scholarly journals Localization of 11β-Hydroxysteroid Dehydrogenase Types 1 and 2 in the Male Reproductive Tract

Endocrinology ◽  
2003 ◽  
Vol 144 (7) ◽  
pp. 3101-3106 ◽  
Author(s):  
Brendan J. Waddell ◽  
Susan Hisheh ◽  
Zygmunt S. Krozowski ◽  
Peter J. Burton
Keyword(s):  
Reproductive Tract ◽  
Hydroxysteroid Dehydrogenase ◽  
Male Reproductive Tract

scholarly journals 11β-Hydroxysteroid dehydrogenase enzymes in the testis and male reproductive tract of the boar (Sus scrofa domestica) indicate local roles for glucocorticoids in male reproductive physiology

Reproduction ◽  
2007 ◽  
Vol 134 (3) ◽  
pp. 473-482 ◽  
Author(s):  
Victoria Sharp ◽  
Lisa M Thurston ◽  
Robert C Fowkes ◽  
Anthony E Michael
Keyword(s):  
Reproductive Tract ◽  
Vas Deferens ◽  
Physiological Role ◽  
Kinetic Studies ◽  
Hydroxysteroid Dehydrogenase ◽  
Enzyme Expression ◽  
Male Reproductive Tract ◽  
Cortisol Metabolism ◽  
Sus Scrofa Domestica ◽  
Caput Epididymidis

11β-Hydroxysteroid dehydrogenase (11βHSD) enzymes modulate the target cell actions of corticosteroids by catalysing metabolism of the physiological glucocorticoid (GC), cortisol, to inert cortisone. Recent studies have implicated GCs in boar sperm apoptosis. Hence, the objective of this study was to characterise 11βHSD enzyme expression and activities in the boar testis and reproductive tract. Although 11βHSD1 and 11βHSD2 mRNA transcripts and proteins were co-expressed in all tissues, cortisol–cortisone interconversion was undetectable in the corpus and cauda epididymides, vas deferens, vesicular and prostate glands, irrespective of nucleotide cofactors. In contrast, homogenates of boar testis, caput epididymidis and bulbourethral gland all displayed pronounced 11βHSD activities in the presence of NADPH/NADP+ and NAD+, and the penile urethra exhibited NAD+-dependent 11β-dehydrogenase activity. In kinetic studies, homogenates of boar testis, caput epididymidis and bulbourethral gland oxidised cortisol with Km values of 237–443 and 154–226 nmol/l in the presence of NADP+ and NAD+ respectively. Maximal rates of NADP+-dependent cortisol oxidation were 7.4- to 28.5-fold greater than the Vmax for NADPH- dependent reduction of cortisone, but were comparable with the rates of NAD+-dependent cortisol metabolism. The relatively low Km estimates for NADP+ -dependent cortisol oxidation suggest that either the affinity of 11βHSD1 has been increased or the cortisol inactivation is catalysed by a novel NADP+-dependent 11βHSD enzyme in these tissues. We conclude that in the boar testis, caput epididymidis and bulbourethral gland, NADP+- and NAD+-dependent 11βHSD enzymes catalyse net inactivation of cortisol, consistent with a physiological role in limiting any local actions of GCs within these reproductive tissues.

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.

Changes in the Male Reproductive Organs of the Dugong, Dugong dugon (Sirenia: Dugondidae) with Age and Reproductive Activity

1984 ◽  
Vol 32 (6) ◽  
pp. 721 ◽  
Author(s):  
H Marsh ◽  
GE Heinsohn ◽  
TD Glover
Keyword(s):  
Reproductive Tract ◽  
Prostate Gland ◽  
Reproductive Activity ◽  
Reproductive Organs ◽  
Seminal Vesicles ◽  
Growth Layer ◽  
Male Reproductive Tract ◽  
Qualitative And Quantitative ◽  
Quantitative Examination ◽  
Testicular Histology

The anatomy and histology of the male reproductive tract of the dugong (Dugong dugon) is described. Each testis and its adjacent epididymis lie immediately caudal to the corresponding kidney. The seminal vesicles are large but there is no discrete prostate gland and the bulbo-urethral glands are also diffuse. Both qualitative and quantitative examination of the testes and epididymides of 59 males whose ages have been estimated from tusk dentinal growth layer counts indicate that the male dugong does not produce spermatozoa continuously, despite the absence of a distinct breeding season. Individual dugongs were observed with testes at all stages between complete quiescence and full spermatogenesis, and only 10 of the 40 mature males had fully spermatogenic testes and epididymides packed with spermatozoa. Androgenic and spermatogenic activity of the testes appeared to be in phase, but the testicular histology of some old males suggested that they may have been sterile for long periods.

Methyl-parathion bioactivation in the male reproductive tract: From mRNA to protein expression of involved CYP isoforms

2009 ◽  
Vol 189 ◽  
pp. S145
Author(s):  
Betzabet Quintanilla-Vega ◽  
Patricia Espíritu-Gordillo ◽  
Yuliana Palacios-Gil ◽  
Margarita Guaderrama-Díaz ◽  
María de Jesús Solís-Heredia ◽  
...  
Keyword(s):  
Protein Expression ◽  
Methyl Parathion ◽  
Reproductive Tract ◽  
Male Reproductive Tract ◽  
Cyp Isoforms

scholarly journals Identification of multiple male reproductive tract-specific proteins that regulate sperm migration through the oviduct in mice

2019 ◽  
Vol 116 (37) ◽  
pp. 18498-18506 ◽  
Author(s):  
Yoshitaka Fujihara ◽  
Taichi Noda ◽  
Kiyonori Kobayashi ◽  
Asami Oji ◽  
Sumire Kobayashi ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Male Fertility ◽  
Reproductive Tract ◽  
Gene Families ◽  
Gene Clusters ◽  
Mutant Mice ◽  
Male Reproductive Tract ◽  
Sperm Migration ◽  
Specific Proteins ◽  
Multiple Male

CRISPR/Cas9-mediated genome editing technology enables researchers to efficiently generate and analyze genetically modified animals. We have taken advantage of this game-changing technology to uncover essential factors for fertility. In this study, we generated knockouts (KOs) of multiple male reproductive organ-specific genes and performed phenotypic screening of these null mutant mice to attempt to identify proteins essential for male fertility. We focused on making large deletions (dels) within 2 gene clusters encoding cystatin (CST) and prostate and testis expressed (PATE) proteins and individual gene mutations in 2 other gene families encoding glycerophosphodiester phosphodiesterase domain (GDPD) containing and lymphocyte antigen 6 (Ly6)/Plaur domain (LYPD) containing proteins. These gene families were chosen because many of the genes demonstrate male reproductive tract-specific expression. AlthoughGdpd1andGdpd4mutant mice were fertile, disruptions ofCstandPategene clusters andLypd4resulted in male sterility or severe fertility defects secondary to impaired sperm migration through the oviduct. While absence of the epididymal protein families CST and PATE affect the localization of the sperm membrane protein A disintegrin and metallopeptidase domain 3 (ADAM3), the sperm acrosomal membrane protein LYPD4 regulates sperm fertilizing ability via an ADAM3-independent pathway. Thus, use of CRISPR/Cas9 technologies has allowed us to quickly rule in and rule out proteins required for male fertility and expand our list of male-specific proteins that function in sperm migration through the oviduct.

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