Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle‐stimulating hormone or by dibutyryl cyclic AMP

Tung, Pierre S.; Burdzy, K; Fritz, Irving B.

doi:10.1002/jcp.1041550118

Cited by 14 publications

(4 citation statements)

References 29 publications

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“…The C-terminal fragment of FLNA then bound to the AR in a ligand-independent manner, repressed AR-mediated transactivation (more than full-length), and was required for AR nuclear translocation (Ozanne et al, 2000;Loy et al, 2003). In addition, it was previously shown that the general protease inhibitor a 2 -macroglobulin prevented the cAMP-mediated reorganization of the Sertoli cell actin cytoskeleton (Tung et al, 1993). So perhaps the most important aspect of Palld expression and regulation in the testis is not which isoform is transcribed, but where and how the protein is cleaved by specific proteases.…”

Section: Discussionmentioning

confidence: 99%

Nuclear localization of the actin regulatory protein palladin in sertoli cells

Niedenberger

Chappell

Kaye

et al. 2013

Molecular Reproduction Devel

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In the testis, F-actin structures are involved in spermatid nuclear remodeling and cytoplasm reduction, maintenance of the blood-testis barrier, support of the spermatogonial stem cell niche, and release of spermatids into the tubular lumen. To gain a better understanding of actin regulation in Sertoli-germ cell interactions, we investigated the expression of the Palladin (Palld) gene, which encodes a widely expressed phosphoprotein that localizes to actin-rich cytoplasmic structures, including focal adhesions, cell-cell junctions, podosomes, and stress fibers, and serves as a molecular scaffold to bundle actin fibers. In germ cells, PALLD was concentrated along the tubulin- and F-actin-containing cytoplasmic manchette that forms adjacent to the elongating spermatid nucleus during spermiogenesis. To our surprise, PALLD relocated from the cytoplasm to the nucleus of Sertoli cells in the juvenile testis, coincident with the onset of puberty, and this localization was maintained in the adult. We provide evidence that the 140 kDa isoform of PALLD predominates in Sertoli cells, and that it is apparently cleaved, with the C-terminus localizing to the nucleus while the N-terminus remains cytoplasmic. We investigated the nuclear localization of the C-terminus of PALLD and found that it is regulated by a putative nuclear export signal. These results provide the foundation for future work employing Sertoli cell- and spermatid-specific Palld-knockout mice to study diverse roles of PALLD as both a nuclear-actin regulatory protein and as a potential regulator of manchette formation during spermatogenesis.

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Section: Discussionmentioning

confidence: 99%

Nuclear localization of the actin regulatory protein palladin in sertoli cells

Niedenberger

Chappell

Kaye

et al. 2013

Molecular Reproduction Devel

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“…Previous research has suggested that Sertoli cells, the primary supportive cells of the seminiferous epithelium, play a key role in triggering and regulating spermatogenesis (de Kretser et al, 1998) and have a well‐developed cytoskeleton that is responsible for the formation of the seminiferous epithelium and the development of germ cells (Boekelheide et al, 1989; Russell et al, 1989; Muffly et al, 1993; Tung et al, 1993). Morphologic studies have implicated the Sertoli cytoskeleton in the maintenance of cell shape, localization and transformation of cytoplasmic organoids, formation and stabilization of cell‐cell or cell‐extracellular matrix contacts, localization, anchoring and migration of developed germ cells, and the release of mature sperm from seminiferous epithelium.…”

Section: Discussionmentioning

confidence: 99%

Cytoskeleton Vimentin Disruption of Mouse Sertoli Cells Injured by Nitrogen Mustard In Vitro

Zhang

Wei

et al. 2007

Journal of Andrology

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Reproductive toxicity is one of the potential side effects of anticancer alkylating agents, with potential effects on vimentin intermediate filaments, one of the main components of the Sertoli cytoskeleton. Research suggests (Aumuller et al, 1988;Aumuller et al, 1992) that the highly organized and active Sertoli cytoskeleton is important in spermatogenesis. The aim of the current study was to investigate the effects of alkylating agents on vimentin filament expression in vitro. Sertoli cells, isolated from 20-day-old mice testes, were cultured for 5 days and then incubated with 0, 50, 100, and 200 mmol/L nitrogen mustard (HN2). Morphologic changes in Sertoli cells were observed per 30-minute interval at 12-hour exposure time points to 100 mmol/L HN2. Vimentin expression was investigated by immunocytochemistry at 6 hours and 24 hours posttreatment and reverse transcriptase polymerase chain reaction and Western blot at 12 hours posttreatment with 50, 100, and 200 mmol/L HN2. Exposure to HN2 resulted in a comparatively small Sertoli cell body with diminished cytoplasm. Sertoli cells were shrunk or detached. Cytoskeletal disruption increased with increasing HN2 concentration. The optical density values of vimentin antibody and expression of vimentin mRNA and protein were significantly decreased with increasing concentration of HN2. Significant treatment dose-dependent and time-dependent differences of vimentin mRNA and protein expression levels were also noted. Our data suggest that the change in the biochemical properties of vimentin may indicate that one of the mechanisms of reproductive toxicity resulting from HN2 is disruption of Sertoli cell vimentin filament structure, accompanied by a down-regulation of vimentin expression.

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“…The tissue remodeling process and the production of Sertoli cell factors leads to the constitution of a specific biochemical and cytoarchitectural microenvironment in the adluminal compartment, in which germ cells will proliferate and differentiate. Sertoli cell products include binding and transport proteins (Han et al, 1993), extracellular matrix and junctional proteins (Dym and Fawcett, 1970, 1971; Russell and Peterson, 1985; Han et al, 1993; Chen and Mruk, 2002), proteases and protease inhibitors (Tang et al, 1993), growth factors (Gnessi et al, 1997), and energy substrates such as lactate (Grootegoed and Den Boer, 1990). However, there is no available information on the mechanism of vitamin C transport across the blood–testis barrier.…”

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confidence: 99%

Molecular identification and functional characterization of the vitamin C transporters expressed by Sertoli cells

Angulo

Castro

Rivas

et al. 2008

Journal Cellular Physiology

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Vitamin C is an essential micronutrient for the development of male germ cells. In the gonad, the germ cells are isolated from the systemic circulation by the blood-testis barrier, which consists of a basal layer of Sertoli cells that communicate through an extensive array of tight junction complexes. To study the behavior of Sertoli cells as a first approach to the molecular and functional characterization of the vitamin C transporters in this barrier, we used the 42GPA9 cell line immortalized from mouse Sertoli cells. To date, there is no available information on the mechanism of vitamin C transport across the blood-testis barrier. This work describe the molecular identity of the transporters involved in vitamin C transport in these cells, which we hope will improve our understanding of how germ cells obtain vitamin C, transported from the plasma into the adluminal compartment of the seminiferous tubules. RT-PCR analyses revealed that 42GPA9 cells express both vitamin C transport systems, a finding that was confirmed by immunocytochemical and immunoblotting analysis. The kinetic assays using radioactive vitamin C revealed that both ascorbic acid (AA) transporters, SVCT1 and SVCT2, are functionally active. Moreover, the kinetic characteristics of dehydroascorbic acid (DHA) and 3-methylglucose (OMG) transport by 42GPA9 Sertoli cells correspond to facilitative hexose transporters GLUT1, GLUT2 and GLUT3 expressed in these cells. This data is consistent with the concept that Sertoli cells have the ability to take up vitamin C. It is an important finding and contributes to our knowledge of the physiology of male germ cells.

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Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle‐stimulating hormone or by dibutyryl cyclic AMP

Cited by 14 publications

References 29 publications

Nuclear localization of the actin regulatory protein palladin in sertoli cells

Nuclear localization of the actin regulatory protein palladin in sertoli cells

Cytoskeleton Vimentin Disruption of Mouse Sertoli Cells Injured by Nitrogen Mustard In Vitro

Molecular identification and functional characterization of the vitamin C transporters expressed by Sertoli cells

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