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PubMed1989

Mature rat testis contains a high molecular weight species of phosphatidylinositol transfer protein.

Immunoblot analysis of a rat testis cytosol fraction revealed two proteins which reacted with a polyclonal rabbit antibody to bovine phosphatidylinositol transfer protein. These two proteins were separated by anion exchange and molecular sieve column chromatographic procedures and shown to catalyze the transfer of phosphatidylinositol and phosphatidylcholine between populations of small unilamellar vesicles. One protein was identified as the phosphatidylinositol transfer protein detectable in 16 other rat tissues and many eukaryotic species; the other phosphatidylinositol transfer protein was unique to testis. The molecular masses of the proteins, determined under denaturing electrophoretic conditions, were 35 and 41 kDa, respectively. When testis was examined in animals from birth to six weeks of age, the 35-kDa protein was present throughout, while the 41-kDa protein first appeared during week 4 and increased to adult levels by week 6; a small yet significant increase in tissue phosphatidylinositol transfer activity accompanied this expression of the testis-specific protein. Selective destruction of Leydig cells by ethylene dimethanesulfonate did not cause any detectable loss of the 41-kDa phosphatidylinositol transfer protein. The structural and catalytic relationships between the two testicular phosphatidylinositol transfer protein species remain to be elucidated.

Age Factors↗
PubMed1977

Production and effects of 7 alpha-hydroxytestosterone on testosterone and dihydrotestosterone metabolism in rat testis.

1. Testicular 7 alpha-hydroxylation of testerone was assayed in cell extracts of rats between 12 and 79 days of age. Maximal 7 alpha-hydroxylase activity was observed about 60 days, while insignificant activity was obtained prior to 42 days of age. 2. 7 alpha-Hydroxytestosterone, a major metabolite of testosterone in mature rat testis, inhibited 5 alpha-reduction of testosterone in cell extracts of mature but not of immature rat testis. 3. Maximal testicular activity of 3 beta-hydroxysteroid dehydrogenase using dihydrotestosterone as substrate was obtained in the presence of NAD, while maximal 3 alpha-hydroxysteroid dehydrogenase activity was observed with NADP. Both enzyme activites were reversible. 4. Sensitivity toward testosterone inhibition of 3-hydroxysteroid dehydrogenase varied greatly with stage of testis development being highest at 25-27 days of age. In contrast to testosterone, 7 alpha-hydroxytestosterone was an inhibitor of 3 alpha-hydroxysteroid dehydrogenase only. In the mature rat testis 7 alpha-hydroxytestosterone may be a naturally occurring inhibitor of dihydrotestosterone and 5 alpha-androstane-3 alpha, 17 beta-diol formation.

Aging↗
PubMed1987

Localization of alpha-inhibin-31 in rodent testis and brain by immunocytochemical procedure and Western blot analysis.

Using an anti-serum against synthetic alpha-inhibin-31, we have studied its cellular locations in rodent testis and brain. Western blot analysis detected several molecular forms of the protein(s). A protein of 17 KDa in size was detected in testis of one month old mice. Two major bands of molecular weights 39 kDA and 21 kDA were detected in mature mouse testis. The 39 kDA protein was also present in male brain, female brain and ovary. No protein similar in size to alpha-inhibin-31 was detected with this antiserum, suggesting that the antibody recognized only the precursor of the alpha-IB-31 molecule. Immunocytochemical studies revealed that these molecules were located in the cytoplasm of the interstitial Leydig cells. The immunocytochemical reaction can be eliminated by pre-incubation with synthetic alpha-inhibin-31. Immunoreactive substances were also demonstrated at the blood-brain barrier on the external surface of the ependymal cells in the third ventricle of the rat brain. In the pituitary, similar pattern of localization was also observed in the cuboidal-columnar epithelial cells that lined the par tuberalis between the anterior and intermediate lobes. The immunoreaction to the neural cells cannot be completely abolished by competition with the synthetic peptide. These observations suggested that alpha-inhibins are located in the Leydig cells of the testis as well as in the brain, pituitary and ovary.

Animals↗
PubMed1992

The evidence for post-meiotic expression of a testis-specific isoform of a regulatory subunit of calcineurin using a monoclonal antibody.

The expression of a regulatory subunit of calcineurin (CaN beta) during rat spermatogenesis was examined in rat testes using a monoclonal antibody Va1. Results showed that a testis-specific isoform of CaN beta was expressed only 3 weeks after birth, when meiosis begins, and increased in amount depending on the maturation of spermatogenesis. The matured sperm, which consists of only post-meiotic cells, is most likely to have only the testis-specific isoform of CaN beta. The brain type isoform of CaN beta was not detected in rat sperm. Immunoblot analysis of testes from different rodent species by a monoclonal antibody Va1 showed that all rodent species examined had their own homologues corresponding to a testis-specific isoform of CaN beta in rats, although they showed distinctively different molecular weights on SDS-PAGE compared to the testis-specific isoform in rats. Each homologue was shown to be specifically expressed in post-meiotic phase of spermatogenesis, as was seen in rats.

Aging↗
PubMed1992

The unique N-terminal sequence of testis angiotensin-converting enzyme is heavily O-glycosylated and unessential for activity or stability.

The testis-specific isozyme of angiotensin-converting enzyme (ACE) is identical, from residue 68 to the C terminus, to the second half or C-terminal domain of somatic ACE. However, the first 67 residues, comprising the signal peptide and a Ser-/Thr-rich 36-residue sequence that constitutes the N terminus of mature testis ACE, are unique. We have expressed a mutant human testis ACE lacking this 36-residue N-terminal sequence and find that compared to the wild-type protein the mutant is 15 kDa smaller due to the loss of greater than 90% of all O-linked sugars, but that it retains full enzymatic activity and is stable in culture. Heavy O-glycosylation is a property of testis ACE that is not shared by the somatic enzyme and is attributable to this unique sequence.

Amino Acid Sequence↗
PubMed1987

Molecular cloning and differential expression of somatic and testis-specific H2B histone genes during rat spermatogenesis.

We have cloned cDNA of a testis-specific histone, TH2B (a variant of H2B), and rat somatic H2B gene to investigate regulation of testis-specific histone genes during rat spermatogenesis. The amino acid sequences deduced from DNA sequences show extensive sequence divergence in the N-terminal third of the two histones. The rest is highly conserved. One cysteine residue was found in TH2B. No cysteine is present in somatic histones except in H3 histone. We investigated the expression of TH2B and H2B genes using the regions of sequence divergence as hybridization probes. The TH2B gene is expressed only in the testis, and the expression of this gene is detected 14 days after birth, reaching a maximum at Day 20. The level of H2B mRNA shows a reciprocal pattern. This contrasting pattern can be explained by the gradually changing proportion of spermatogonia and spermatocytes with testicular maturation. In situ cytohybridization studies show that H2B gene is expressed primarily in proliferating spermatogonia and preleptotene spermatocytes, whereas TH2B gene is expressed exclusively in pachytene spermatocytes which first appear in testis about 14 days after birth. H2B and TH2B genes appear to be ideal markers for the study of proliferation and differentiation events in spermatogenesis and their regulatory mechanisms.

Amino Acid Sequence↗
PubMed1996

The TRH-like peptides in rabbit testis are different from the TRH-like peptide in the prostate.

Human seminal fluid contains a number of tripeptide amides with similar structures to thyrotropin releasing hormone (TRH), two of which have been identified as pGlu-Glu-Pro amide and pGlu-Phe-Pro amide. To determine whether these peptides originate in the same tissues and have the same molecular origin, TRH-immunoreactive peptides were extracted from the prostate and testis of the rabbit, purified by ion exchange chromatography and HPLC, and identified by co-chromatography with 3H-labelled marker peptides. In addition, trypsin digestion was used to release TRH-like tripeptides from N-extended forms of these peptides. The sole TRH-like peptide in the prostate was shown to be pGlu-Glu-Pro amide; it was not accompanied by a detectable amount of pGlu-Phe-Pro amide. The prostate also appeared to contain a very small amount of N-extended forms of these peptides. In contrast to the prostate, the testis contained high concentrations of N-extended forms of pGlu-Phe-Pro amide but essentially no tripeptide. The testis also contained N-extended forms of two other neutral TRH-like peptides which were less hydrophobic than pGlu-Phe-Pro amide. Neither the prostate nor the testis contained a significant amount of TRH. The results show that in the rabbit the TRH-like peptides pGlu-Glu-Pro amide and pGlu-Phe-Pro amide occur in different tissues and appear to be formed from different precursors.

Amino Acid Sequence↗
PubMed1983

The differentiation of Leydig cells, steroidogenesis, and the spermatogenetic wave in the testis of Necturus maculosus.

The study of seminiferous tubule--Leydig cell interactions in relation to specific germ cell stages during the cycle of the seminiferous epithelium is extremely difficult in most mammalian species due to the continual presence of different spermatogenetic stages in the testis from the onset of puberty. The problem is also compounded by the uniform distribution of both seminiferous tubules and interstitial tissue throughout the entire testis. This difficulty can be circumvented, however, by studying certain species where there is a topographical distribution of germ cell stages within the testis. The urodele amphibian Necturus maculosus exhibits a breeding cycle during which a longitudinal wave of spermatogenesis occurs along the length of the testis, resulting in a spatial and temporal segregation of differentiating germ cells. Moreover, this topographical pattern of spermatogenesis is also reflected in the degree of development of adjacent Leydig cells. This anatomical arrangement allows distinct testicular regions to be obtained using a dissecting microscope. The isolated zones, containing germ cells and Leydig cells in various stages of development, were analyzed for 17 alpha-hydroxylase, C-17,20-lyase, and aromatase activities (key enzymes for the synthesis of androgens and estrogen), estrogen binding, and cytochrome P-450 content. Functional parameters were then correlated with the morphology of Leydig cells in the various zones observed by both light and electron microscopy. It was found that there existed a distinct correlation between the state of differentiation of the leydig cells, their steroidogenic potential, and the distribution of estrogen receptors. These results in Necturus indicate indicate in this species, at least, the steroidal microenvironment of different germ cell associations may be quite specific.

Androgens↗
PubMed1984

Onset of the response to chorionic gonadotropin in the chick embryo testis.

The stage of development of the chick embryo testis when it begins to respond to gonadotropin stimulation was investigated. The testosterone secretion in vitro, measured by radioimmunoassay, was employed to evaluate the response to hCG in testis from 8 to 16 days of incubation. At 8 to 10 days of the chick embryo development, the testis secreted testosterone, but no increment in the steroid production has been observed after hCG treatment. On the contrary, at 12, 14, and 16 days a clear increase in testosterone secretion has been demonstrated when hCG was added to the culture medium. The absence of hCG response before 12 days of incubation agrees with the hypothesis of an early independence period between testis and adenohypophysis during embryonic development.

Animals↗
PubMed1985

Seasonal variations of androgens, estrogens, and progesterone in the different lobules of the testis and in the plasma of Salamandra salamandra.

Progesterone, 4-androstenedione, testosterone, dihydrotestosterone, 5 alpha-androstane-3 alpha,17 beta-diol (3 alpha-diol), 5 alpha-androstane-3 beta, 17 beta-diol (3 beta-diol), estrone, and estradiol levels were determined by radioimmunoassay in the different lobules of the testis of Salamandra salamandra throughout the year according to the seasonal cycle. 3 beta-diol levels were not detectable. High levels of steroids were found in the grandular tissue (enlarged pericystic cells after spermiation) and large variations were showed for progesterone, 4-androstenedione, testosterone, 3 alpha-diol, and estrone. In the mature lobule (formed by cysts with mature spermatozoa), only testosterone showed seasonal variations and in the immature lobule (with early stages of meiosis), 3 alpha-diol showed fluctuations. The major estrogen found in the testis of Salamandra was estrone; estradiol stayed at a low level throughout the cycle. The steroids fluctuation seems to be related to the histological evolution of the testis throughout the cycle. The present data were the first on steroid seasonal variations in the testis of an urodele.

Androgens↗
PubMed1990

Progesterone metabolism in the microsomal fraction of the testis, head kidney, and trunk kidney from the rainbow trout.

In the present study on male rainbow trout, well-defined microsomal fractions from gonad, trunk kidney, and head kidney were used to study enzymes active on progesterone. The metabolites produced were identified by mass spectrometric analysis. In the testis the main metabolite was 17 alpha-hydroxyprogesterone which is an intermediate in the steroid biosynthetic pathway. 17 alpha-Hydroxyprogesterone was also identified in incubations from head and trunk kidney. The 17 alpha-hydroxylase activity was higher in the head kidney than in the trunk kidney which probably reflects the presence of steroid producing interrenal cells in this part of the kidney. The conversion of progesterone to 17 alpha-hydroxylated products in the testis and head kidney was NADPH dependent and inhibited by carbon monoxide, indicating the participation of cytochrome P450 monooxygenase in this reaction. NADH supported the reaction to some extent (27% of the NADPH-dependent activity) in the testis but not in the head kidney. In addition to 17 alpha-hydroxyprogesterone the head and trunk kidney microsomes gave rise to 16 alpha- and 6 beta-hydroxyprogesterone. These activities were low or absent in testis microsomes. Progesterone 5 alpha-reductase activity was only detected in trunk kidney microsomes.

17-alpha-Hydroxyprogesterone↗
PubMed1991

Evaluation of the scrotal testis before and after orchidopexy in experimental unilateral cryptorchidism.

Unilateral cryptorchidism was induced in newborn Wistar rats. With standard histological techniques, no abnormality was found in the scrotal testis at any age. Using DNA flow cytometry to measure the proportion of cells in the haploid phase in the testis, secondary degenerative changes were noted at 40 days of age. Orchidopexy carried out at 30 days of age prevented these changes appearing; at 50 days reversed the abnormality already present; and at 90 days failed to reverse the degeneration of the scrotal testis. These data would suggest that although early orchidopexy can prevent secondary changes in the scrotal testis, operation up to puberty will allow these changes to be reversed.

Age Factors↗
PubMed1982

Lipoproteins stimulate androgen production by cultured rat testis cells.

The effects of human high density lipoprotein (hHDL), human low density lipoprotein (hLDL), and rat high density lipoprotein (rHDL) on androgen production by cultured rat testis cells were investigated. Enzymatically dissociated testis cells from hypophysectomized adult rats were cultured in a serum-free medium. During the first 2 days of culture, the addition of human or rat lipoprotein alone stimulated testis cell testosterone (T) production by 100 to 250% in a dose-dependent manner. Likewise, treatment with hCG caused a 2.5-fold increase in T production. Furthermore, the effect of lipoproteins plus hCG was synergistic; the stimulation of T production by concomitant treatment with hCG and lipoproteins was greater than the sum of each added individually. Rat HDL augmented hCG stimulated T production in a concentration-dependent manner and maximum synthesis was achieved at 100 micrograms protein/ml (240% increase) with an ED50 value of 25 micrograms/ml rHDL. At low concentrations (10-30 micrograms protein/ml), all lipoproteins tested had similar stimulatory effects on T production but at the highest dose tested (300 micrograms protein/ml), hHDL was more effective than rHDL. The stimulatory effect of lipoprotein was shown to be time-dependent. Maximum stimulation of T production by lipoprotein was seen during the initial 48 h of culture, whereas lipoproteins were ineffective during the first 5 h and during days 8 to 10 of culture. The present data are consistent with the concept that lipoproteins provide cholesterol substrate while gonadotropins stimulate tha rate limiting enzyme(s) which convert cholesterol to T. This primary culture model of testis cells in serum-free medium is responsive to serum lipoproteins and offers a unique opportunity to study the direct effect of lipoproteins and gonadotropins on testicular steroidogenesis.

Animals↗
PubMed1982

17 beta-Oxidation of estradiol and testosterone in the human testis.

The oxidation of 17 beta-estradiol in the human testis was studied in order to characterize a potentially important regulatory step in the action of estradiol in the human testis. 17 beta-Estradiol was shown to be converted to estrone, a weaker estrogen, in a reaction which was not inhibited by testosterone to any greater extent. When compared with the corresponding 17 beta-oxidation of testosterone, differences in coenzyme preferences, hydrogen ion sensitivity and inhibitions by estradiol and testosterone were observed, suggesting to a presence of different 17 beta-hydroxysteroid dehydrogenases in the human testis. Thus the human testis may counteract some of the deleterious effects of 17 beta-estradiol on androgen biosynthesis by metabolizing it to a weaker estrogen, in a reaction which probably is not inhibited by high testicular testosterone concentrations.

17-Hydroxysteroid Dehydrogenases↗
PubMed1983

Biochemical characterization of glucocorticoid receptors of rat testis.

Rat testis cytosolic glucocorticoid receptors were characterized by DEAE-cellulose chromatography, Sephadex G-100 columns and sucrose-density gradients. The unactivated [3H]dexamethasone-receptor complex showed two distinct peaks of macromolecular bound radioactivity on DEAE-cellulose chromatography. Peak I eluted just after the column wash, while peak II eluted at 0.28 M KCl. Activation of the complex at 25 degrees C for 45 min resulted in a significant increase in peak I with a concomitant decrease in peak II and the appearance of a third peak at 0.18 M KCl. Both the unactivated and activated [3H]dexamethasone-receptor complex, when analyzed on Sephadex G-100 columns, showed a single macromolecular bound radioactive peak having a Stokes radius of 6.5 nm. Treatment of the [3H]dexamethasone-receptor complex (6.5 nm holo-receptor) with trypsin (0.5 microgram/ml) resulted in the appearance of a smaller (2.0 nm) fragment but no intermediate sized forms of the receptor were observed. The complexes sedimented as 7-8 S (in low salt) and as 4.6 S (in high salt) forms in sucrose gradients in the presence or absence of 10 mM molybdate. Steroid unbound receptors were inactivated at 25 degrees C and 4 degrees C with a T 1/2 of 2 h and 24 h, respectively. Ten mM molybdate slightly protected the unbound testis receptor at 25 degrees C. However, molybdate, dithiothreitol, and molybdate plus dithiothreitol were unable to either enhance or reactivate [3H]dexamethasone binding of unbound receptors at 4 degrees C or 25 degrees C. Activation of testis [3H]dexamethasone-receptor complexes resulted in a 2-3 fold enhancement in subsequent binding to testis nuclei in vitro. In addition, we observed that activated [3H]dexamethasone-receptor complexes were precipitated with 30-35% ammonium sulfate, while unactivated complexes were precipitated with 30-40% ammonium sulfate.

Animals↗
PubMed1984

5 Alpha- and 5 beta-reductases for 4-ene-3-ketosteroids and 17 beta-ol-dehydrogenase in epididymis and testis of golden hamster during sexual development.

Homogenates of the epididymis, testis and seminal vesicle from 15, 25, 35 and 60-day old golden hamsters were incubated with [3H]4-androstene-3,17-dione and NADPH and enzyme activity was estimated. In the testis, activities of 5 alpha- and 5 beta-reductases were the highest (32 +/- 4 and 68 +/- 13 (SD) nmol/100 mg protein/h, respectively) at 25 days of age, moderately high at 35 days and very low (1-3 and 5-6, nmol/100 mg protein/h, respectively) at 15 and 60 days. In the epididymis, 5 alpha-reductase activities increased with age during sexual development by up to 50-fold and reached the maximum value (40 +/- 11 nmol/100 mg protein/h) at 60 days. The 5 alpha-reductase activities in the seminal vesicle were found to be relatively low (0.5-1 nmol/100 mg protein/h), compared with those in the epididymis and testis. Activities of 5 beta-reductase in the epididymis and seminal vesicle were very low (0.1-0.5 nmol/100 mg protein/h) at all ages. These results indicate the existence of a marked, but transient, increase in 5 alpha- and 5 beta-reductase activities during immature period in the testis of golden hamster. In the epididymis, however, 5 alpha-reductase activity increases with age during sexual maturation, while 5 beta-reductase activity is almost undetectable at all ages.

17-Hydroxysteroid Dehydrogenases↗
PubMed1989

Synthesis and aromatization of 19-norandrogens in the stallion testis.

The results of the measurement of 19-nortestosterone in the testiscular artery and vein of the stallion, the very low levels of this steroid in the peripheral blood of geldings and the similar patterns of increase in the peripheral levels of 19-nortestosterone and testosterone after hCG stimulation, show that 19-nortestosterone, like testosterone, is essentially synthesized in the testis. This testicular origin was confirmed by the ability of testicular tissue to synthesize 19-norandrogens from [4-14C]androgens in vitro. 19-Nortestosterone was 50% conjugated in the peripheral blood and almost entirely conjugated after biosynthesis in vitro. The sequence of appearance of steroids in the peripheral blood after a single injection of 10,000 IU hCG suggests that, in the equine testis, 19-norandrogens are produced by a specific C10-19 desmolase (estrene synthetase), stimulable by hCG. 19-Nortestosterone was aromatized into estradiol-17 beta by stallion testicular microsomes. The affinity of the aromatase for 19-nortestosterone was very low compared to that for testosterone. At low and presumably physiological levels, and at a high testosterone/19-nortestosterone ratio, testosterone did not inhibit 19-nortestosterone aromatization by more than 53%. Thus, 19-nortestosterone may be aromatized in vivo in the testis in spite of the endogenous concentrations of androgens. However, the low velocity of 19-nortestosterone aromatization by testicular microsomes at roughly physiological concentrations suggests that 19-norandrogen aromatization may only participate slightly in the testicular estrogen production. These results suggest that in the equine testis, two aromatizing enzyme systems may exist: one which aromatizes both androgens and 19-norandrogens, and a minority system more specific for 19-norandrogens.

Animals↗
PubMed1990

Differential regulation of DNA methylation in rat testis and its regulation by gonadotropic hormones.

Eukaryotic DNA methylation occurs exclusively at the 5'-position of cytosine and has been implicated in the regulation of gene expression. Using high-performance liquid chromatography, the methylation of testis DNA during its development, in different cell populations and during regulation by gonadotropic hormones, were studied. The 5-mC content of testis DNA increased significantly from days 30 to days 150, while in 2-yr-old testis 5-mC content decreased significantly. Among various populations of testicular cells, pachytene spermatocyte DNA contained a significantly high amount of 5-mC when compared to spermatogonia, spermatids and mature sperm DNA. However, the 5-mC content of elongated spermatids was significantly less when compared to the above four fractions. Administration of follicle stimulating hormone to immature rats caused hypomethylation of seminiferous tubular DNA while luteinizing hormone caused similar effects in Leydig cells. These results indicate that in testis, DNA methylation is differentially regulated during development and is controlled by gonadotropic hormones.

5-Methylcytosine↗