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MeSH Review

Spermatids

 
 
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Disease relevance of Spermatids

 

High impact information on Spermatids

  • Maturation of spermatids is unsynchronized and impaired in seminiferous tubules of Cnot7(-/-) mice [6].
  • The sequential deposition of sperm basic nuclear proteins on chromatin is disrupted, with a specific loss of protamine-2 and prolonged retention of transition protein-2 (Tnp2) in step-15 spermatids [7].
  • Elongating spermatids are not transcriptionally active, raising the possibility that Camk4 has a novel function in male germ cells [7].
  • Deletion of the AZF region is associated with highly variable testicular defects, ranging from complete absence of germ cells to spermatogenic arrest with occasional production of condensed spermatids [8].
  • In males CFTR mRNA is found in the round spermatids (spermatogenic stages V-X) and in the principal cells that line the initial segment of the epididymis [9].
 

Chemical compound and disease context of Spermatids

 

Biological context of Spermatids

  • In contrast, mice of the widely used CD-1 line, which has been selected for large litter size, showed little or no inhibition of spermatid maturation even in response to 16 times as much E2 [12].
  • These results suggest that spe-26 encodes a cytoskeletal protein, perhaps actin binding, which is necessary to segregate the cellular components that form haploid spermatids [13].
  • In adults, the data suggest that Zfy-1 and Zfy-2 transcription is linked to spermatogenesis, that transcription increases with the initiation of meiosis, and that high levels of these mRNAs are found in postmeiotic round spermatid cells [14].
  • Indirect immunofluorescent studies show RHL-2/3-like immunoreactivity on the surface of Sertoli cell, meiotic prophase spermatocytes, spermatids, and epididymal sperm [15].
  • Phosphorylation in spermatids, and probably at fertilization, occurs at repeated -Ser-Pro-X-Basic-motifs in the distinctive N-terminal basic domains of both histones and at the end of the much longer C-terminal domain of H1 [16].
 

Anatomical context of Spermatids

 

Associations of Spermatids with chemical compounds

 

Gene context of Spermatids

 

Analytical, diagnostic and therapeutic context of Spermatids

References

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  4. Delivery of a cyclic adenosine 3',5'-monophosphate response element-binding protein (creb) mutant to seminiferous tubules results in impaired spermatogenesis. Scobey, M., Bertera, S., Somers, J., Watkins, S., Zeleznik, A., Walker, W. Endocrinology (2001) [Pubmed]
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  6. Oligo-astheno-teratozoospermia in mice lacking Cnot7, a regulator of retinoid X receptor beta. Nakamura, T., Yao, R., Ogawa, T., Suzuki, T., Ito, C., Tsunekawa, N., Inoue, K., Ajima, R., Miyasaka, T., Yoshida, Y., Ogura, A., Toshimori, K., Noce, T., Yamamoto, T., Noda, T. Nat. Genet. (2004) [Pubmed]
  7. Spermiogenesis and exchange of basic nuclear proteins are impaired in male germ cells lacking Camk4. Wu, J.Y., Ribar, T.J., Cummings, D.E., Burton, K.A., McKnight, G.S., Means, A.R. Nat. Genet. (2000) [Pubmed]
  8. Diverse spermatogenic defects in humans caused by Y chromosome deletions encompassing a novel RNA-binding protein gene. Reijo, R., Lee, T.Y., Salo, P., Alagappan, R., Brown, L.G., Rosenberg, M., Rozen, S., Jaffe, T., Straus, D., Hovatta, O. Nat. Genet. (1995) [Pubmed]
  9. CFTR expression is regulated during both the cycle of the seminiferous epithelium and the oestrous cycle of rodents. Trezise, A.E., Linder, C.C., Grieger, D., Thompson, E.W., Meunier, H., Griswold, M.D., Buchwald, M. Nat. Genet. (1993) [Pubmed]
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  12. Genetic variation in susceptibility to endocrine disruption by estrogen in mice. Spearow, J.L., Doemeny, P., Sera, R., Leffler, R., Barkley, M. Science (1999) [Pubmed]
  13. The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin. Varkey, J.P., Muhlrad, P.J., Minniti, A.N., Do, B., Ward, S. Genes Dev. (1995) [Pubmed]
  14. The two candidate testis-determining Y genes (Zfy-1 and Zfy-2) are differentially expressed in fetal and adult mouse tissues. Nagamine, C.M., Chan, K., Hake, L.E., Lau, Y.F. Genes Dev. (1990) [Pubmed]
  15. Identification of rat testis galactosyl receptor using antibodies to liver asialoglycoprotein receptor: purification and localization on surfaces of spermatogenic cells and sperm. Abdullah, M., Kierszenbaum, A.L. J. Cell Biol. (1989) [Pubmed]
  16. Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs. Hill, C.S., Rimmer, J.M., Green, B.N., Finch, J.T., Thomas, J.O. EMBO J. (1991) [Pubmed]
  17. Vesicle fusion, pseudopod extension and amoeboid motility are induced in nematode spermatids by the ionophore monensin. Nelson, G.A., Ward, S. Cell (1980) [Pubmed]
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  20. Protamine 3'-untranslated sequences regulate temporal translational control and subcellular localization of growth hormone in spermatids of transgenic mice. Braun, R.E., Peschon, J.J., Behringer, R.R., Brinster, R.L., Palmiter, R.D. Genes Dev. (1989) [Pubmed]
  21. E-MAP-115, encoding a microtubule-associated protein, is a retinoic acid-inducible gene required for spermatogenesis. Komada, M., McLean, D.J., Griswold, M.D., Russell, L.D., Soriano, P. Genes Dev. (2000) [Pubmed]
  22. Histone transition during spermiogenesis is absent in segregation distorter males of Drosophila melanogaster. Kettaneh, N.P., Hartl, D.L. Science (1976) [Pubmed]
  23. The effects of temperature and glucose on protein biosynthesis by immature (round) spermatids from rat testes. Nakamura, M., Romrell, L.J., Hall, P.F. J. Cell Biol. (1978) [Pubmed]
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  25. Male infertility, impaired spermatogenesis, and azoospermia in mice deficient for the pseudophosphatase Sbf1. Firestein, R., Nagy, P.L., Daly, M., Huie, P., Conti, M., Cleary, M.L. J. Clin. Invest. (2002) [Pubmed]
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  27. Absence of the prion protein homologue Doppel causes male sterility. Behrens, A., Genoud, N., Naumann, H., Rülicke, T., Janett, F., Heppner, F.L., Ledermann, B., Aguzzi, A. EMBO J. (2002) [Pubmed]
  28. Premature translation of protamine 1 mRNA causes precocious nuclear condensation and arrests spermatid differentiation in mice. Lee, K., Haugen, H.S., Clegg, C.H., Braun, R.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  29. Protamine transcript sharing among postmeiotic spermatids. Caldwell, K.A., Handel, M.A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  30. Transient expression of the cholecystokinin gene in male germ cells and accumulation of the peptide in the acrosomal granule: possible role of cholecystokinin in fertilization. Persson, H., Rehfeld, J.F., Ericsson, A., Schalling, M., Pelto-Huikko, M., Hökfelt, T. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  31. Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. Ishibashi, K., Kuwahara, M., Gu, Y., Kageyama, Y., Tohsaka, A., Suzuki, F., Marumo, F., Sasaki, S. J. Biol. Chem. (1997) [Pubmed]
  32. Cloning and developmental analysis of murid spermatid-specific thioredoxin-2 (SPTRX-2), a novel sperm fibrous sheath protein and autoantigen. Miranda-Vizuete, A., Tsang, K., Yu, Y., Jiménez, A., Pelto-Huikko, M., Flickinger, C.J., Sutovsky, P., Oko, R. J. Biol. Chem. (2003) [Pubmed]
 
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