Expression of Selenoprotein-P Messenger Ribonucleic Acid in the Rat Testis

Koga, Minoru; Tanaka, Hiromitsu; Yomogida, Kentaro; Tsuchida, Junji; Uchida, Katsuo; Kitamura, Masaya; Sakoda, Saburo; Matsumiya, Kiyomi; Okuyama, Äkïhïko; Nishimune, Yoshitake

doi:10.1095/biolreprod58.1.261

Cited by 58 publications

(34 citation statements)

References 25 publications

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“…The present data indicated that the expression of Sepp mRNA in the developing kidney was abundantly detected in the metanephric corpuscles and tubules. Sepp is required for sperm development and is expressed predominantly in the interstitial Leydig cells in the rat and mouse testes (Koga et al, 1998;Steinert et al, 1998;Olson et al, 2005). In the present study, Sepp mRNA was expressed predominantly in the interstitial Leydig cells in the developing testes.…”

Section: Discussionsupporting

confidence: 60%

Spatiotemporal expression of the selenoprotein P genein postimplantational mouse embryos

Lee¹,

Yon²,

Baek³

et al. 2008

Int. J. Dev. Biol.

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Selenoprotein P (Sepp) is an extracellular glycoprotein which functions principally as a selenium (Se) transporter and antioxidant. In order to assess the spatiotemporal expression of the Sepp gene during mouse embryogenesis, quantitative RT-PCR and in situ hybridization analyses were conducted in embryos and extraembryonic tissues, including placenta. Sepp mRNA expression was detected in all embryos and extraembryonic tissues on embryonic days (E) 7.5 to 18.5. Sepp mRNA levels were high in extraembryonic tissues, as compared to embryos, on E 7.5-13.5. However, the levels were higher in embryos than in extraembryonic tissues on E 14.5-15.5, but were similar in both tissues during the subsequent periods prior to birth. According to the results of in situ hybridization, Sepp mRNA was expressed principally in the ectoplacental cone and neural ectoderm, including the neural tubes and neural folds. In whole embryos, Sepp mRNA was expressed abundantly in nervous tissues on E 9.5-12.5. Sepp mRNA was also expressed in forelimb and hindlimb buds on E 10.5-12.5. In the sectioned embryos, on E 13.5-18.5, Sepp mRNA was expressed persistently in the developing limbs, gastrointestinal tract, nervous tissue, lung, kidney and liver. On E 16.5-18.5, Sepp mRNA expression in the submandibular gland, whisker follicles, pancreas, urinary bladder and skin was apparent. In particular, Sepp mRNA was detected abundantly in blood cells during all the observed developmental periods. These results show that Sepp may function as a transporter of selenium, as well as an antioxidant, during embryogenesis.

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Section: Discussionsupporting

confidence: 60%

Spatiotemporal expression of the selenoprotein P genein postimplantational mouse embryos

Lee¹,

Yon²,

Baek³

et al. 2008

Int. J. Dev. Biol.

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“…Testicular cells were fractionated by a modification of the methods described by Raeside & Renaud (1983) and Koga et al (1998). Small tissue cubes taken from the pubertal testis at 18 weeks of age were cut thinly by hand to obtain tissue slices measuring 1 cm 2 !3-5 mm thick.…”

Section: Fractionation Of Testicular Cellsmentioning

confidence: 99%

Evidence for expression of relaxin hormone-receptor system in the boar testis

Kato¹,

Siqin²,

Minagawa³

et al. 2010

Journal of Endocrinology

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Although the physiological role of relaxin (RLN) in males remains largely unknown, there is limited evidence that the testis might be a candidate source and target of RLN in boars, as RLN transcripts are detected in the boar testis and it contains RLN-binding sites. To determine whether the boar testis acts as a source and target tissue of RLN, we characterised the expression pattern and cellular localisation of both RLN and its own receptor LGR7 (RXFP1) in boar testes during postnatal development by molecular and immunological approaches. Testes were collected from Duroc boars, and partial cDNA sequences of the boar homologue of human RXFP1 were identified. RLN expression increased through puberty onwards, while RXFP1 expression changed little during development.RLN mRNA and protein expression were restricted to the Leydig cells, whereas both Leydig cells and seminiferous epithelial cells expressed RXFP1 mRNA and protein.Interestingly, RLN was expressed in the testis as an 18 kDa form (the expected size of proRLN), but not as the 6 kDa mature form, during development because of a lack of the enzyme required for proRLN processing. In contrast, RXFP1 was detected at all stages as specific bands of 75 and 91-95 kDa (likely non-glycosylated and glycosylated RXFP1 respectively). Thus, we provide evidence for expression of RLN-RXFP1 ligand-receptor system in the boar testis, suggesting that the testis act as a source and possible target tissue of RLN.

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“…Germ and other somatic cells of the testes were prepared as described in our previous report (22). Cryptorchid testes and those of various mutants defective in germ cell differentiation such as jsd/jsd, Sl 17H /Sl 17H , and W/W v were also used (5).…”

Section: Construction Of the Subtracted Library And Screening-totalmentioning

confidence: 99%

Identification and Characterization of a Haploid Germ Cell-specific Nuclear ProteinKinase (Haspin) in Spermatid Nuclei and Its Effects on Somatic Cells

Tanaka¹,

Yoshimura²,

Nozaki³

et al. 1999

Journal of Biological Chemistry

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110

111

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We have cloned the entire coding region of a mouse germ cell-specific cDNA encoding a unique protein kinase whose catalytic domain contains only three consensus subdomains (I-III) instead of the normal 12. The protein possesses intrinsic Ser/Thr kinase activity and is exclusively expressed in haploid germ cells, localizing only in their nuclei, and was thus named Haspin (for haploid germ cell-specific nuclear protein kinase). Western blot analysis showed that specific antibodies recognized a protein of M r 83,000 in the testis. Ectopically expressed Haspin was detected exclusively in the nuclei of cultured somatic cells. Even in the absence of kinase activity, however, Haspin caused cell cycle arrest at G 1 , resulting in growth arrest of the transfected somatic cells. In a DNA binding experiment, approximately onehalf of wild-type Haspin was able to bind to a DNAcellulose column, whereas the other half was not. In contrast, all of the deletion mutant Haspin that lacked autophosphorylation bound to the DNA column. Thus, the DNA-binding activity of Haspin may, in some way, be associated with its kinase activity. These observations suggest that Haspin has some critical roles in cell cycle cessation and differentiation of haploid germ cells.

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Expression of Selenoprotein-P Messenger Ribonucleic Acid in the Rat Testis

Cited by 58 publications

References 25 publications

Spatiotemporal expression of the selenoprotein P genein postimplantational mouse embryos

Spatiotemporal expression of the selenoprotein P genein postimplantational mouse embryos

Evidence for expression of relaxin hormone-receptor system in the boar testis

Identification and Characterization of a Haploid Germ Cell-specific Nuclear ProteinKinase (Haspin) in Spermatid Nuclei and Its Effects on Somatic Cells

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