The production of lactate and pyruvate as sensitive indices of altered rat Sertoli cell function in vitro following the addition of various testicular toxicants

1988 ◽  
Vol 94 (1) ◽  
pp. 160-170 ◽  
Author(s):  
J. Williams ◽  
P.M.D. Foster
1985 ◽  
Vol 132 (2) ◽  
pp. 729-734 ◽  
Author(s):  
M. Benahmed ◽  
C. Grenot ◽  
E. Tabone ◽  
P. Sanchez ◽  
A.M. Morera

Endocrinology ◽  
1993 ◽  
Vol 132 (3) ◽  
pp. 975-982 ◽  
Author(s):  
J P de Winter ◽  
H M Vanderstichele ◽  
M A Timmerman ◽  
L J Blok ◽  
A P Themmen ◽  
...  

Endocrinology ◽  
2021 ◽  
Vol 162 (4) ◽  
Author(s):  
Siwen Wu ◽  
Lixiu Lv ◽  
Linxi Li ◽  
Lingling Wang ◽  
Baiping Mao ◽  
...  

Abstract Throughout spermatogenesis, cellular cargoes including haploid spermatids are required to be transported across the seminiferous epithelium, either toward the microtubule (MT) plus (+) end near the basement membrane at stage V, or to the MT minus (−) end near the tubule lumen at stages VI to VIII of the epithelial cycle. Furthermore, preleptotene spermatocytes, differentiated from type B spermatogonia, are transported across the Sertoli cell blood-testis barrier (BTB) to enter the adluminal compartment. Few studies, however, have been conducted to explore the function of MT-dependent motor proteins to support spermatid transport during spermiogenesis. Herein, we examined the role of MT-dependent and microtubule plus (+) end–directed motor protein kinesin 15 (KIF15) in the testis. KIF15 displayed a stage-specific expression across the seminiferous epithelium, associated with MTs, and appeared as aggregates on the MT tracks that aligned perpendicular to the basement membrane and laid across the entire epithelium. KIF15 also tightly associated with apical ectoplasmic specialization, displaying strict stage-specific distribution, apparently to support spermatid transport across the epithelium. We used a loss-of-function approach by RNAi to examine the role of KIF15 in Sertoli cell epithelium in vitro to examine its role in cytoskeletal-dependent Sertoli cell function. It was noted that KIF15 knockdown by RNAi that reduced KIF15 expression by ~70% in Sertoli cells with an established functional tight junction barrier impeded the barrier function. This effect was mediated through remarkable changes in the cytoskeletal organization of MTs, but also actin-, vimentin-, and septin-based cytoskeletons, illustrating that KIF15 exerts its regulatory effects well beyond microtubules.


2016 ◽  
Vol 14 (6) ◽  
pp. 5325-5333 ◽  
Author(s):  
Yanfeng Zhu ◽  
Hua Xu ◽  
Min Li ◽  
Zhibin Gao ◽  
Jie Huang ◽  
...  

1988 ◽  
Vol 119 (2) ◽  
pp. 315-326 ◽  
Author(s):  
R. M. Sharpe ◽  
I. A. Swanston ◽  
I. Cooper ◽  
C. G. Tsonis ◽  
A. S. McNeilly

ABSTRACT Immunoreactive inhibin was measured in testicular interstitial fluid (IF) from rats during sexual maturation or after impairment of spermatogenesis induced by ethane dimethanesulphonate (EDS), unilateral cryptorchidism or local heating (43 °C, 30 min) of the testes, to ascertain its usefulness as a marker of changing Sertoli cell function. Cultures of isolated seminiferous tubules were also studied. Inhibin was measured by a radioimmunoassay directed towards the first 26 amino acids of the N-terminus of the α-subunit, and the results confirmed for selected pools of IF by in-vitro bioassay using dispersed ovine pituitary cells. During puberty, IF levels of immunoactive inhibin fell by more than 90% (P<0·001) between 30 and 60 days of age, a decrease paralleled by the levels of androgen-binding protein (ABP), another Sertoli cell product secreted into IF. These changes also paralleled, but preceded, the fall (60%; P<0·001) in serum levels of FSH between 40 and 70 days, while the serum and IF levels of testosterone increased more than two-fold over this period. When adult rats were injected with EDS to destroy the Leydig cells, testosterone levels in IF and serum were undetectable at 3 and 7 days after treatment, were just detectable at 14 days and thereafter returned slowly towards normal by 42 days. The initial androgen withdrawal following EDS treatment caused a progressive reduction in testicular weight up to 21 days and this was accompanied by a significant increase in the serum levels of FSH and a two- to threefold increase in the IF levels of immunoactive inhibin (and also of ABP). Serum FSH and IF levels of immunoactive inhibin returned to within the normal range by 42 days when testosterone levels had normalized. In contrast, in two other experimental situations in which a marked decrease in testicular weight coupled with an increase in IF levels of ABP occurs, different results for the IF levels of immunoactive inhibin were obtained. Thus, in rats exposed to local heating of the testes, IF levels of immunoactive inhibin remained unchanged from control values at 21–40 days after treatment, a finding confirmed by bioassay results. In rats made unilaterally cryptorchid for 10 months, levels of immunoactive inhibin in IF were reduced by 60% (P<0·01) in the abdominal compared with the contralateral scrotal testis. These results suggest that (1) IF levels of immunoactive inhibin do not always change in parallel to the levels of ABP and may be a useful marker of changing Sertoli cell function, and (2) in at least two situations (puberty and after EDS treatment), there may be a positive relationship between the serum levels of FSH and the IF levels of immunoactive inhibin. This positive relationship was confirmed by in-vitro findings in which FSH and dibutyryl cyclic AMP (but not testosterone) were shown to stimulate immunoactive inhibin production by isolated rat seminiferous tubules during culture for 2–6 days. J. Endocr. (1988) 119, 315–326


1997 ◽  
Vol 21 (8) ◽  
pp. 1409-1417 ◽  
Author(s):  
Qianlong Zhu ◽  
David H. Van Thiel ◽  
Judith S. Gavaler
Keyword(s):  

1995 ◽  
Vol 108 (3) ◽  
pp. 917-925
Author(s):  
N. Gerard ◽  
A. Corlu ◽  
B. Kneip ◽  
H. Kercret ◽  
M. Rissel ◽  
...  

We have identified a liver-regulating protein involved in cell contact-mediated regulation of Sertoli cell function by primary spermatocytes in rat testis. Liver-regulating protein was studied using monoclonal antibody L8 prepared from rat primitive biliary epithelial cells. This molecule was located in vivo at the interface of Sertoli cells and spermatocytes, and expressed in a stage-dependent manner (expression peaked on leptotene-zygotene spermatocytes). In vitro, the liver-regulating protein was found on Sertoli cell, spermatocyte and early spermatid membranes. Immunoaffinity procedures revealed two peptides of 85 and 73 kDa for Sertoli cells, while spermatocytes and spermatids displayed a single smaller peptide of 56 kDa. The involvement of the liver-regulating protein in cell interaction-mediated regulation of Sertoli cell was assessed in vitro by tracing Sertoli cell transferrin and inhibin secretion, as well as mRNA synthesis in spermatocyte-Sertoli cell cocultures and in rat liver biliary epithelial cell-Sertoli cell cocultures, performed in the presence or absence of monoclonal antibody L8. Inhibition of the spermatocyte- and liver biliary epithelial cell-stimulated secretion of transferrin and inhibin by Sertoli cells was observed in the presence of antibody, whereas spermatocyte adhesiveness was unchanged. Using northern blot analysis, the steady state levels of transferrin mRNA decreased when the anti-liver-regulating protein antibody was added to the Sertoli cell-spermatocyte cocultures or to the Sertoli cell-liver biliary epithelial cell cocultures. The data demonstrate the role of the liver-regulating protein in cell-cell contact-mediated regulation of Sertoli function by primary spermatocytes and the important implications of this cell contact-dependent control in testicular activity.


1984 ◽  
Vol 438 (1 Hormonal Cont) ◽  
pp. 684-687 ◽  
Author(s):  
M. BENAHMED ◽  
J. REVENTOS ◽  
E. TABONE ◽  
J. M. SAEZ

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