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PubMed2004

Genomic structure and expression analysis of the mouse testis-specific ribbon protein (Trib) gene.

During our analyses of genes required for the development and function of the mouse gonads, we identified a novel testis-specific mRNA, transcribed from a gene that we have named testis-specific ribbon protein (Trib). In the mouse, Trib is located on chromosome 15, overlapping with and transcribed in the opposite orientation of the meiosis specific gene Smc1beta. The deduced amino acid sequence of testis ribbon (TRIB) protein is highly conserved between human, mouse, and rat and contains the ribbon motifs found in the largely uncharacterized microtubule ribbon protein ribbon43a (RIB43A). We show by Northern blot analyses and reverse transcription-polymerase chain reaction (RT-PCR) that Trib mRNA is specifically expressed in the adult testis. In situ hybridization indicates that Trib is expressed solely in germ cells during the leptotene-pachytene stages of spermatogenesis. The high level of evolutionary conservation and the cellular and temporal expression suggest that Trib may be required for mouse spermatogenesis and male fertility. Here, we describe the genomic structure and expression profile of mouse Trib and compare its homology with other ribbon proteins.

Amino Acid Sequence↗

PubMed2006

Expression and subcellular localization of GSE protein in germ cells and preimplantation embryos.

We previously identified a novel gonad-specific expression gene (Gse) and investigated its expression during gametogenesis in the mouse testis and ovary. In this study, we generated a polyclonal antibody to GSE protein and determined the profiles of the protein's expression in germ cells and preimplantation embryos in detail using immunocytochemical and immunofluorescence staining. In a Western blot analysis, the anti-GSE antibody recognized long and short isoforms (approximately 27.6 kDa and 23.1 kDa) of the protein in the mouse testis and the long isoform in the ovary. In the mouse testis, GSE protein was expressed in spermatocytes I in the pachytene stage, round spermatids, and elongated spermatids. In the mouse ovary, the protein was located in the cytoplasm and nucleus of all oocytes regardless of the stage of the ovarian follicles. In preimplantation embryos from the pronuclear to blastocyst stage, however, GSE protein was mainly detected in the nuclei of cells. At the blastocyst stage, the protein was confirmed to have accumulated in the inner cell mass (ICM), whereas it had mostly disappeared from the trophectoderm (TE). These findings suggest that GSE protein may play a role in the establishment of nuclear totipotency and may be associated with early lineage specification.

Amino Acid Sequence↗

PubMed1992

Vasopressin biosynthesis in rodent Leydig cells.

Local biosynthesis of the peptide hormone vasopressin is demonstrated in vitro in Leydig cells derived from rat and mouse testis. Cycloheximide-sensitive production of the nonapeptide was shown for rat Leydig cells in primary culture. A polymerase chain reaction technique demonstrated the presence of functionally constituted vasopressin mRNA in rat and mouse testis, primary mouse Leydig cells and in rat and mouse Leydig tumour cell lines (MA10, R2C). Stimulation of cells with gonadotropins, however, had no effect either on peptide production or on levels of specific mRNA. Similarly, treatment of the MA10 cell line with a phorbol ester, or with rat atriopeptin, which activate other second messenger pathways, had no influence on vasopressin mRNA levels. The results are discussed in terms of an autocrine regulatory system which would provide the cell with information about its microenvironment.

Animals↗

PubMed2000

Estrogen receptor alpha has a functional role in the mouse rete testis and efferent ductules.

Previous studies of the estrogen receptor-alpha knockout (alpha ERKO) in the male mouse demonstrate that the rete testis and efferent ductules are targets of estrogen. Because the alpha ERKO mouse lacks a functional estrogen receptor alpha (ER alpha) throughout development, it was not known whether the morphological and physiological abnormalities observed in the alpha ERKO male were due to developmental defects or to dysfunctions concurrent with the lack of ER alpha in the tissue. This study was designed to determine if treatment of normal wild-type (WT) mice with the pure antiestrogen, ICI 182,780, (ICI) could reproduce the morphological characteristics seen in alpha ERKO mice. Thirty-day-old male mice were treated for 35 days with either castor oil or ICI. Age-equivalent alpha ERKO mice were used for comparison. Light microscopic examinations of the reproductive tracts revealed dramatic changes in the efferent ductules of treated mice: a 1.7-fold increase in luminal diameter, a 56% reduction in epithelial cell height, a 60% reduction in brush boarder height of nonciliated cells, and an apparent reduction of the number of observable lysosomes and endocytotic vesicles. Testes of ICI-treated mice showed swollen rete testes area (6.5 times larger than control) and a 65% reduction in rete testis epithelium height. However, there were no significant changes in body and testis weights. These results indicate that ER blockage with ICI in WT mice results in morphological changes of the efferent ductules resembling those seen in alpha ERKO siblings of the same age. Based on this study, we conclude that ER alpha has a functional role in the mouse reproductive tract and the aberrant morphology observed in the efferent ductules of the alpha ERKO mouse is likely the result of a concurrent response to the lack of functional ER alpha, and not solely due to the lack of ER alpha during early developmental times.

Animals↗

PubMed1998

Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes.

Occludin is the only integral membrane protein identified to date as a component of tight junctions (TJs). Here, we examined the distribution and expression of occludin in murine testis bearing well-developed TJ. In the adult mouse testis, occludin was concentrated at TJ strands, which are located at the most basal regions of lateral membranes of Sertoli cells. In immunoblotting, occludin showed a characteristic multiple banding pattern, suggesting that occludin is highly phosphorylated in the testis. In 1-wk-old mouse testis, occludin was distributed diffusely at the lateral membranes of Sertoli cells, and even at this stage, highly phosphorylated occludin was detected. With development, occludin gradually became concentrated at the most basal regions of Sertoli cells. The same results were obtained in rat, but unexpectedly occludin was not detected in human or guinea pig Sertoli cells by immunofluorescence microscopy as well as by immunoblotting. Inasmuch as TJs are also well developed in Sertoli cells of these species, we concluded that, at least in the testes of these species, there are some Sertoli cell-specific isoforms of occludin or other TJ-associated integral membrane proteins that differ from occludin.

Animals↗

PubMed2000

Differential gene expression detected by suppression subtractive hybridization in the ethylene glycol monomethyl ether-induced testicular lesion.

The solvent ethylene glycol monomethyl ether (EGME) produces the same testicular lesions in rodents and human testis cultures, whose onset is characterized by apoptosis of pachytene spermatocytes. To identify gene changes early in the lesion and determine the possible involvement of cells other than the spermatocytes, we employed a suppression subtractive hybridization technique using whole testes from mice treated 8 h previously with 500 mg/kg EGME to generate two subtracted mouse testis cDNA libraries enriched for gene populations either up-regulated or down-regulated by EGME. A total of 70 clones were screened, and 6 of them were shown by Northern blotting to be differentially expressed in the EGME lesion. The three clones with increased expression after EGME treatment were identical to t-complex testis expressed gene 1 (tctex1), a gene encoding ribosomal protein S25, and a heretofore uncharacterized mouse testis expressed sequence tag. Three other genes suppressed by EGME were tctex2, alpha-2,6-sialyltransferase gene, and another uncharacterized mouse testis expressed sequence tag. Predicted peptide sequences of these clones contain multiple motifs for phosphorylation, glycosylation, and myristoylation. In situ hybridization with the antisense RNA probes further supported the expression changes of these six clones and localized the changes in multiple germ cell stages as well as other cell types (Sertoli, interstitial and peritubular cells). These data at the gene expression level are the first to demonstrate the early involvement in this lesion of cell types other than the dying spermatocytes.

Amino Acid Motifs↗

PubMed2003

NYD-SP16, a novel gene associated with spermatogenesis of human testis.

By hybridizing human adult testis cDNA microarrays with human adult and embryo testis cDNA probes, a novel human testis gene NYD-SP16 was identified. NYD-SP16 expression was 6.44-fold higher in adult testis than in fetal testis. NYD-SP16 contains 1595 base pairs (bp) and a 762-bp open reading frame encoding a 254-amino acid protein with 73% amino acid sequence identity with the mouse testis homologous protein. The NYD-SP16 gene was localized to human chromosome 5q14. The deduced structure of the NYD-SP16 protein contains one transmembrane domain, which was confirmed by GFP/NYD-SP16 fusion protein expression in the cytomembrane of the transfected human choriocarcinoma JAR cells, suggesting that it is a transmembrane protein. Multiple tissue distribution indicated that NYD-SP16 mRNA is highly expressed in the testes and pancreas, with little or no expression elsewhere. Further analysis of abnormal expression in infertile male patients revealed complete absence of NYD-SP16 in the testes of patients with Sertoli-cell-only syndrome and variable expression in patients with spermatogenic arrest. Homologous gene expression in mouse testis was confirmed in spermatogenic cells by in situ hybridization. The results of cDNA microarray, in situ hybridization, and semiquantitative polymerase chain reaction in mouse testis of different stages indicated that NYD-SP16 expression is developmentally regulated. These results suggest that the putative NYD-SP16 protein may play an important role in testicular development/spermatogenesis and may be an important factor in male infertility.

Adult↗

PubMed1998

Differential expression pattern of retinoid X receptors in adult murine testicular cells implies varying roles for these receptors in spermatogenesis.

Retinoids have previously been shown to be crucial for normal spermatogenesis. The role of retinoic acid receptors has been studied, but relatively little is known about the function of retinoid X receptors (RXRs). To gain more insight in the function of RXRs during spermatogenesis, the cellular localization of RXRs in the mouse testis was examined using immunohistochemistry and RNase protection assays. In both normal and vitamin A-deficient (VAD) testes, a strong immune response to an RXRalpha antibody occurred in Leydig cells, peritubular myoid cells, and A spermatogonia. Weaker signals were found in spermatocytes and spermatids. In normal testes, an RXRbeta antibody gave a reaction in Leydig cells, and, to a lesser extent, in Sertoli cells, A spermatogonia, pachytene spermatocytes, and spermatids. In Leydig cells, a cytoplasmatic signal was found in addition to the nuclear signal. In the VAD testis, only Leydig cells and A spermatogonia were positive, which indicates that RXRbeta expression may be dependent on the retinoid status. Previous studies have shown RXRgamma mRNA expression in the mouse testis at a low level. Nevertheless, an RXRgamma antibody caused a strong immune response in interstitial cells and in A spermatogonia, and a weak signal in pachytene spermatocytes. These immunohistochemical data were supported by the results of RNase protection assays on mRNA of testicular cell isolations. In conclusion, the different RXRs in the mouse testis have distinct expression patterns, suggesting that they may have different functions.

Animals↗

PubMed2005

Single-chain tissue-type plasminogen activator is a substrate of mouse glandular kallikrein 24.

Leydig cells of the adult mouse testis express at a detectable level three distinct glandular (tissue) kallikrein genes: mKlk21, mKlk24, and mKlk27. Recently, the proteins encoded by these genes were characterized using active recombinant proteases, but their roles in the mouse testis remained to be determined. The present study showed that among the proteases, mK24 markedly enhanced the activity of human recombinant single-chain tissue-type plasminogen activator when the two were incubated together. This activation was found to be due to proteolytic conversion of the single-chain enzyme to a two-chain form. The expression of tissue-type plasminogen activator in interstitial Leydig cells was demonstrated by RT-PCR and immunohistochemical analyses. The primary culture medium of adult male testicular Leydig cells contained immunoreactive substances recognized by anti-mK24 antibodies. In addition, the same medium was capable of converting the single-chain plasminogen activator to the two-chain protein. These results suggest that mK24 may play a role in the degradation of extracellular matrix proteins in the interstitial area surrounding the Leydig cells of the adult mouse testis, due not only to its own activity, but also to that of plasmin produced by the single-chain tissue-type plasminogen activator-converting activity of mK24.

Animals↗

PubMed2006

Human testicular protein NYD-SP16 is involved in sperm capacitation and the acrosome reaction.

OBJECTIVE: To investigate the functional role of human testicular protein NYD-SP16. DESIGN: Controlled experimental study. SETTING: University research laboratory. ANIMAL(S): ICR strain of mice. INTERVENTION(S): Testicular tissue and sperms were collected from 12- to 16-week-old male mice; cumulus-oocyte complexes were harvested from mature female mice after inducing superovulation. MAIN OUTCOME MEASURE(S): Expression of NYD-SP16 in mouse testis was analyzed by immunohistochemistry, its localization in mouse sperm was evaluated by immunofluorescence, and the functional role of NYD-SP16 in the process of fertilization was determined by CTC staining and in vitro fertilization. RESULT(S): In mouse testis, NYD-SP16 was immunolocalized to elongating spermatids and the staining was confined to the head. Immunoreactivity in mouse sperm was mainly seen in the acrosomal region and this expression pattern was not altered in capacitated sperm. However, after the acrosome reaction (AR), the intensity of the fluorescence staining attenuated significantly. NYD-SP16 antiserum significantly inhibited mouse sperm capacitation and the AR in a concentration-dependent manner and the presence of anti-NYD-SP16 serum, during co-incubation of gametes, produced a concentration-dependent decrease in the percentage of zygotes. CONCLUSION(S): NYD-SP16 protein is a component of sperm acrosome, which plays a functional role in sperm capacitation and the AR and is consequently necessary for fertilization.

Acrosome Reaction↗

PubMed2001

Mouse testis-brain RNA-binding protein (TB-RBP): expression, purification and crystal X-ray diffraction.

TB-RBP (testis-brain RNA-binding protein) is a mouse RNA-binding protein that controls the temporal and spatial expression of mRNA. Found most abundantly in brain and male germ cells in the testis, TB-RBP is known to suppress the translation of specific testicular and brain mRNAs as part of cell development. TB-RBP-mRNA complexes can bind microtubules and thereby facilitate RNA translocation. Translin is the human orthologue of TB-RBP which binds to single-stranded ends of DNA sequences in breakpoint regions of chromosomal translocations. TB-RBP/translin has been crystallized in space group P2(1)2(1)2. The expression, purification, and crystallization of TB-RBP are described as well as preliminary X-ray diffraction data. The multimeric state of TB-RBP is addressed using dynamic light-scattering results.

Animals↗

PubMed1987

Molecular characterization of the testis specific c-abl mRNA in mouse.

The c-abl gene encodes a protein tyrosine kinase and is transcribed from at least two promoters giving rise to transcripts of two size classes of approximately 5 and 6 kb in length. These mRNAs only differ in their most 5' exon and encode proteins of similar size but with different N-termini. In the mouse testis an additional abundant c-abl mRNA of 4 kb is detected. This mRNA was shown to be expressed in the haploid male germ cells of the adult mouse. Here we describe the cloning and molecular characterization of a cDNA representing the testis specific c-abl transcript. We show that the 4 kb c-abl mRNA arises from alternative polyadenylation of an RNA transcribed from the same promoter as the 5 kb mRNA. The site of polyadenylation is unusual in this shorter transcript as it is not preceded by the highly conserved hexanucleotide AAUAAA. The use of this polyadenylation site removes 1.2 kb of 3' sequences present in the somatic c-abl mRNAs, but does not affect the main open reading frame of the transcript. Using in situ hybridization on whole testis sections it is shown that the 4 kb c-abl mRNA is most abundant in the elongating spermatids.

Animals↗

PubMed2003

[Molecular cloning of mTSARG3 gene related to apoptosis in mouse spermatogenic cells].

Beginning from a mouse EST (GenBank Accession No: BE644537) which was significantly changed in cryptorchidism and represented a novel gene, GeneScan program was performed and a predicted mouse novel gene full-length cDNA sequence containing the BE644537 sequence was attained. Gene-specific primers were designed for PCR in mouse testis cDNA library. The sequencing result of the PCR product showed that we obtain a new gene mTSARG3 (GenBank Accession No: AF419292) whose full cDNA length is 1328 bp containing 8 exons and 7 introns. The predicted open reading frame encodes a protein of 316 amino acid residues. The protein encoded by the new gene is a new member of HSP40 protein family because the sequence contains the highly conserved J domain which is present in all DnaJ-like proteins and is considered to have a critical role in DnaJ-DnaK protein-protein interactions. mTSARG3 protein displays a 46% identity in a 336-amino-acid overlap with DJB4-MOUSE protein. The result of RT-PCR analysis and Northern blot showed that mTSARG3 is specifically expressed in mouse testis. Southern blot showed that there were no loss and rearrangement in cryptorchid. Based upon all these observations, it is considered that the function of the new gene is related to inhibit mouse testis spermatogenesis apoptosis.

Amino Acid Sequence↗

PubMed1996

Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion.

A new gene family of multidomain membrane proteins (ADAMs) that include A Disintegrin And Metalloprotease domain comprises an increasing number of identified members. Two members of this family, fertilin alpha and fertilin beta, form a heterodimeric protein that is required for sperm-egg fusion. Most recently, it has been shown that a third family member, meltrin alpha, is involved in myoblast fusion (Yagami-Hiromasa et al., 1995, Nature 377: 652-656). Using restriction fragment length polymorphism analysis of a DNA panel from an interspecific backcross, we have determined the chromosomal locations of four mouse genes of this family that are expressed in testis: fertilin alpha, fertilin beta, ADAM 4, and ADAM 5. These genes have been given the locus symbols Ftna (fertilin alpha), Ftnb (fertilin beta), Adam4 (ADAM 4), and Adam5 (ADAM 5). They were mapped to chromosomes 5, 14, 9, and 8, respectively, revealing a dispersed localization. Human chromosome locations of these genes are predicted on the basis of the mapping results using the information provided by comparative linkage maps. Because all four of these ADAM genes are expressed in testis and fertilin alpha and beta have been found to be important for fertilization, we compared their chromosomal locations with known mouse mutations affecting spermatogenesis and fertility.

ADAM Proteins↗

PubMed1995

A Bkm-associated human y-chromosomal DNA is conserved and transcribed in the testis of mouse.

Y chromosome associated genes and repetitive sequences are continually viewed from the point of view of their possible involvement in sex determination and in the evolution of such a mechanism, thus sustaining an interest in the identification of novel sequences to gain newer insights. Here we have used the highly conserved class of Bkm repeats to isolate its associated sequences from the Y chromosome under the assumption that these sequences could be involved in sex determination and might also reflect the evolutionary status of the Y chromosome. Towards this end we have screened a genomic library enriched with human Y chromosome DNA with Bkm. One of the positive clones, C65, has a pericentromeric location on the Y chromosome and is present in a number of human sex-reversed XX males. The 10.5kb insert of clone C65 has been further subcloned (pFI, pFII, pFIII, pFIV). The subclone pFIII is present in both sexes in human and mouse, whereas pFIV is primate specific and present in both sexes. pFII contains sequences homologous to Bkm. pFI is conserved in mouse and man, but is Y specific only in primates. Although present in both sexes in mouse, pFI is transcribed specifically in the male testis suggesting that it may be involved in the process of sex determination or testis differentiation and spermatogenesis.

Animals↗

PubMed1983

Effects of human choriogonadotropin on mitochondrial and microsomal cytochrome P-450 levels in mouse testes.

The mitochondrial and microsomal cytochrome P-450 contents of C57B1/6 mouse testis have been measured using difference spectroscopy on stable enzyme preparations containing the ferrous-carbon monoxide complex. Results were obtained on control animals (52 +/- 3 days of age) and on animals injected subcutaneously with human choriogonadotropin (0.017 micrograms/g body weight 24 h prior to sacrifice). The high ratio of testicular mitochondrial cytochrome oxidase to P-450, which has previously precluded measurements of basal P-450 levels, was overcome by using N,N,N',N'-tetramethyl-p-phenylene diamine to bypass site II, in combination with antimycin A to prevent reverse electron flow. The basal levels of mitochondrial and microsomal P-450 in mouse testis were 37.9 +/- 3.5 and 28.9 +/- 1.6 pmol/mg protein, respectively. Following administration of a desensitizing dose of gonadotropin, the respective values were lowered to 19.9 +/- 1.4 and 19.6 +/- 2.1 pmol/mg protein in 24 h. This is the first report of a gonadotropin-mediated decrease in mitochondrial P-450 and thus demonstrates that desensitization leads to alterations in both microsomal and mitochondrial P-450 in mouse testis.

Animals↗

PubMed1999

Recipient preparation is critical for spermatogonial transplantation in the rat.

Testis cell transplantation from mice or rats into recipient mouse seminiferous tubules results in donor cell-derived spermatogenesis in nearly all host testes. Normal spermatozoa are produced and, in the most successful mouse transplantations, the donor haplotype is transmitted to progeny of the recipient. However, few studies have been performed in other species. In this report, we demonstrate that rat and mouse testis cells will generate donor cell-derived spermatogenesis in recipient rat seminiferous tubules. Depletion of endogenous spermatogenesis before donor cell transplantation was more difficult in rat than reported for mouse recipients. A protocol employing treatment of neonatal rats with busulfan was most effective in preparing recipients and allowed more than 90% of testes to be colonized by donor cells. Transplantation of mouse testis cells into rat seminiferous tubules was most successful in recipients made cryptorchid and treated with busulfan. In the best experiments, about 55% of rat testes were colonized by mouse cells. Both rat and mouse donor cell-derived spermatogenesis were improved by treatment of rat recipients with leuprolide, a gonadotropin-releasing hormone agonist. The studies indicated that recipient preparation for spermatogonial stem cell transplantation was critical in the rat and differs from the mouse. However, modification of currently used techniques should allow male germ line stem cell transplantation in many species.

Age Factors↗

PubMed1995

The Sry-related HMG box-containing gene Sox6 is expressed in the adult testis and developing nervous system of the mouse.

We have cloned and sequenced a full-length cDNA for the HMG box-containing, SRY-related gene Sox6 from mouse. The deduced protein sequence of Sox6 has considerable homology with that of the previously determined Sox5 sequence. It seems likely that these genes have diverged more recently than other members of the SOX gene family, although the two genes map to different chromosomes in the mouse. In common with Sox5, Sox6 is highly expressed in the adult mouse testis and the HMG domains of both proteins bind to the sequence 5'-AACAAT-3'. This suggests that the two genes may have overlapping functions in the regulation of gene expression during spermatogenesis in the adult mouse. However, Sox6 may have an additional role in the mouse embryo, where it is specifically expressed in the developing nervous system.

Amino Acid Sequence↗