Changes in distribution of labile zinc in mouse spermatozoa during maturation in the epididymis assessed by the fluorophore Zinquin

1996 ◽  
Vol 8 (7) ◽  
pp. 1097 ◽  
Author(s):  
PD Zalewski ◽  
X Jian ◽  
LL Soon ◽  
WG Breed ◽  
RF Seamark ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Reproductive Tract ◽  
Regional Distribution ◽  
Sodium Dodecyl ◽  
Sperm Head ◽  
Male Reproductive Tract ◽  
Intracellular Location ◽  
And Function ◽  
Triton X

The Zn(II)-specific fluorophore Zinquin was used to determine the regional distribution of free or loosely-bound Zn(II) in mouse spermatozoa. Spermatozoa from the testes exhibited bright fluorescence over the entire head; those from the caput epididymides generally fluoresced more brightly in the post-acrosomal region; and spermatozoa from the caudae epididymides fluoresced less brightly, with foci of fluorescence over the sperm head which were lost after extraction with Triton X-100 and hence appeared to be membrane-associated. Treatment of cauda sperm with sodium dodecyl sulfate resulted in a bright uniform Zinquin fluorescence in the heads, similar to that observed in caput sperm, indicating that the two types of sperm have similar amounts of head Zn(II) but that the availability of Zn(II) for binding Zinquin is different. By contrast, the intensity of tail fluorescence was similar in spermatozoa from different regions of the male reproductive tract and was largely unaffected by Triton X-100 extraction, consistent with an intracellular location. Similar differences were observed between caput sperm and cauda sperm in the rat. It is concluded that visualization and measurement of free or loosely-bound Zn(II) in subcellular compartments of spermatozoa should facilitate investigation of the role of this metal in the development and function of spermatozoa and abnormalities that might accompany infertility and Zn(II) deficiency.

Carboxylesterase overexpression in the male reproductive tract: a universal safeguarding mechanism?

1999 ◽  
Vol 11 (3) ◽  
pp. 133 ◽  
Author(s):  
A. T. Mikhailov ◽  
M. Torrado
Keyword(s):  
Reproductive Tract ◽  
Expression Patterns ◽  
Cell Lineage ◽  
Environmental Chemicals ◽  
Male Reproductive Tract ◽  
Morphological Organization ◽  
Associated Functions ◽  
And Function ◽  
Hypothetical Explanation

Data on expression patterns of carboxylesterases in the male reproductive tract of different animal groups (i.e. bivalve mollusks, fruitflies and rodents) are summarized to highlight some particularly interesting questions in the context of sperm differentiation, maturation and function. The male reproduc-tive system, in spite of extreme variation in the anatomical/morphological organization in different species, is characterized by similar patterns of male-dependent carboxylesterase overexpression. The phenomenon of conserved carboxylesterase overexpression indicates similar male sex-associated functions of the enzymes. There is possible evidence of carboxylesterase recruitment by male reproductive-tract tissues indi-cating that it could be adaptive for spermatogenesis, sperm maturation and sperm use. Moreover, this idea can be extended to include a sperm cell lineage protection. This issue is discussed in the light of recent data on environmental reproductive xenobiotics that can provide a basis for a hypothetical explanation of car-boxylesterase overexpression in the male reproductive tract. Based on a well-known role of car-boxylesterases in detoxification of environmental chemicals such as organophosphate pesticides, it is proposed that various male genital tract carboxylesterases may be characterized by a similar physiological function to protect the male reproductive system against xenobiotic influences that could provoke its dys-function, thus altering sperm differentiation and maturation.

scholarly journals Estrogen Modulates Glycerol Permeability in Sertoli Cells through Downregulation of Aquaporin-9

Cells ◽  
2018 ◽  
Vol 7 (10) ◽  
pp. 153 ◽  
Author(s):  
Raquel Bernardino ◽  
David Carrageta ◽  
Ana Silva ◽  
Giuseppe Calamita ◽  
Marco Alves ◽  
...  
Keyword(s):  
Sertoli Cells ◽  
Reproductive Tract ◽  
Fluid Secretion ◽  
Male Reproductive Tract ◽  
Aquaporin 9 ◽  
Important Regulator ◽  
17Β Estradiol ◽  
And Function ◽  
Glycerol Permeability

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 evaluated by stopped-flow light scattering. We were able to identify the expression of AQP3 and AQP9 in mSCs where AQP9 is more abundant than AQP3. Our results show that high E2 levels decrease AQP9 mRNA abundance with no influence on AQP3 in mSCs. Interestingly, high E2 levels decreased mSCs’ permeability to glycerol, while downregulating AQP9 expression, thus suggesting a novel mechanism by which E2 modulates fluid secretion in the testis. In conclusion, E2 is an important regulator of mSCs physiology and secretion through changes in AQP9 expression and function. Thus, alterations in glycerol permeability induced by E2 may be the cause for male infertility in cases associated with the presence of high E2 levels.

Solubility and adsorption behaviors of chlorophenols in the presence of surfactant

1997 ◽  
Vol 35 (7) ◽  
pp. 123-130 ◽  
Author(s):  
J. C. Liu ◽  
P. S. Chang
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Critical Micelle Concentration ◽  
Sodium Dodecyl ◽  
Adsorption Behaviors ◽  
Brij 35 ◽  
Important Index ◽  
Dodecyl Sulfate ◽  
Triton X

The solubility of chlorophenols as affected by surfactant was investigated. Three kinds of surfactant, sodium dodecyl sulfate, Triton X-100, and Brij 35, were utilized. The solubilization of chlorophenols by surfactant follows the order of 2,4,6-trichlorophenol > 2,4-dichlorophenol > 2,6-dichlorophenol > 2-chlorophenol; and the critical micelle concentration is an important index. The adsorption reactions of 2,4-dichlorophenol and 2,4,6- trichlorophenol onto hydrous montmorillonite in the presence of surfactant were examined. The presence of surfactant decreased the adsorption of chlorophenols significantly. The roles of hydrophobicity of chlorophenols in solubilization and adsorption behaviors are discussed.

The Effect of PDE5 Inhibitors on the Male Reproductive Tract

2020 ◽  
Vol 26 ◽  
Author(s):  
Nikolaos Sofikitis ◽  
Aris Kaltsas ◽  
Fotios Dimitriadis ◽  
Jens Rassweiler ◽  
Nikolaos Grivas ◽  
...  
Keyword(s):  
Male Infertility ◽  
Reproductive Tract ◽  
Tunica Albuginea ◽  
Scientific Data ◽  
Secretory Function ◽  
Pde5 Inhibitors ◽  
Male Reproductive Tract ◽  
Review Study ◽  
Phosphodiesterase 5

The therapeutic range of cyclic nucleotide phosphodiesterase 5 inhibitors (PDE5) inhibitors is getting wider in the last years. This review study focuses on the potential employment of PDE5 inhibitors as an adjunct tool for the therapeutic management of male infertility. The literature tends to suggest a beneficial effect of PDE5 inhibitors on Leydig and Sertoli cells secretory function. It also appears that PDE5 inhibitors play a role in the regulation of the contractility of the testicular tunica albuginea and the epididymis. Moreover scientific data suggest that PDE5 inhibitors enhance the prostatic secretory function leading to an improvement in sperm motility. Other studies additionally demonstrate a role of PDE5 inhibitors in the regulation of sperm capacitation process. Placebo-controlled, randomized, blind studies are necessary to unambiguously incorporate PDE5 inhibitors as an adjunct tool for the pharmaceutical treatment of semen disorders and male infertility.

Different submicellar solubilization mechanisms revealed by 1H NMR and 2D diffusion ordered spectroscopy (DOSY)

2020 ◽  
Vol 22 (19) ◽  
pp. 11075-11085
Author(s):  
Mengjian Wu ◽  
Zhaoxia Wu ◽  
Shangwu Ding ◽  
Zhong Chen ◽  
Xiaohong Cui
Keyword(s):  
Nmr Spectroscopy ◽  
Sodium Dodecyl Sulfate ◽  
1H Nmr ◽  
Sodium Dodecyl ◽  
Butyl Methacrylate ◽  
H Nmr ◽  
Molecular Scale ◽  
Two Systems ◽  
Dodecyl Sulfate ◽  
Triton X

Different submicellar solubilization mechanisms of two systems, Triton X-100/tetradecane and sodium dodecyl sulfate (SDS)/butyl methacrylate, are revealed on the molecular scale by 1H NMR spectroscopy and 2D diffusion ordered spectroscopy (DOSY).

A metalloproteinase extracellularly released byCrithidia deanei

2003 ◽  
Vol 49 (10) ◽  
pp. 625-632 ◽  
Author(s):  
Claudia Masini d'Avila-Levy ◽  
Rodrigo F Souza ◽  
Rosana C Gomes ◽  
Alane B Vermelho ◽  
Marta H Branquinha
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Residual Activity ◽  
Major Protein ◽  
Motile Cells ◽  
Sds Page ◽  
Triton X

Actively motile cells from a cured strain of Crithidia deanei released proteins in phosphate buffer (pH 7.4). The molecular mass of the released polypeptides, which included some proteinases, ranged from 19 to 116 kDa. One of the major protein bands was purified to homogeneity by a combination of anion-exchange and gel filtration chromatographs. The apparent molecular mass of this protein was estimated to be 62 kDa by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE). The incorporation of gelatin into SDS–PAGE showed that the purified protein presented proteolytic activity in a position corresponding to a molecular mass of 60 kDa. The enzyme was optimally active at 37 °C and pH 6.0 and showed 25% of residual activity at 28 °C for 30 min. The proteinase was inhibited by 1,10-phenanthroline and EDTA, showing that it belonged to the metalloproteinase class. A polyclonal antibody to the leishmanial gp63 reacted strongly with the released C. deanei protease. After Triton X-114 extraction, an enzyme similar to the purified metalloproteinase was detected in aqueous and detergent-rich phases. The detection of an extracellular metalloproteinase produced by C. deanei and some other Crithidia species suggests a potential role of this released enzyme in substrate degradation that may be relevant to the survival of trypanosomatids in the host.Key words: endosymbiont, trypanosomatid, extracellular, proteinase.

scholarly journals ATP secretion in the male reproductive tract: essential role of CFTR

2012 ◽  
Vol 590 (17) ◽  
pp. 4209-4222 ◽  
Author(s):  
Ye Chun Ruan ◽  
Winnie W. C. Shum ◽  
Clémence Belleannée ◽  
Nicolas Da Silva ◽  
Sylvie Breton
Keyword(s):  
Essential Role ◽  
Reproductive Tract ◽  
Male Reproductive Tract ◽  
Atp Secretion
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