to Positively Impact the Early Life Physiology, Endocrinology, and Productivity of Bulls." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1480521360099455.

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Plotton, Ingrid. "Implication de facteurs sertoliens dans la physiologie et la physiopathologie de la spermatogenèse : étude des ARNm de la clusterine et du stem cell factor." Lyon 1, 2006. http://www.theses.fr/2006LYO10079.

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La cellule de Sertoli a un rôle fondamental dans le contrôle des différentes étapes de la spermatogenèse. Le stem cell factor et la clusterine sont produits par la cellule de Sertoli. Nous avons mesuré par RT-PCR quantitative leurs ARNm au cours du développement et après avoir induit un trouble de la spermatogenèse chez le rat et dans des biopsies testiculaires de patients présentant une azoospermie soit obstructive (groupe contrôle) soit par trouble de la spermatogenèse. Les résultats suggèrent que la différenciation des cellules de Sertoli est altérée dans les troubles de la spermatogenèse constitutifs ou idiopathiques chez l'homme, contrairement aux troubles de la spermatogenèse acquis chez l'homme ou induit chez le rat adulte
The sertoli cell is essential in the control of the different stages in the spermatogenisis. Stem cell factor and clusterin are product by the Sertoli Cell. We mesured by quantitative RT PCR their mRNA during the developpement and after induction of spermatogenisis failure in the rat and in the testicular biopsies from men with either obstructive azoospermia (control group) or spermatogenic failure. The results suggest that Sertoli cell differentiation is altered in cases of constitutive or idiopathic spermatogenic failure in human, in opposite of acquired spermatogenesic failure in human or induced spermatogenic failure in adult rat
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Papadopoulos, Vassilios. "Etude in vitro de la régulation de la fonction leydigienne chez le rat mature." Paris 6, 1986. http://www.theses.fr/1986PA066103.

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La participation des phospholipides (protéine kinase dépendante du ca**(2+) et des phospholipides, méthylations et leukotriène b4) et du cytosquelette dans le mécanisme d'action de la LH sur la cellule de Leydig purifiée chez le rat adulte a été étudiée et l'existence d'un contrôlé local a été démontré. Ce contrôle s'exerce par l'intermédiaire des facteurs synthétisés par les cellules de Sertoli et agissant sur les productions d'AMPC et de testostérone leydigiennes. L'aromatisation de la testostérone en estradiol 17beta a été aussi étudiée. Cette activité enzymatique est sous le contrôle endocrine de la LH, des glucocorticoïdes, de la prolactine et paracrine par des facteurs secrètes par la cellule de Sertoli
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Hayes, Marianne Kay. "Bovine testicular cells in vitro: establishment of primary cultures and investigations of secretory functions / by Marianne Kay Hayes." Thesis, 1986. http://hdl.handle.net/2440/20634.

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Includes bibliographical references (leaves 98-128).
iv, 128 leaves, [22] leaves of plates : ill. ; 30 cm.
Investigates protein secretion by bovine Sertoli cells in culture. Cultures were obtained from bulls at all stages of post natal development and from sexually mature animals.
Thesis (Ph.D.) -- University of Adelaide, Dept. of Animal Sciences, 1987
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Books on the topic "Sertoli cells Physiology"

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D, Griswold Michael, ed. The Sertoli cell. Clearwater, FL: Cache River Press, 1993.

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Dee, Russell Lonnie, and Griswold Michael D, eds. The Sertoli cell. Clearwater, FL: Cache River Press, 1993.

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Griswold, Michael D. Sertoli Cell Biology. Elsevier Science & Technology Books, 2014.

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K, Skinner Michael, and Griswold Michael D, eds. Sertoli cell biology. Amsterdam: Elsevier Academic Press, 2005.

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Griswold, Michael D. Sertoli Cell Biology. Elsevier Science & Technology Books, 2014.

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Griswold, Michael D. Sertoli Cell Biology. Elsevier, 2018.

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Griswold, Michael D., and Michael K. Skinner. Sertoli Cell Biology. Elsevier Science & Technology Books, 2004.

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(Editor), Michael K. Skinner, and Michael D. Griswold (Editor), eds. Sertoli Cell Biology, Volume 1. Academic Press, 2004.

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(Editor), Michael K. Skinner, and Michael D. Griswold (Editor), eds. Sertoli Cell Biology, Volume 1. Academic Press, 2004.

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Book chapters on the topic "Sertoli cells Physiology"

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Steinberger, Anna, Andrzej Janecki, and Andrzej Jakubowiak. "Use of Two-Compartment Cultures of Sertoli Cells for Investigating Blood-Testis Barrier Physiology." In Function of Somatic Cells in the Testis, 167–85. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4612-2638-3_9.

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Kovacs, William J. "Male Reproductive Function." In Textbook of Endocrine Physiology. Oxford University Press, 2011. http://dx.doi.org/10.1093/oso/9780199744121.003.0012.

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The testes are the source of both germ cells and hormones essential for male reproductive function. The production of both sperm and steroid hormones is under complex feedback control by the hypothalamic-pituitary system. The testis consists of a network of tubules for the production and transport of sperm to the excretory ducts and a system of interstitial cells (called Leydig cells) that express the enzymes required for the synthesis of androgens. The spermatogenic or seminiferous tubules are lined by a columnar epithelium composed of the germ cells themselves as well as supporting Sertoli cells surrounded by peritubular tissue made up of collagen, elastic fibers, and myofibrillar cells. Tight junctions between Sertoli cells at a site between the spermatogonia and the primary spermatocyte form a diffusion barrier that divides the testis into two functional compartments, basal and adluminal. The basal compartment consists of the Leydig cells surrounding the tubule, the peritubular tissue, and the outer layer of the tubule containing the spermatogonia. The adluminal compartment consists of the inner two-thirds of the tubules containing primary spermatocytes and germ cells in more advanced stages of development. The base of the Sertoli cell is adjacent to the basement membrane of the spermatogenic tubule, with the inner portion of the cell engulfing the developing germ cells so that spermatogenesis actually takes place within a network of Sertoli cell cytoplasm. The mechanism by which spermatogonia pass through the tight junctions between Sertoli cells to begin spermatogenesis is unknown. The close proximity of the Leydig cell to the Sertoli cell with its embedded germ cells is thought to be critical for normal male reproductive function. The seminiferous tubules empty into a network of ducts termed the rete testis. Sperm are then transported into a single duct, the epididymis. Anatomically, the epididymis can be divided into the caput, the corpus, and the cauda regions. The caput epididymidis consists of 8 to 12 ductuli efferentes, which have a larger lumen tapering to a narrower diameter at the junction of the ductus epididymidis.
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GRISWOLD, M., and D. MCLEAN. "The Sertoli Cell." In Knobil and Neill's Physiology of Reproduction, 949–75. Elsevier, 2006. http://dx.doi.org/10.1016/b978-012515400-0/50024-5.

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