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PubMed1992

Immunolocalization of a 25-kilodalton protein in mouse testis and epididymis.

We have recently observed that a polyclonal antibody raised against a mouse epididymal luminal fluid protein (MEP 9) recognizes a 25-kDa antigen in mouse testis and epididymis [Rankin et al., Biol Reprod 1992; 46:747-766]. This antigen was localized by light and electron microscopic immunohistochemistry. The immunoreactivity in the testis was found in the residual cytoplasm of the elongated spermatids, in the residual bodies, and in the cytoplasmic droplets of spermatozoa. In the epididymis, the epithelial principal cells were stained from the distal caput to the distal cauda. Immunogold labeling in the principal cells showed diffuse distribution without preferential accumulation in either the endocytic or the secretory apparatus of the cells. In the epididymal lumen, the immunoreactivity was restricted to the sperm cytoplasmic droplets. No membrane-specific labeling was observed in luminal spermatozoa, cytoplasmic droplets, or isolated sperm plasma membranes. Three weeks after hemicastration or severance of the efferent ducts, a normal distribution of the immunoreactive sites was found in the epididymis. Immunoreactivity, was also detected in the epididymal epithelium of immature mice as well as in that of XXSxr male mice having no spermatozoa in the epididymis. These results suggest that the immunoreactivity seen in the principal cells originates from synthesis rather than endocytosis of the testicular protein from disrupted cytoplasmic droplets. Furthermore, these results suggest that the 25-kDa protein is synthesized independently by both testis and epididymis.

Animals↗
PubMed1980

Loss of mouse testis mass after X-irradiation or injection of 22Na.

Mass loss in the mouse testis per unit of absorbed dose was used as a means of comparing acute external with protracted internal whole body irradiation. The external and internal sources were X-rays and 22Na respectively. Estimates of the absolute dose to the testis from 22Na were made. The effects of acute and protracted radiation on the integrated loss in mass in the testis per unit of absorbed dose are similar.

Animals↗
PubMed2005

Retinoic acid metabolism and signaling pathways in the adult and developing mouse testis.

As a first step in investigating the role of retinoic acid (RA) in mouse testis, we analyzed the distribution pattern of the enzymes involved in vitamin A storage (lecithin:retinol acyltransferase), RA synthesis (beta-carotene 15,15'-monoxygenase and retinaldehyde dehydrogenases) and RA degradation (cytochrome P450 hydroxylases) as well as those of all isotypes of receptors transducing the RA signal [RA receptors (RARs) and rexinoid receptors (RXRs)]. Our data indicate that in adult testis 1) cytochrome P450 hydroxylase enzymes may generate in peritubular myoid cells a catabolic barrier that prevents circulating RA and RA synthesized by Leydig cells to enter the seminiferous epithelium; 2) the compartmentalization of RA synthesis within this epithelium may modulate, through paracrine mechanisms, the coupling between spermatogonia proliferation and spermatogenesis; 3) retinyl esters synthesized in round spermatids by lecithin:retinol acyltransferase may be transferred and stored in Sertoli cells, in the form of adipose differentiation-related protein-coated lipid droplets. We also show that RARalpha and RXRbeta are confined to Sertoli cells, whereas RARgamma is expressed in spermatogonia and RARbeta, RXRalpha, and RXRgamma are colocalized in step 7-8 spermatids. Correlating these expression patterns with the pathological phenotypes generated in response to RAR and RXR mutations and to postnatal vitamin A deficiency suggests that spermiation requires RXRbeta/RARalpha heterodimers in Sertoli cells, whereas spermatogonia proliferation involves, independently of RXR, two distinct RAR-mediated signaling pathways in both Sertoli cells and spermatogonia. Our data also suggest that the involvement of RA in testis development starts when primary spermatogonia first appear.

Animals↗
PubMed1987

Autoradiographic study of binding and internalization of follicle-stimulating hormone in the mouse testis minces in vitro.

The internalization of FSH-receptor complexes was demonstrated in mouse testis by means of light and electron microscopic autoradiography. Chopped testicular pieces were incubated with radioiodinated FSH (131I-NIADDK-rat FSH-I-4) for 10, 20, 60 and 180 min. After incubation the pieces were fixed with glutaraldehyde containing tannic acid, and embedded in Spurr's resin. Semithin and ultrathin sections were cut for light and electron microscopic autoradiography, respectively. In light microscopic autoradiographs, silver grains were preferentially localized over Sertoli cells, regardless of incubation time. Sixty to 70% of the total number of grains were located over Sertoli cells which account for only about 4% of the total cell population of the seminiferous tubules. The majority of these grains correspond to the specific FSH binding sites, because few grains remained after incubation with an excess amount of unlabeled FSH. In electron microscopic autoradiographs, the half-distance (HD) value for the 131I-labeled line source was about 216 nm in the present study. After 10 min of incubation, 56.6% of the total number of silver grains were located over the plasma membrane of Sertoli cells. In testicular pieces incubated for longer periods (20, 60 and 180 min), both the percentage and relative concentration of grains increased in the Golgi apparatus and lysosomes and decreased in the plasma membrane. These results suggest that [131I]iodo-FSH first binds to FSH receptors on the plasma membrane of Sertoli cells, then FSH-receptor complexes are internalized. The increase in the number of grains over the lysosomes following longer incubation, indicates that internalized [131I]iodo-FSH or FSH-receptor complexes are subjected to degradation.

Animals↗
PubMed2006

Gene expression study in the juvenile mouse testis: identification of stage-specific molecular pathways during spermatogenesis.

A gene expression time course in the juvenile mouse testis was established using cDNA microarrays derived from a variety of isolated testis cell types. In conjunction with the use of four germ cell-deficient mouse models, a stage and cell-type classification over nine time points has been obtained and analyzed for differential expression of genes. The expression profiles have been clustered into nine groups and subjected to detailed analysis of associated gene ontology. This has allowed the correlation of particular cellular processes and functions with different expression clusters. Focused analysis of transcripts involved in cell number regulation (apoptosis and proliferation) and their spatiotemporal expression patterns are presented. The findings indicate that for genes involved in both apoptosis and proliferation, several distinct pathways regulating these processes are active in somatic and germ cell lineages.

Animals↗
PubMed1986

Histone messenger RNAs of the mouse testis.

A 6-12S RNA fraction has been isolated following sucrose gradient fractionation of mouse testis RNA, and further resolved into poly A+ and poly A- RNA fractions by oligo-(dt)-cellulose chromatography. Polyacrylamide gel electrophoresis of products formed in a reticulocyte lysate-dependent cell-free translation system has enabled identification of histone variants, H1t, H2S, H2A . X, an H4-like protein and a low Mr protein (presumably TP and/or protamine). Cell-free synthesis of a number of these histone variants appears to be directed by poly A+ mRNAs.

Animals↗
PubMed1995

Identification of thyrotropin-releasing hormone receptor mRNA in the Leydig cells of the mouse testis by in situ hybridization.

Thyrotropin-releasing hormone receptor (TRH-R) mRNA was detected in cryostat sections of the mouse testis using biotinylated oligonucleotides complementary to the cDNA encoding the mouse pituitary TRH-R by in situ hybridization. Hybridization signals were detected exclusively in the Leydig cells. The intensity of the signal was probe-concentration dependent. This result suggests that testicular TRH may serve as an autocrine regulator of reproductive function and development via TRH-R in a fashion that is similar or identical to that in the pituitary.

Animals↗
PubMed1992

The cDNA cloning, nucleotide sequence and expression of an intracellular protein tyrosine phosphatase from mouse testis.

The PTP-1 cDNA encoding an intracellular protein tyrosine phosphatase (PTPase) was isolated and sequenced from a mouse testis cDNA library. This PTP-1 cDNA was found to contain an open reading frame of 1,296 nucleotides as well as 5' (83 nucleotides) and 3' (289 nucleotides) non-coding regions. The deduced sequence of 432 amino acids of mouse PTPase-1 exhibited 93% and 83% identity to that of rat PTPase-1 and human PTPase-1B, respectively. Thus, this PTP-1 is a mouse homologue of human PTP-1B and rat PTP-1. Northern blot analysis indicated that PTP-1 mRNAs were most abundant in testis, and were detected in sizes of 4.4 Kb, 2.4 Kb and 2.2 Kb, 2.0 Kb. The PTP-1 transcripts of 4.4 Kb and 2.0 Kb, but not 2.4 Kb and 2.2 Kb, were also present in kidney, spleen, muscle, liver, heart and brain. Genomic blot analysis showed that a single copy of the PTP-1 gene is contained in the mouse genome and that introns are present in mammalian PTP-1 genes.

Amino Acid Sequence↗
PubMed2003

Co-localized expression of FasL, Fas, Caspase-3 and apoptotic DNA fragmentation in mouse testis after oral exposure to di(2-ethylhexyl)phthalate.

Expression of apoptosis-related proteins FasL, Fas and Caspase-3, as well as DNA fragmentation were examined in mouse testis 12 h after exposure to 4-0.004 mg/g di(2-ethylhexyl)phthalate (DEHP). Immunocytochemical examination of the highest dose (4 mg/g DEHP) mouse revealed a distribution of FasL in Sertoli cell and Fas in nearby spermatocyte, and Fas and Caspase-3 in the same spermatocyte. Fas-positive spermatocytes had a DNA-fragmented nucleus detectable by terminal deoxynucleotidyl transferase-mediated fluorescein-dUTP nick end labeling (TUNEL) method. After exposure to 4, 0.4, 0.04 or 0.004 mg/g DEHP, the maximum number of nuclei with fragmented DNA per 0.5 microm testis section was 22, 7, 5 and 3, respectively. In unexposed control the maximum number was 3. To further estimate total amount of the fragmented DNA in testis of the exposed mouse, the extracted DNA fragments were analyzed by agarose gel electrophoresis. The amount of fragments in the first three steps of the DNA ladder was estimated by a photo-densitometry. In the highest dose mouse (4 mg/g DEHP), the fragmented DNA was 2.2 times as much in the control. In lower dose mouse (0.4, 0.04 or 0.004 mg/g DEHP), it was 1.1 times as much in the control. Taken together, these observations suggest that a single oral exposure to DEHP as low as 0.04 mg/g might be effective to testicular DNA fragmentation and apoptosis.

Administration, Oral↗
PubMedDate not supplied

Two lectin-like receptors for alpha 1-acid glycoprotein in mouse testis.

Three glycoforms of alpha 1-acid glycoprotein (AGP) were biotinylated to examine their binding in mouse testis by light microscopy. The transition from one stage to another in the spermatogenic cycle is marked with an appearance of a receptor for the Concanavalin A (Con A) non-reactive glycoform AGP-A in the cytoplasm of spermatocytes, young spermatids and Sertoli cells. This receptor disappears in the late stages of the spermatids. The Con-A intermediately reactive and the Con-A reactive glycoforms, AGP-B and AGP-C, showed weak reaction in the cytoplasm of spermatocytes, spermatids and Sertoli cells and, at the last stages in the spermatogenic cycle, a very strong reaction in the late elongated spermatids and the apical extensions of Sertoli cells. The interactions are lectin-like as confirmed by inhibition with simple sugars. In addition, the bindings were inhibited by steroid hormones. AGP-A was inhibited by testosterone, oestradiol and progesterone, while AGP-B and AGP-C were inhibited by mannose, GlcNAc, cortisone, aldosterone, oestradiol and progesterone. The receptors and the corresponding AGP glycoforms may be adhesion molecules between Sertoli cells and the spermatogenic cells and may have a function as a regulatory factor for spermatozoa development.

Animals↗
PubMed1994

Differential distribution of the alpha 6 subunit of integrins in the development and sexual differentiation of the mouse testis.

The distribution of the alpha 6 subunit of integrins in the development and sexual differentiation of mouse testis was analyzed by light and electron microscopy during the embryonic, fetal and early postnatal periods. At the pregonadal phase only the epithelial cells of the mesonephric duct and of the distal mesonephric tubules showed a reaction to alpha 6, whereas the surface epithelium and the mesenchyme of the mesonephros were negative or contained only a rudimentary amount of the alpha 6 subunit. With the formation of the gonadal ridge and the testicular blastema, the gonadal cells became positive for the alpha 6 subunit. This expression remained in embryonic cord cells and in the vascular endothelial cells, whereas the differentiating cells of the surface epithelium, tunica albuginea, the Leydig cells, and the interstitial mesenchymal cells were negative. With the fetal and postnatal differentiation, the expression of the alpha 6 subunit gradually diminished in the cord cells, and by the prepubertal phase, alpha 6 was found only at adhesion sites between some Sertoli cells. Similar changes were seen in the mesonephric duct and tubules, and in the rete cords. The presence of alpha 6 in regions undergoing developmental cell aggregation processes and their disappearance during tissue maturation, suggest that alpha 6 plays a specific but transient role in gonadal cell adhesion necessary for the histogenetic organization of the testis. In addition to its role in developing and organizing cells, alpha 6 integrin was also a prominent component in degenerating cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Analysis of cDNA sequences from mouse testis.

Few mammalian proteins involved in chromosome structure and function during meiosis have been characterized. As an approach to identify such proteins, cDNA clones expressed in mouse testis were analyzed by sequencing and Northern blotting. Various cDNA library screening methods were used to obtain the clones. First, hybridization with cDNA from testis or brain allowed selection of either negative or differentially expressed plaques. Second, positive plaques were identified by screening with polyclonal antisera to prepubertal testis nuclear proteins. Most clones were selected by negative hybridization to correspond to a low abundance class of mRNAs. A PCR-based solid-phase DNA sequencing protocol was used to rapidly obtain 306 single-pass cDNA sequences totaling more than 104 kb. Comparison with nucleic acid and protein databases showed that 56% of the clones have no significant match to any previously identified sequence. Northern blots indicate that many of these novel clones are testis-enriched in their expression. Further evidence that the screening strategies were appropriate is that a high proportion of the clones which do have a match encode testis-enriched or meiosis-specific genes, including the mouse homolog of a rat gene that encodes a synaptonemal complex protein.

Amino Acid Sequence↗
PubMed1981

DNA analysis and sorting of viable mouse testis cells.

The dye Hoechst 33342 and a 2-parameter cell sorter have been used to measure DNA content in viable testis cells and to sort pachytene spermatocytes and round spermatids from adult mouse testis to virtually 100% homogeneity. Early diploid spermatogenic cells were enriched to 90%, a 10-fold purification. The capability for viable sorting of most testis cell types to homogeneity in numbers suitable for many biochemical applications is demonstrated.

Animals↗
PubMed2001

Expression of LIM Protein KyoT in Adult Mouse Testis.

The KyoT expression in the adult mouse was reported here for further investigation on the functions of KyoT in adult mouse. To study the expression of mRNA and protein of KyoT, Northern blot, RT-PCR, Immunohistochemical SABC methods and in situ hybridization methods were used in the experiments. Two kinds of KyoT were expressed at high levels in testis of adult mouse, and KyoT immunore activity was mainly located in Leydig's cells. The reactive substance was distributed in cytoplasm rather than in nuclei. KyoT mRNA hybridization signals were also detected in cytoplasm of Leydig's cells rather than in nuclei. The spermatogenic cells and negative controls showed negative results. These results suggest that KyoT was expressed in testis of adult mouse and mainly located in Leydig's cells.

Journal Article↗
PubMed1984

Evidence for the re-establishment of a heterogeneity in radiosensitivity among spermatogonial stem cells repopulating the mouse testis following depletion by X-rays.

Earlier studies have shown that the spermatogonial stem cells of the mouse testis recovering from previous radiation or chemical mutagen exposure give subnormal yields of genetic damage with subsequent X-irradiation. This response has been investigated further: (a) with a high, 9-Gy X-ray dose given 4, 12 or 21 days after a 1-Gy conditioning dose (Expt. 1), and (b) with a 1 + 7-Gy, 24-h fractionation regime given 4 or 14 days after a 1-Gy conditioning dose (Expt. 2). In Expt. 1 the 1 + 9-Gy, 4-day interval regime gave a very low response, lower than obtained previously with an equivalent 1 + 5-Gy treatment. This suggests that a heterogeneity in radiosensitivity, such as exists in unirradiated stem cell populations and absent 24-48 h after radiation depletion, is quickly re-established among the stem cells repopulating the testis. By contrast, the 1 + 7-Gy, 24-h fractionation when given 4 days after the 1-Gy conditioning dose (Expt. 2) gave a very high yield of genetic damage, almost as high as that given by the fractionated (1 + 7 Gy) dose applied to previously unirradiated stem cells. This suggests that the newly established heterogeneity is removed by the second 1-Gy conditioning dose. With longer intervals between treatments, genetic yields consistent with additivity were obtained in Expt. 1; less clear results were obtained Expt. 2. Comparison with earlier data generally suggested that the duration of the repopulating period is dose-dependent. In a third experiment evidence was obtained that genetic damage induced by X-irradiation can be reduced by a subsequent treatment with triethylenemelamine (TEM) during the repopulating phase. This confirmed an earlier finding. Such an interaction could not be demonstrated with two X-ray treatments. An explanation for the X-ray/TEM interaction is offered.

Animals↗
PubMed2006

New PKCdelta family members, PKCdeltaIV, deltaV, deltaVI, and deltaVII are specifically expressed in mouse testis.

We isolated and characterized four new PKCdelta isoforms, PKCdeltaIV, deltaV, deltaVI, and deltaVII, specifically expressed in the mouse testis. These isoforms possess neither V1 nor C2-like domains. Moreover, PKCdeltaVI and deltaVII have a different last exon as their V5 domain. The transcription of PKCdeltaIV, deltaV, deltaVI, and deltaVII is initiated from the same site in the upstream region of exon4 of the PKCdelta gene. They are expressed exclusively in the testis in an age-dependent manner. PKCdeltaIV and deltaV are expressed in spermatids with sperm maturation stage-specific manner, and that PKCdeltaVI and deltaVII are expressed in spermatogonia and spermatocytes.

Animals↗
PubMed1985

Estimation of glutathione in purified populations of mouse testis germ cells.

Glutathione (GSH), a ubiquitous cysteine-containing tripeptide, is present in high concentration in adult mouse testis (4.3 +/- 0.2 mumol/g). Examination of testis at 0, 7, 14, 21, 28, 35, 42, 50, and 60 days of age reveals that the level of testicular GSH, only 1.4 +/- 0.1 mumol/g in neonates, increases steadily until 28 days of age, when the adult level is reached. An even steeper increase in GSH concentration, when expressed in mumol/mg DNA, is seen between 0 days (0.19 +/- 0.01) and 42 days (1.19 +/- 0.05), at which time the adult level is attained. Enzymatic dissociation of 4-wk-postnatal seminiferous epithelium, using collagenase and dispase either sequentially or in combination, followed by unit gravity sedimentation, yielded maximal GSH concentrations (mumol/mg DNA) in those cell fractions most enriched in pachytene spermatocytes, followed by a second slightly lower peak of activity in the purest round spermatid fraction, which may have lost a significant percentage of its original GSH content. A relatively high GSH content in condensing spermatids, which are at present not isolable without loss of cytoplasm, is implied by the continually increasing levels of testicular GSH/mg DNA between 28 and 42 days of age. It is proposed that retention of GSH is a sensitive indicator of germ cell viability following cell separation procedures. The functions of GSH during meiotic and postmeiotic germ cell development may include protection against mutagens and reduction of disulfide bonds during the processing of cysteine-containing proteins.

Age Factors↗
PubMed1982

Biochemical and immunological analysis of an abundant form of glutathione S-transferase, in mouse testis.

One of the major forms of glutathione S-transferase (designated as Ft transferase) has been identified and purified to near homogeneity from mouse testis. The purification was achieved by ammonium sulfate fractionation, DEAE cellulose chromatography, hydroxylapatite chromatography and the preparative isoelectric focusing. Purified Ft transferase has an isoelectric point of 4.9 +/- 0.3 and was shown to be a homodimer with a native molecular weight of about 50000. Immunologically, antisera to Ft transferase do not crossreact with F2 or F3 transferase. However, a weak cross reactivity was observed between the antisera to F3 transferase and FT transferase. Biochemical properties of purified Ft transferase are similar to those transferases isolated from mouse liver. Tissue distributions of the multiple forms of glutathione S-transferase were examined by column isoelectric focusing of various mouse tissue homogenates. It was found that mouse Ft transferase is present only in testis as a major form and in brain as a minor form, but not in other tissues that were examined.

Animals↗