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PubMedDate not supplied

Low molecular weight FSH binding inhibitor in bovine testis.

Purification of low Mr (less than 5000) inhibitors of FSH binding to receptors has been hampered by their low concentration in tissue extracts and physiologic fluids. The calf testis represents an accessible and economic source of large quantities of tissue, and was therefore studied as a source of FSH binding inhibitors. Supernatants (27,000 X g) of calf testis homogenates inhibited binding of [125I]-hFSH as well as [125I]-hCG to membrane-bound receptor from the same source. FSH binding inhibitor was concentrated from large volumes of testis supernatant by precipitation of inert material with metaphosphoric acid, concentration/desalting of the resulting supernatant by ultrafiltration (Amicon UM-05 membranes) and lyophilization. Separation of FSH binding inhibitor and LH(hCG) binding inhibitor activities could be achieved by molecular sieving on Sephadex G-25. A partially purified fraction with inhibitors of FSH binding activity (ED50 = 44 micrograms protein) and free of LH(hCG) binding inhibitor activity (no activity at 800 micrograms protein) emerged with a Ve/Vo of 1.9, reflecting an apparent Mr of about 1500. Inhibitors of LH(hCG) binding activity emerged with the column outer volume. Rechromatography of the FSH binding inhibitor fraction on G-25 indicated two closely associated peaks of activity. These could be further resolved by gel filtration through BioGel P2, to give a salt-free fraction with an FSH binding inhibitor activity (ED50) of 24 micrograms protein. The inhibitor was heat-labile, losing 80% of its activity after 2 hours at 100 C. The testicular low molecular weight FSH binding inhibitor is similar to bovine follicular fluid and serum FSH binding inhibitor by several parameters.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMedDate not supplied

Morphologic and endocrine changes in the reproductive organs in rats implanted with gossypol acetate pellet in the testis.

Gossypol acetate pellets in concentrations ranging from 0.5, 1.0, 5.0, 10.0, to 20.0 mg were implanted in the testis of rats for a period up to 7 weeks. The implant was made in one testis only. In animals with a 10.0-mg implant, the germinal epithelium showed degenerative changes following the 7-week period, but spermatogonia and spermatocytes were unaffected. The effect of gossypol acetate appeared to be at the spermatid level. The electron microscopic study showed that the acrosomal membranes were disrupted. Blood testosterone and LH, but not FSH, decreased significantly (P less than 0.01). The fertility studies showed 100% infertility but no loss in libido in the 10-mg implant group. Up to the 7-week period, implants of less than 10 mg produced no significant effects on any of the parameters mentioned above. Animals with 20-mg implants had toxic symptoms. From the results in this study, it is concluded that 10.0 mg of gossypol acetate implanted in a single pellet in one testis causes antispermatogenic effects.

Animals↗
PubMedDate not supplied

Effects of prolactin on luteinizing hormone-stimulated testosterone secretion in isolated perfused rat testis.

The direct peripheral effect of prolactin on LH-stimulated testosterone secretion was re-evaluated using the intact, isolated, perfused rat testis. In paired experiments, one testis was infused with the hormones being studied; the other testis of the same rat was used as the control. A dose-response curve of LH-stimulated testosterone secretion was established first. A dose of 300 ng of LH, which was on the ascending portion of the dose-response curve, was selected so that both stimulatory and inhibitory effects of prolactin could be observed. Prolactin doses ranging from 0 ng to 3000 ng were then tested to determine alterations in LH-stimulated testosterone secretion. Prolactin inhibited LH-stimulated testosterone secretion at low doses (less than 300 ng), but augmented LH action at high doses (greater than 1000 ng). These results showed that prolactin and LH interact with each other in a biphasic dose-dependent manner.

Animals↗
PubMedDate not supplied

Identification of androgen binding-protein (ABP) from testis and epididymis of the seasonal rodent, Octodon degus (Molina, 1872).

ABP, a Sertoli cell secretory product, was identified in the seasonal rodent Octodon degus (Molina, 1872). It was shown to be present in cytosols from the testis and epididymis. It migrated with an Rf of 0.37 on nondenaturing polyacrylamide gels. Ligation of the vas efferens caused the disappearance of ABP from the epididymis and its accumulation in the testis, indicating its testicular origin. Binding to [3H]5 alpha-DHT was specific and completely reversible, with an apparent Kd of 3.5 +/- 0.4 X 10(-9) M. Half-times of association and dissociation were at 15 and 120 minutes, respectively. Binding equilibrium was achieved at 120 minutes. Steroid affinity relative to the best competitor, 5 alpha-DHT, was 0.27 for testosterone, 0.06 for 17 beta-estradiol, and 0.01 for cyproterone acetate. The presence and similar characteristics of ABP in a wide variety of mammals, including those with special reproductive strategies such as seasonal breeding, suggests that this protein may play a general role in the mechanisms regulating spermatogenesis, probably affecting the transport and concentration of androgens in the testis and epididymis.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMedDate not supplied

Developmental and stage-specific expression of Smad2 and Smad3 in rat testis.

Members of the transforming growth factor beta type (TGFbeta) superfamily and their receptors are expressed in the testis, and are believed to play important paracrine and autocrine roles during testicular development and spermatogenesis. The Smad proteins are downstream mediators for the family of TGFbeta growth factors. Smad2 and Smad3 are associated with both TGFbeta and activin signaling. However, very little is known about the expression and regulation of the Smad signaling proteins in the testis. In the present study, we have determined that Smad2 and Smad3 proteins are expressed in the postnatal testes of rats from 5 days to 60 days of age. Expression levels for both proteins are higher in young rats than in sexually mature rats. Smad2 and Smad3 messenger RNA levels parallel protein expression. Smad2 and Smad3 proteins are mainly localized in the cytoplasm of meiotic germ cells, Sertoli cells, and Leydig cells. Smad3 protein is localized to the nucleus of preleptotene to zygotene primary spermatocytes in young rats. Both proteins are expressed throughout all stages of the cycle of seminiferous tubules but are expressed at their lowest levels at stages VII-VIII in the seminiferous epithelium of adult rats. The presence of these downstream mediators in these cell types supports a role for TGFbeta and activin during spermatogenesis. The difference between the expression of Smad2 and Smad3 suggests that they may have different functions within the testis.

Age Factors↗
PubMedDate not supplied

Expression of a novel RAD23B mRNA splice variant in the human testis.

A gene coding a novel human RAD23B protein named RAD23-like protein B, presumably involved in spermatogenesis, was identified and characterized using a complementary DNA (cDNA) microarray. In the human testis, its expression was 2.33 times higher than it was in the embryo testis, with a particularly high expression in ejaculated human spermatozoa. The full length of this gene is 1548 bp, and the putative protein is 338 amino acids long. This protein is homologous to RAD23B, which is one of two human homologs of Saccharomyces cerevisiae RAD23, and is involved in both nucleotide excision repair (NER) and ubiquitin (Ub)-dependent proteolysis. However, RAD23-like protein B lacks the Ub-like (UbL) domain that functions as a proteasome localization signal. Multiple-tissue expression profile of the messenger RNA (mRNA) that encodes the RAD23-like protein B also showed that it is highly expressed in the human testis and in ejaculated spermatozoa. Our present study indicates that this novel alternative splicing form of RAD23B is correlated with human spermatogenesis.

Amino Acid Sequence↗
PubMedDate not supplied

Evidence for the presence of angiogenin in human testis.

We have reported the expression and possible roles of angiogenin, a potent angiogenic factor, in human female reproductive organs. In this study, we investigated the expression of angiogenin in the human testis, a male reproductive organ. Western blot analysis showed the presence of angiogenin in the human testis, with a single band of the same size as recombinant human angiogenin. Immunohistochemical study and in situ hybridization showed that the angiogenin protein and messenger RNA (mRNA) localized in peritubular myoid cells (PTMCs) and vascular endothelial and smooth muscle cells. PTMCs are known to play various roles in the testes concerned with spermatogenesis, transport of spermatozoa, structural support to the seminiferous tubules, and mediation of Sertoli cell function. The specific localization of angiogenin in PTMCs suggests that angiogenin plays physiologic roles in the human testis.

Aged↗
PubMed2005

Transcriptional activation of the testis-specific histone H1t gene by RFX2 may require both proximal promoter X-box elements.

The rat testis-specific linker histone H1t gene is transcribed in pachytene primary spermatocytes during spermatogenesis. Our previous work using transgenic mice demonstrated that spermatocyte-specific transcription of the H1t gene is dependent upon a proximal promoter element designated the TE element. TE is composed of two adjacent and inverted imperfect repeat sequences designated TE1 and TE2 and both of these palindromic elements are similar in sequence to the X-box, a DNA consensus sequence that binds regulatory factor X (RFX). RFX2 is the major enriched protein derived from rat testis nuclear extracts when using the TE1 element as an affinity chromatography probe. Co-expression of RFX2 together with an H1t promoted reporter vector in transient expression assays activates the H1t promoter in the GC-2spd germinal cell line, and mutation of either X-box significantly represses activity. However, RFX2 partially reactivates the promoter when either of the X-box elements is independently mutated. In order to totally block reactivation by RFX2, it is necessary to mutate both X-boxes simultaneously. Therefore, RFX2 appears to be able to bind to either X-box independently to partially activate the promoter of the testis-specific histone H1t gene, but simultaneous binding of RFX2 to both X-box elements may be required for maximal promoter activation.

Animals↗
PubMed2006

Anti-apoptotic factor humanin is expressed in the testis and prevents cell-death in leydig cells during the first wave of spermatogenesis.

Humanin (HN) is a 24 amino acids peptide with potent neuro-survival properties that protects against damage associated with Alzheimer's disease. In the present report, we have demonstrated by immunohistochemical analysis and Western blotting the pattern of expression of rat humanin (HNr) in the testis of 10- to 60-day-old rats. The Leydig cells of 10- and 40- day-old rats expressed this peptide at high levels; and in the testis of 60-day-old rats the expression of HNr expanded to include Leydig, endothelial, peritubular and germ cells. As monitored by Western blotting, HNr was released into the medium of cultures of Leydig cells isolated from 10-, 40-, and 60-days-old rats. HNr stimulated the incorporation of [(3)H]TdR into DNA of Leydig cells from 10-days-old rats, in a manner that indicated promotion of cell survival rather than an increase in the rate of cell multiplication. This peptide also enhanced steroidogenesis by cultured Leydig cells from 10- to 40-day-old rats both alone and synergistically with IGF-I. The expression of HNr in cultured Leydig cells increased in response to GH and IGF-I. In summary, we demonstrated here that HNr was expressed at all stages of maturation in the rat testis. This peptide promoted the survival of Leydig cells in culture and interacted with IGF-I to stimulate DNA synthesis and steroidogenesis. We propose that HNr is a novel testicular anti-apoptotic factor.

Animals↗
PubMed1991

Ultrastructure of the seminiferous epithelium and intertubular tissue of the human testis.

The ultrastructural features of the human testis are reviewed with emphasis upon the process of spermatogenesis and the cytology of the Leydig cells. The seminiferous epithelium is structurally partitioned by the Sertoli cells into basal and adluminal compartments via the specialized tight junctions between the Sertoli cells. Spermatogonia reside in the basal compartment, and, via a series of cell divisions, produce the primary spermatocytes, which at the commencement of their development move into the adluminal compartment, and thus the lengthy process of meiotic maturation is initiated. The fine structure of primary spermatocytes is described together with the complex transformation of the spermatids into spermatozoa during the process of spermiogenesis. Earlier studies of the organization of the human seminiferous epithelium showed that germ cells at different developmental stages formed identifiable collections termed cell associations or stages, but since several stages were seen in a single tubule cross-section, this gave the impression of an extremely irregular pattern of spermatogenic development. When the topographic arrangement of germ cells was re-examined with the aid of computer modelling, a highly ordered distribution was revealed, conforming to a helical pattern based on the geometry of spirals. Thus spermatogenesis in the human testis is subjected to a precise regulation in keeping with the ordered arrangement of the germ cells seen in other mammalian species. The intertubular tissue of the human testis is composed of loose connective tissue containing blood vessels, occasional lymph capillaries, macrophages, mast cells, and the Leydig cells which occur either as single cells or form small clusters. The Leydig cell cytoplasm contains an abundant supply of smooth endoplasmic reticulum and mitochondria with tubular cristae, both features being characteristic of steroidogenic cells. Human Leydig cells contain large Reinke crystalloids of variable size and number, but their function remains obscure. The frequent occurrence of paracrystalline inclusions within the cytoplasm of the human Leydig cell suggests that these elements are precursors of the Reinke crystalloids.

Epithelium↗
PubMed1995

Immunocytochemical localization of the Ya, Yc, Yb1, and Yb2 subunits of glutathione S-transferases in the testis and epididymis of adult rats.

Glutathione S-transferases (GSTs) are dimeric proteins that come from a multigene family. They can be grouped into five classes (alpha, mu, pi, sigma, theta) based on the degree of amino acid homology of their subunits. These GST isozymes are able to catalyze the conjugation of glutathione with a wide variety of electrophiles, thereby protecting important cellular constituents from electrophilic attack. In the present study, the distribution of the Ya and Yc subunits from the alpha family, as well as the Yb1 and Yb2 subunits from the mu gene family was examined using immunocytochemistry in the adult rat testis and epididymis. The results of these four GST subunits were also compared with two other subunits, the Yf and Yo proteins, which have already been investigated in our laboratory [Veri et al. (1993), J. Androl., 14:23-44; Veri et al. (in press), J. Androl.]. In the testis, Leydig cells were intensely stained for all six subunits. Within the seminiferous epithelium, Sertoli cells were reactive only for antibodies raised against the Ya, Yb1 and Yf subunits. Among germ cells, all spermatogonia, spermatocytes and step 1-15 spermatids were virtually unreactive for each of the six GSTs. However, moderate to intense staining was seen over steps 16-19 spermatids with the anti-Yo and anti-Ya antibodies, and intense staining over step 19 spermatids with the anti-Yb1 and anti-Yb2 antibodies. In the rete testis, Yf, Yo, Yb1, and Yb2 subunits were intensely reactive over the epithelial cells with weak staining for Yc and no staining for Ya antibodies. Interestingly, in the efferent ducts the Yc, Yb1, and Yf proteins were intensely reactive over ciliated cells, whereas only the Yc protein was intensely reactive over nonciliated cells. In the epididymis, immunoreactivity varied among the principal and basal cells of a given epididymal region for each GST antibody. In the case of principal cells, several of the GSTs showed a similar immunostaining pattern along the tubule. Although not identical in intensity of reaction, the Yc, Yb1, Ya and Yo proteins showed an increase in staining intensity from the proximal to distal segments of the epididymis. In contrast, the Yb2 protein was intensely expressed only in the distal caput with weak levels throughout the rest of the epididymis. The Yf reactivity was strongest from the distal initial segment to the distal caput and unreactive in the corpus and proximal cauda epididymidis.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1978

Testosterone and 5alpha-dihydrotestosterone inhibit both growth and spermatogenesis in the remaining testis in partially castrated adult newts, Notophthalmus viridescens.

The testis of the newt, Notophthalmus viridescens, undergoes hypertrophy following partial castration. Injections of either testosterone or 5alpha-dihydrotestosterone are equally effective in inhibiting the increase in testis weight which follows partial castration. In addition, both of these androgens inhibit spermatogenesis, i.e., spermatogonia appear to be inhibited resulting in early cessation of spermatogenesis and a precocious division of the testis into separate spermatogonia and sperm compartments.

Animals↗
PubMed1987

Immunohistochemical study of calmodulin in developing mouse testis.

The purpose of this study was to determine the localization of calmodulin in the developing mouse testis by the indirect immunoperoxidase method. In addition, the amount of calmodulin in pachytene spermatocytes, spermatids, and residual bodies isolated from the mouse testis and epididymal spermatozoa was quantitated by the adenylate cyclase activation assay and by enzyme immunoassay. The relative levels of calmodulin in the developing mouse testis and in the isolated testicular germ cells were confirmed by western transfer staining. The level of immunoreactive calmodulin was very low in the testes from immature animals. In testes from the mature mouse, calmodulin was found to be localized in spermatocytes and spermatids, but was not found in spermatogonia, Sertoli cells, and interstitial cells. By contrast, immunochemical staining of tubulin was extremely intense in Sertoli cells. Biochemical determinations also showed that pachytene spermatocytes, round spermatids, spermatozoa, and residual bodies contained 14.9 micrograms, 15.8 micrograms, 2.3 micrograms and 5.2 micrograms of calmodulin per mg of protein, respectively. Both the immunochemical and the biochemical studies revealed that levels of calmodulin were high in the spermatocytes and in the round spermatids, as compared to the level in spermatozoa. This fact strongly suggests that the large amount of calmodulin in mammalian testes may be associated primarily with meiotic divisions and/or spermatogenesis.

Aging↗
PubMed1988

Gonadotropin action on androgen synthesis in short-term incubation of explants and dispersed cells of the testis of Xenopus laevis.

Testis cells of the toad Xenopus laevis were dissociated with collagenase and the cell suspension was enriched for steroidogenic cells by Percoll gradients. Results suggested that cells should be preincubated during a 6-h period before stimulation with gonadotropin. Our results indicate that a 2-h incubation period with gonadotropin was necessary to obtain a significant response. Furthermore, the cells can be maintained in a functional state longer than mammalian testis cells. Different gonadotropins were used to stimulate androgen production, and their effects were compared in both dissociated cells and testicular explants. Cells were more sensitive to luteinizing hormone (LH) and follicle stimulating hormone (FSH) than the explants (ED50LH = 0.041 +/- 0.003 micrograms for cells and 0.097 +/- 0.002 micrograms for explants: ED50FSH = 0.41 +/- 0.03 micrograms for cells and 0.63 +/- 0.03 micrograms for explants). Moreover, human chorionic gonadotropin (hCG) which only stimulates testicular explants at high doses, failed to stimulate the androgen production of dissociated cells; this indicates a low sensitivity of amphibian testis to hCG and a possible damaging effect of collagenase on the receptors of isolated cells.

Androgens↗
PubMed1978

Structure and ultrastructure of the testis and sperm formation in goodeid teleosts.

Testis structure in four species of goodeid teleosts is described. Testicular tubules terminate blindly at the testis periphery where spermatogonia are located. In goodeid teleosts, development of sperm takes place synchronously within cysts whose periphery is made up of a single layer of Sertoli cells. Upon completion of spermiogenesis, spermiation ensues wherein sperm are shed, as spermatozeugmata, into the testis efferent duct system. Subsequently, Sertoli cells, which comprised the cyst periphery, transform into efferent duct cells. Sertoli cells phagocytize residual bodies and are involved in the formation of spermatozeugmata. The structure of the goodeid spermatozeugmatum is quite different from that observed in the related poeciliids. It is concluded, in view of this and other considerations, that the goodeids and poeciliids have independently evolved solutions to the problems of internal fertilization and gestation.

Animals↗
PubMed2002

Testis differentiation in the glowworm, Lampyris noctiluca, with special reference to the apical tissue.

The gonads of Lampyris noctiluca are sexually undifferentiated during the first larval instars. They consist of many gonadal follicles that include the germ stem cells enclosed by the somatic cells of the follicle wall. Follicle wall cells are more numerous at the follicle apices than at the distal parts, but different cell types cannot be distinguished. In male larvae, the appearance of apical follicle tissue, derived from follicle wall cells, marks the onset of testis differentiation. When maximally expressed, the apical tissue occupies about the upper half of the testis follicles and can be observed in larvae of the fifth and sixth instar. The apical tissue is characterized by its "light" appearance (due to poor stainability) caused by the small number cellular organelles, especially a paucity of free ribosomes. Maximal expression of the apical tissue must be very brief, since in most examined fifth and sixth instar larvae the apical tissue is partly or mostly translocated into the center of the upper half of the follicles and spermatogonia then occupy the apical follicle tips. During and after translocation apical cells form projections that grow around clusters of spermatogonia (spermatocysts). Thus, the apical cells transform into spermatocyst envelope cells. They retain their "light" appearance but undergo dramatic subcellular differentiation: smooth ER becomes extremely prominent, forming stacks and whorls of parallel cisternae. Golgi complexes are also conspicuous. The cellular organization suggests secretory activity. The possibility of ecdysteroid production and its function is discussed. The spermatocyst envelope cells persist into the pupal stage. When spermiohistogenesis takes place in cysts, cyst envelope cells show signs of regression. At all stages of testis development apical cells and their derivatives, the spermatocyst envelope cells, phagocytize degenerating spermatogonia. Although this is an important task of these cells, the impressive formation of sER in the cyst envelope cells is indicative of an additional, as yet unknown, function.

Animals↗
PubMed1992

Variability of venous anatomy of rat testis: application to experimental testicular surgery.

The venous drainage of the testis of the laboratory rat was observed in 31 animals. The right testicular (internal spermatic) vein drained directly into the right common iliac vein in 77.4%, and into the inferior vena cava in 22.6% of the animals. The left testicular vein drained into the left common iliac vein in all animals, but in 90.3% there was also an accessory branch of the testicular vein draining into the left renal vein. These observations suggest that in the rat the exact anatomy of the venous drainage of each testis should be identified prior to undertaking any surgical procedure on the testis where the venous vasculature plays a major role such as testicular transplantation or the creation of an experimental varicocele.

Animals↗
PubMed2001

Stage-dependent and alternative splicing of sGnRH messengers in rainbow trout testis during spermatogenesis.

The gonadotropin releasing hormone (GnRH) has long been considered as a neuropeptide involved in the control of the reproductive cycle. However, the presence of GnRH and its receptors in various tissues, including ovary and testis, suggests a role as autocrine/paracrine factor. In the present study, we report the expression of the sGnRH-1 and sGnRH-2 genes encoding salmon GnRH in rainbow trout testis throughout testicular development and spermatogenesis. We demonstrate that both sGnRH mRNA are expressed prior of sexual differentiation. In adult, northern blot analysis indicates that sGnRH-2 transcripts are expressed in the testis at higher levels than sGnRH-1 messengers. Moreover, we observed that the expression of sGnRH-2, and not sGnRH-1, messengers was stage-dependent. sGnRH-2 mRNA expression decreases at the onset and progressively rebounds at the end of spermatogenesis. In addition, we demonstrate that a complex stage-dependent and differential splicing of the sGnRH-2 messengers occurs throughout spermatogenesis. We isolated five transcripts corresponding to sGnRH-2 messengers. Two of them may encode a novel and shortened GnRH-associated peptide containing 18 residues instead of 46. Our data provide new insight in the putative role of GnRH and GAP peptides as autocrine/paracrine factors of spermatogenesis.

Alternative Splicing↗