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)

Induction of functional cytodifferentiation in the epithelium of tissue recombinants. II. Instructive induction of Wolffian duct epithelia by neonatal seminal vesicle mesenchyme

Development ◽  
1989 ◽  
Vol 106 (2) ◽  
pp. 235-250 ◽  
Author(s):  
S.J. Higgins ◽  
P. Young ◽  
G.R. Cunha
Keyword(s):  
Seminal Vesicle ◽  
Normal Development ◽  
Seminal Vesicles ◽  
Wolffian Duct ◽  
Secretory Proteins ◽  
Ductus Deferens ◽  
Tissue Sections ◽  
Duct Epithelium ◽  
Mouse Tissues ◽  
Renal Grafts

When grown as renal grafts in adult male hosts, the upper (cranial), middle and lower (caudal) portions of fetal mouse and rat Wolffian ducts developed into epididymis, epididymis plus ductus deferens, and seminal vesicle, respectively. In heterotypic tissue recombinants, the epithelia from upper and middle Wolffian ducts were instructively induced to undergo seminal vesicle morphogenesis by neonatal seminal vesicle mesenchyme. Functional cytodifferentiation was examined in these recombinants using antibodies against major androgen-dependent, seminal vesicle-specific secretory proteins. The instructively induced Wolffian duct epithelia synthesized normal amounts of all of the secretory proteins characteristic of mature seminal vesicles, as judged by immunocytochemistry on tissue sections and gel electrophoresis plus immunoblotting of secretions extracted from the recombinants. In heterospecific recombinants composed of rat and mouse tissues, the seminal vesicle proteins induced were specific for the species that had provided the epithelium. This showed that the seminal vesicle epithelium in the recombinants was derived from instructively induced Wolffian duct epithelium and not from epithelial contamination of the mesenchymal inductor. Upper Wolffian duct epithelium, instructively induced to undergo seminal vesicle morphogenesis, did not express epididymis-specific secretory proteins, showing that its normal development had been simultaneously repressed.

scholarly journals Location of a membrane-bound carbonic anhydrase isoenzyme (CA IV) in the human male reproductive tract.

1993 ◽  
Vol 41 (5) ◽  
pp. 751-757 ◽  
Author(s):  
S Parkkila ◽  
A K Parkkila ◽  
K Kaunisto ◽  
A Waheed ◽  
W S Sly ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Carbonic Anhydrase ◽  
Reproductive Tract ◽  
Muscle Layer ◽  
Apical Plasma Membrane ◽  
Specific Staining ◽  
Ductus Deferens ◽  
Male Reproductive Tract ◽  
Human Male ◽  
Membrane Bound

We studied the location of a membrane-bound carbonic anhydrase (CA IV) in the human male reproductive tract using a specific antiserum to human CA IV in conjunction with immunoblotting, immunoperoxidase, and immunofluorescence techniques. The microvilli and apical plasma membrane of the epithelial cells and the subepithelial smooth muscle layer of the epididymis, ductus deferens, and ampulla of the ductus deferens showed specific staining for CA IV. The epithelial cells of the prostate and seminal vesicle failed to stain for CA IV, however, whereas the subepithelial smooth muscle layer showed positive staining. No specific staining for CA II was seen in the epithelium of the epididymal duct or the proximal ductus deferens. The presence of CA IV in the epididymis was confirmed by immunoblotting, which revealed 35 KD and 33 KD polypeptides. The results show that the microvilli and the apical plasma membrane of the lining epithelium of the epididymal duct, ductus deferens, and ampulla of the ductus deferens contain the membrane-bound carbonic anhydrase isoenzyme IV. The presence of the enzyme in the epithelium of the epididymis and ductus deferens is probably linked to the acidification of the epididymal fluid that prevents premature sperm activation. Its physiological role in the smooth muscle cells remains to be elucidated.

X-Ray Diffraction Study on Human Male Reproductive Tract and Semen

2009 ◽  
Vol 76 (3) ◽  
pp. 198-202 ◽  
Author(s):  
K.P. Skandhan ◽  
S. Amith ◽  
K.P.S. Avni
Keyword(s):  
Seminal Vesicle ◽  
Calcium Silicate ◽  
Reproductive Tract ◽  
Prostate Gland ◽  
X Ray Diffraction ◽  
Male Reproductive Tract ◽  
X Ray ◽  
Human Male ◽  
Barium Silicate ◽  
Copper Gold

In the present study authors had separated testis, epididymis-caput, corpus, cauda, vas deferens, seminal vesicle, prostate gland and bulbourethral gland from human male reproductive tract, made it to ash form. Semen also underwent same procedure. All samples had undergone X-ray diffraction analysis. Results Results showed there where two distinct rings for each sample. We named it is “A” &” B”. Under “A” Barium silicate, Barium silicate hydrate and three metal complexes of copper, gold and zinc were seen. Under “B” Calcium silicate and calcium silicate hydrate were observed. Both “A” and “B” were seen throughout the length (expect for “A” is seminal vesicle) and in semen. Conclusions A tri metal complex of copper, gold and zinc is reported in this study, is first of its kind in Biology.

scholarly journals The Male Reproductive Structure and Spermatogenesis of Trypophloeus Klimeschi Eggers (Coleoptera: Curculionidae: Scolytinae)

2019 ◽  
Author(s):  
Jing Gao ◽  
Guanqun Gao ◽  
Lulu Dai ◽  
Jiaxing Wang ◽  
Hui Chen
Keyword(s):  
Seminal Vesicle ◽  
Reproductive Tract ◽  
Vas Deferens ◽  
Ejaculatory Duct ◽  
Reproductive Organ ◽  
Accessory Gland ◽  
Male Reproductive Tract ◽  
Short Branch ◽  
Male Reproductive Organ ◽  
Dense Band

Abstract Background Trypophloeus Klimeschi Eggers (Coleoptera: Curculionidae: Scolytinae) is one of the most destructive pests of Populus alba var. pyramidalis (Bunge), resulting in significant losses in economic, ecological and social benefits in China’s northwest shelter forest. But research of reproductive system, spermiogenesis and spermatozoon ultrastructure of T. klimeschi that is basis of phylogeny, reproductive biology and controlling is still black. Results The male reproductive organ of T. klimeschi is composed of testis, seminal vesicle, strand shaped accessory gland containing long branch of strand shaped accessory gland and short branch of strand shaped accessory gland, curly accessory gland, vas deferens and a common ejaculatory duct. The number of sperm per cyst is 350~512. Its spermatozoon is slender, measuring about 75 μm in length and 0.5 μm in wide and composed of a 3-layred acrosomal complex, a nucleus with two different states of aggregation, two mitochondrial derivatives with dark crystal, a 9+9+2 axoneme that run more or less parallel to mitochondrial derivatives, two crystalline accessory bodies with a big compact “puff”-like expansion. Especially in the seminal vesicle, its long flagella folded into several turns and the whole sperm is wrapped in a film.Conclusion The general morphology of male reproductive tract, the spermatogenesis and the spermatozoa of T. klimeschi are, for the most part, similar to the majority of the Curculionidae. However, some distinct differences were found: the low electron-dense band in the cytoplasm of spermatocytes; two different aggregation states of spermatozoon nucleus; especially the stored way of T. klimeschi spermatozoa.

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.

Neonatal seminal vesicle mesenchyme induces a new morphological and functional phenotype in the epithelia of adult ureter and ductus deferens

Development ◽  
1991 ◽  
Vol 111 (1) ◽  
pp. 145-158 ◽  
Author(s):  
G.R. Cunha ◽  
P. Young ◽  
S.J. Higgins ◽  
P.S. Cooke
Keyword(s):  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Developmental Plasticity ◽  
Androgen Receptors ◽  
Seminal Vesicles ◽  
Neonatal Mouse ◽  
Secretory Proteins ◽  
Complete Spectrum ◽  
Ductus Deferens ◽  
Functional Phenotype

Mesenchyme from neonatal mouse and rat seminal vesicles (SVM) was grown in association with postnatal (adult) epithelial cells from the ureter (URE) and ductus deferens (DDE) in chimeric tissue recombinants composed of mouse mesenchyme and rat epithelium or vice versa. Functional cytodifferentiation was examined in these SVM + URE and SVM + DDE tissue recombinants with antibodies against major androgen-dependent seminal-vesicle-specific secretory proteins. Adult DDE and URE were induced to express seminal cytodifferentiation and produced the complete spectrum of major seminal vesicle secretory (SVS) proteins. The SVS proteins produced were specific for the species that provided the epithelium. In the case of SVM + URE recombinants, the URE, which normally lacks androgen receptors (AR), expressed AR. These results demonstrate that adult epithelial cells retain a developmental plasticity equivalent to their undifferentiated fetal counterparts and are capable of being reprogrammed to express a completely new morphological, biochemical and functional phenotype.

Characterization and biological role of cysteine-rich venom protein belonging to CRISPs from turkey seminal plasma

2021 ◽  
Author(s):  
Mariola Słowińska ◽  
Laura Pardyak ◽  
Ewa Liszewska ◽  
Sylwia Judycka ◽  
Joanna Bukowska ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Seminal Plasma ◽  
Reproductive Tract ◽  
Protein Localization ◽  
Mass Spectrometry Analysis ◽  
Etiologic Factor ◽  
Secretory Proteins ◽  
Ductus Deferens ◽  
Venom Protein

Abstract Turkey semen contains cysteine-rich secretory proteins (CRISPs) that belong to the dominant seminal plasma proteins. We aimed to isolate and characterize CRISP from turkey seminal plasma and evaluate its possible involvement in yellow semen syndrome (YSS). YSS, which is well characterized, causes reduced fertility and hatchability. The protein was purified using hydrophobic interaction, gel filtration, and reverse phase chromatography. It then was subjected to identification by mass spectrometry, analysis of physicochemical properties and specific antibody production. The biological function of the isolated protein was tested and included its effects on sperm motility and migration and sperm-egg interactions. Sperm motility was measured with the CASA system using Hobson Sperm Tracker. The reproductive tract of turkey toms was analyzed for gene expression; immunohistochemistry was used for protein localization in the male reproductive tract, spermatozoa, and inner perivitelline layer. The isolated protein was identified as cysteine-rich venom protein-like isoform X2 (CRVP X2; XP_010706464.1) and contained feature motifs of CRISP family proteins. Turkey CRVP X2 was present in both spermatozoa and seminal plasma. The extensive secretion of CRVP X2 by the epithelial cells of the epididymis and ductus deferens suggests its involvement in post-testicular sperm maturation. The internally localized CRVP X2 in the proximal part of the sperm tail might be responsible for stimulation of sperm motility. CRVP X2 on the sperm head might be involved in several events prior to fusion and may also participate in gamete fusion itself. Although the mechanisms by which CRPV X2 mediates fertilization are still unknown, the involvement of complementary sites cannot be excluded. The disturbance of CRVP X2 expression can serve as an etiologic factor of YSS in the turkey. This study expands the understanding of the detailed mechanism of fertilization in birds by clarifying the specific role of CRVP X2.

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

Structural and biochemical characteristics of the male accessory organs of reproduction in the hairy-nosed wombat (Lasiorhinus latifrons)

1978 ◽  
Vol 201 (1143) ◽  
pp. 191-207 ◽  
Keyword(s):  
Sialic Acid ◽  
Citric Acid ◽  
Reproductive Tract ◽  
Prostate Gland ◽  
High Concentration ◽  
Ductus Deferens ◽  
Chemical Examination ◽  
Male Reproductive Tract ◽  
Accessory Glands ◽  
Cauda Epididymidis

A description is given of the male reproductive tract in the South Australian marsupial, the hairy-nosed wombat, Lasiorhinus latifrons ; the study was based mainly on material obtained from animals shot in the field during the period October-December, but a few observations on captive wombats are also reported. The testes, located in a pre-penile scrotum, contained in the region of the ductuli efferentes a characteristic pigment, which occasionally extended as far as the caput epididymidis. The cauda epididymidis was enclosed within a separate pocket formed by the tunica vaginalis. The ductus deferens had no ampulla. The penis, bifid at the tip, was held in an S-bend position by the retractor penis muscles. The male accessory apparatus was of a highly complex type. In addition to the carrot-shaped prostate gland with three clearly discernible portions (anterior, central and posterior), three other pairs of glands were identified, which for the purpose of the present study have been designated as ‘Cowper’s glands’ ( A , B , and C ) without implying, however, that they are strictly analogous to the Cowper’s gland of eutherian mammals. Chemical examination of the male accessory glands led to the identification of a number of chemical substances, including fructose, sorbitol, glycogen, glucose, inositol, glycerol, citric acid, sialic acid, N -acetylglucosamine and N -acetylgalactosamine. The three most characteristic constituents of the anterior, central and posterior segments of the prostate gland were sorbitol, fructose and glycogen, respectively; the central and posterior segment of the prostate contained also some glucose and N -acetylhexosamine. Citric acid was shown to occur at high concentration in the Cowper’s gland A while the C gland was characteristically rich in sialic acid. A description is given of spermatozoa which had been recovered from the urine.

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