scholarly journals Cysteine-rich secretory proteins are not exclusively expressed in the male reproductive tract

2008 ◽  
Vol 237 (11) ◽  
pp. 3313-3323 ◽  
Author(s):  
Thulasimala Reddy ◽  
Gerard M. Gibbs ◽  
D. Jo Merriner ◽  
Jeffrey B. Kerr ◽  
Moira K. O'Bryan
Keyword(s):  
Reproductive Tract ◽  
Secretory Proteins ◽  
Male Reproductive Tract

425. Expression of mammalian cysteine-rich secretory proteins in the mouse model

2008 ◽  
Vol 20 (9) ◽  
pp. 105
Author(s):  
T. Reddy ◽  
G. M. Gibbs ◽  
D. J. Merriner ◽  
J. B. Kerr ◽  
M. K. O.'Bryan
Keyword(s):  
Expression Profile ◽  
Reproductive Tract ◽  
Sequence Similarity ◽  
Immunohistochemical Analysis ◽  
The Body ◽  
Mouse Tissue ◽  
Amino Acid Sequence Similarity ◽  
Secretory Proteins ◽  
Male Reproductive Tract ◽  
High Amino Acid

Mammalian cysteine rich secretory proteins are a family of four proteins exhibiting a high amino acid sequence similarity and belonging to the CAP (Cysteine rich secretory proteins, Antigen-5 proteins and the plant Pathogenesis related-1 proteins) superfamily of proteins. They are designated CRISP 1, 2, 3 and 4. Structurally, mammalian CRISP’s are characterised by 16 cysteine residues involved in intra-molecular di-sulfide bonds and the formation of 2 domains, ie., the CRISP domain (CD) and CAP domain. Whilst studies on mouse CRISP2 suggest that the CD is involved in ion channel regulation, studies on non-mammalian CAP superfamily members suggest that the CAP domain is involved in proteolytic activity.They are predominantly expressed and localised in the male reproductive tract, however, the EST expression databases suggest that mammalian CRISPs are expressed more widely than in the male reproductive tract. The objective of this study was therefore to conclusively define the expression and localisation of each CRISP protein in a mammalian system.A reverse transcription PCR expression profile and immunohistochemical analysis of 16 mouse tissue was conducted to establish the expression and localisation of each of the four CRISPs. These data showed that although the CRISPs have a strong expression and localisation bias to the male reproductive tract, they are widely distributed throughout the body in mice, including the ovary, uterus, and mammary gland. Whilst each CRISP has a clear expression profile, there was a striking localisation of androgen regulated CRISPs (1, 3, 4) in immune tissue including the spleen and thymus. Such a localisation raises the spectre of a role for CRISPs in the normal physiology and disease of several organs.

Induction of prostatic morphology and secretion in urothelium by seminal vesicle mesenchyme

Development ◽  
1995 ◽  
Vol 121 (7) ◽  
pp. 2199-2207 ◽  
Author(s):  
A.A. Donjacour ◽  
G.R. Cunha
Keyword(s):  
Seminal Vesicle ◽  
Reproductive Tract ◽  
Urogenital Sinus ◽  
Secretory Proteins ◽  
Ductus Deferens ◽  
Male Reproductive Tract ◽  
Mesodermal Origin ◽  
Tissue Recombination ◽  
Endodermal Origin ◽  
Recombination Experiments

Mesenchymal-epithelial interactions are essential for the development of the male reproductive tract. Tissue recombination experiments have been used to define the characteristics of these interactions. When mesenchyme, embryonic connective tissue, is recombined with epithelium from another organ an instructive induction may occur in which the developmental fate of the epithelium is altered. Instructive inductions are most common when the epithelium that is removed from the mesenchyme and the epithelium that is recombined with the mesenchyme are from the same germ layer. All of the mesenchyme of the male reproductive tract is of mesodermal origin. The epithelia of these organs are derived from either the mesodermal Wolffian duct epithelium or the endodermal urogenital sinus epithelium. Urogenital sinus mesenchyme can instructively induce bladder and urethral epithelium to form prostate (Donjacour, A. A. and Cunha, G. R. (1993) Endocrinol. 132, 2342–2350) and seminal vesicle mesenchyme can instructively induce epithelium from the ductus deferens and ureter (Cunha, G. R., Young, P., Higgins, S. J. and Cooke, P. S. (1991) Development 111, 145–158) to form seminal vesicle. To see whether inductive interactions could occur across germ layers in this system, seminal vesicle mesenchyme, normally associated with a mesodermal epithelium, was recombined with epithelium from neonatal or adult bladder or urethra, which are of endodermal origin. The resulting tissue recombinants were analyzed histologically and by immunocytochemistry and western blotting with antibodies to prostatic and seminal vesicle secretory proteins. Full prostatic differentiation was observed in tissue recombinants made with seminal vesicle mesenchyme plus either adult or neonatal bladder or urethral epithelium.(ABSTRACT TRUNCATED AT 250 WORDS)

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.

Sign in / Sign up

Export Citation Format

Share Document