Low testicular zinc level, p53 expression and impairment of Sertoli cell phagocytosis of residual bodies in rat subjected to psychological stress

Andrologia ◽  
2021 ◽  
Author(s):  
Leke Jacob Medubi ◽  
Oluwole Busayo Akinola ◽  
Adeoye Oyetunji Oyewopo
Keyword(s):  
Psychological Stress ◽  
Sertoli Cell ◽  
Zinc Level ◽  
P53 Expression ◽  
Residual Bodies

scholarly journals Ezrin is an Actin Binding Protein That Regulates Sertoli Cell and Spermatid Adhesion During Spermatogenesis

Endocrinology ◽  
2014 ◽  
Vol 155 (10) ◽  
pp. 3981-3995 ◽  
Author(s):  
N. Ece Gungor-Ordueri ◽  
Elizabeth I. Tang ◽  
Ciler Celik-Ozenci ◽  
C. Yan Cheng
Keyword(s):  
Sertoli Cell ◽  
Sertoli Cells ◽  
Adherens Junction ◽  
Actin Binding ◽  
Permeability Barrier ◽  
Tight Junction Permeability ◽  
Residual Bodies ◽  
Cell Interface

Abstract During spermatogenesis, the transport of spermatids and the release of sperms at spermiation and the remodeling of the blood-testis barrier (BTB) in the seminiferous epithelium of rat testes require rapid reorganization of the actin-based cytoskeleton. However, the mechanism(s) and the regulatory molecule(s) remain unexplored. Herein we report findings that unfold the functional significance of ezrin in the organization of the testis-specific adherens junction at the spermatid-Sertoli cell interface called apical ectoplasmic specialization (ES) in the adluminal compartment and the Sertoli cell-cell interface known as basal ES at the BTB. Ezrin is expressed at the basal ES/BTB in all stages, except from late VIII to IX, of the epithelial cycle. Its knockdown by RNA interference (RNAi) in vitro perturbs the Sertoli cell tight junction-permeability barrier via a disruption of the actin microfilaments in Sertoli cells, which in turn impeded basal ES protein (eg, N-cadherin) distribution, perturbing the BTB function. These findings were confirmed by a knockdown study in vivo. However, the expression of ezrin at the apical ES is restricted to stage VIII of the cycle and limited only between step 19 spermatids and Sertoli cells. A knockdown of ezrin in vivo by RNAi was found to impede spermatid transport, causing defects in spermiation in which spermatids were embedded deep inside the epithelium, and associated with a loss of spermatid polarity. Also, ezrin was associated with residual bodies and phagosomes, and its knockdown by RNAi in the testis also impeded the transport of residual bodies/phagosomes from the apical to the basal compartment. In summary, ezrin is involved in regulating actin microfilament organization at the ES in rat testes.

scholarly journals PARP-I and p53 expression in Sertoli cell during rat ontogenesis

2010 ◽  
Vol 83 (1) ◽  
Author(s):  
R. Taherian ◽  
L. Scarabelli ◽  
I. Demori ◽  
C. Lanza ◽  
S.. Palmero
Keyword(s):  
Sertoli Cell ◽  
P53 Expression

Wild-type p53-induced phosphatase 1 (WIP1) regulates the proliferation of swine Sertoli cells through P53

2020 ◽  
Vol 32 (18) ◽  
pp. 1350
Author(s):  
Bingyuan Wang ◽  
Mingrui Zhang ◽  
Jingjing Che ◽  
Kui Li ◽  
Yulian Mu ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
Male Reproduction ◽  
Wild Type ◽  
P53 Expression ◽  
Cancer Types ◽  
Wild Type P53 ◽  
Oncogenic Function ◽  
Sertoli Cell Line

Wild-type p53-induced phosphatase 1 (WIP1) plays an oncogenic function by increasing cell proliferation in various cancer types. Deficiency in WIP1 expression leads to male infertility, possibly by impairing the blood–testis barrier and spermatogenesis. However, how WIP1 functions in the Sertoli cells to affect male reproduction remains unclear. Thus, in the present study we used a swine Sertoli cell line to investigate whether WIP1 regulated the proliferation of Sertoli cells to participate in male reproduction. The WIP1 inhibitor GSK2830371, WIP1-short interference (si) RNAs and an upstream microRNA (miR-16) were used to inhibit the expression of WIP1, after which the proliferation of swine Sertoli cells, P53 expression and the levels of P53 phosphorylation were determined. Inhibiting WIP1 expression suppressed swine Sertoli cell proliferation, increased P53 expression and increased levels of P53 phosphorylation. In addition, overexpression of miR-16 in swine Sertoli cells resulted in a decrease in WIP1 expression and increases in both P53 expression and P53 phosphorylation. Together, these findings suggest that WIP1 positively regulates the proliferation of swine Sertoli cells by inhibiting P53 phosphorylation, and the miR-16 is likely also involved by targeting WIP1.

scholarly journals Stimulation of rat Sertoli cell secretory activity in vitro by germ cells and residual bodies

Reproduction ◽  
1986 ◽  
Vol 77 (2) ◽  
pp. 489-498 ◽  
Author(s):  
B. Le Magueresse ◽  
F. Le Gac ◽  
M. Loir ◽  
B. Jegou
Keyword(s):  
Sertoli Cell ◽  
Germ Cells ◽  
Secretory Activity ◽  
Residual Bodies ◽  
Stimulation Of

Residual Bodies Stimulate Rat Sertoli Cell Plasminogen Activator Activity

1998 ◽  
Vol 250 (1) ◽  
pp. 59-62 ◽  
Author(s):  
Francesco Sigillo ◽  
Gilles Pernod ◽  
Lucien Kolodie ◽  
Mohamed Benahmed ◽  
Brigitte Le Magueresse-Battistoni
Keyword(s):  
Plasminogen Activator ◽  
Sertoli Cell ◽  
Plasminogen Activator Activity ◽  
Residual Bodies

Freeze-etch observations on the tight junctions of sertoli cells grown in organ culture with FSH

1978 ◽  
Vol 36 (2) ◽  
pp. 340-341
Author(s):  
Rita Meyer ◽  
Zoltan Posalaky ◽  
Dennis Mcginley
Keyword(s):  
Organ Culture ◽  
Tight Junctions ◽  
Sertoli Cell ◽  
Germ Cells ◽  
Sertoli Cells ◽  
Barrier Function ◽  
Cell Junction ◽  
Intramembranous Particles ◽  
Junctional Complexes ◽  
Oriented Parallel

The Sertoli cell tight junctional complexes have been shown to be the most important structural counterpart of the physiological blood-testis barrier. In freeze etch replicas they consist of extensive rows of intramembranous particles which are not only oriented parallel to one another, but to the myoid layer as well. Thus the occluding complex has both an internal and an overall orientation. However, this overall orientation to the myoid layer does not seem to be necessary to its barrier function. The 20 day old rat has extensive parallel tight junctions which are not oriented with respect to the myoid layer, and yet they are inpenetrable by lanthanum. The mechanism(s) for the control of Sertoli cell junction development and orientation has not been established, although such factors as the presence or absence of germ cells, and/or hormones, especially FSH have been implicated.

1419: A Multi-Step Kinase-Based Sertoli Cell Autocrine-Amplifying Loop Regulates Prostaglandins, their Receptors, and Cytokines

2006 ◽  
Vol 175 (4S) ◽  
pp. 458-458
Author(s):  
Tomomoto Ishikawa ◽  
Masato Fujisawa ◽  
Patricia L. Morris
Keyword(s):  
Sertoli Cell
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