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TSGA10 prevents nuclear localization of the hypoxia‐inducible factor (HIF)‐1α

dc.contributor.authorHägele, Sonjaen_US
dc.contributor.authorBehnam, Babaken_US
dc.contributor.authorBorter, Emanuelaen_US
dc.contributor.authorWolfe, Jonathanen_US
dc.contributor.authorPaasch, Uween_US
dc.contributor.authorLukashev, Dmitriyen_US
dc.contributor.authorSitkovsky, Michailen_US
dc.contributor.authorWenger, Roland H.en_US
dc.contributor.authorKatschinski, Dörthe M.en_US
dc.date.accessioned2016-01-04T20:51:50Z
dc.date.available2016-01-04T20:51:50Z
dc.date.issued2006-06-26en_US
dc.identifier.citationHägele, Sonja ; Behnam, Babak; Borter, Emanuela; Wolfe, Jonathan; Paasch, Uwe; Lukashev, Dmitriy; Sitkovsky, Michail; Wenger, Roland H.; Katschinski, Dörthe M. (2006). "TSGA10 prevents nuclear localization of the hypoxiaâ inducible factor (HIF)â 1α." FEBS Letters 580(15): 3731-3738.en_US
dc.identifier.issn0014-5793en_US
dc.identifier.issn1873-3468en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/116345
dc.publisherCache River Pressen_US
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherOxygenen_US
dc.subject.otherProteasomeen_US
dc.subject.otherPAS proteinsen_US
dc.subject.otherGene regulationen_US
dc.subject.otherSperm cellsen_US
dc.subject.otherProlyl hydroxylationen_US
dc.titleTSGA10 prevents nuclear localization of the hypoxia‐inducible factor (HIF)‐1αen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Ophthamology and Visual Sciences, University of Michigan, Ann Arbor, MI 48105, USAen_US
dc.contributor.affiliationotherNew England Inflammation and Tissue Protection Institute, Northeastern University, 360 Huntington Avenue, 113MU Boston, MA 02115, USAen_US
dc.contributor.affiliationotherCell Physiology Group, Martin-Luther University of Halle, Magdeburger Strasse 2, D-06097 Halle, Germanyen_US
dc.contributor.affiliationotherInstitute of Physiology and Center for Integrative Human Physiology (CIHP), University of Zürich, Winterthurerstr. 190, CH-8057 Zürich, Switzerlanden_US
dc.contributor.affiliationotherDepartment of Biology, The Galton Laboratory, University College London, London NW1 2HE, UKen_US
dc.contributor.affiliationotherClinic of Dermatology/Andrology Unit, University of Leipzig, Liebig Strasse 21, D-04103 Leipzig, Germanyen_US
dc.contributor.affiliationotherDepartment of Physiology, Georg-August University of Göttingen, Humboldtallee 23, D-37073 Göttingen, Germanyen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/116345/1/feb2s0014579306006715.pdf
dc.identifier.doi10.1016/j.febslet.2006.05.058en_US
dc.identifier.sourceFEBS Lettersen_US
dc.identifier.citedreferenceM.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72,( 1976 ), 248 – 254.en_US
dc.identifier.citedreferenceJ.P. Dadoune, J.P. Siffroi, M.F. Alfonsi, Transcription in haploid male germ cells. Int. Rev. Cytol., 237,( 2004 ), 1 – 56.en_US
dc.identifier.citedreferenceL.D. Russell, R.A. Ettlin, A.P. Sinha Hikim, E.D. Clegg, Histological and histopathological evaluation of the testis.( 1990 ), Cache River Press Clearwater, FLen_US
dc.identifier.citedreferenceB. Max, This and that: hair pigments, the hypoxic basis of life and the Virgilian journey of the spermatozoon. Trends Pharmacol. Sci., 13,( 1992 ), 272 – 276.en_US
dc.identifier.citedreferenceK. Miki, Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. Proc. Natl. Acad. Sci. USA, 101,( 2004 ), 16501 – 16506.en_US
dc.identifier.citedreferenceWenger, R.H., Stiehl, D.P. and Camenisch, G. (2005) Integration of oxygen signaling at the consensus HRE. Sci STKE 2005, re12.en_US
dc.identifier.citedreferenceT.N. Seagroves, H.E. Ryan, H. Lu, B.G. Wouters, M. Knapp, P. Thibault, K. Laderoute, R.S. Johnson, Transcription factor HIF-1 is a necessary mediator of the pasteur effect in mammalian cells. Mol. Cell Biol., 21,( 2001 ), 3436 – 3444.en_US
dc.identifier.citedreferenceP.H. Maxwell, The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature, 399,( 1999 ), 271 – 275.en_US
dc.identifier.citedreferenceA.C. Epstein, C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell, 107,( 2001 ), 43 – 54.en_US
dc.identifier.citedreferenceM. Ivan, HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O 2 sensing. Science, 292,( 2001 ), 464 – 468.en_US
dc.identifier.citedreferenceP. Jaakkola, Targeting of HIF-α to the von Hippel–Lindau ubiquitylation complex by O 2 -regulated prolyl hydroxylation. Science, 292,( 2001 ), 468 – 472.en_US
dc.identifier.citedreferenceR.H. Wenger, A. Rolfs, H.H. Marti, J.L. Guénet, M. Gassmann, Nucleotide sequence, chromosomal assignment and mRNA expression of mouse hypoxia-inducible factor-1α. Biochem. Biophys. Res. Commun., 223,( 1996 ), 54 – 59.en_US
dc.identifier.citedreferenceR.H. Wenger, A. Rolfs, I. Kvietikova, P. Spielmann, D.R. Zimmermann, M. Gassmann, The mouse gene for hypoxia-inducible factor-1α. Genomic organization, expression and characterization of an alternative first exon and 5′ flanking sequence. Eur. J. Biochem., 246,( 1997 ), 155 – 165.en_US
dc.identifier.citedreferenceR.H. Wenger, A. Rolfs, P. Spielmann, D.R. Zimmermann, M. Gassmann, Mouse hypoxia-inducible factor-1α is encoded by two different mRNA isoforms: expression from a tissue-specific and a housekeeping-type promoter. Blood, 91,( 1998 ), 3471 – 3480.en_US
dc.identifier.citedreferenceA. Görlach, G. Camenisch, I. Kvietikova, L. Vogt, R.H. Wenger, M. Gassmann, Efficient translation of mouse hypoxia-inducible factor-1α under normoxic and hypoxic conditions. Biochim. Biophys. Acta, 1493,( 2000 ), 125 – 134.en_US
dc.identifier.citedreferenceR.H. Wenger, D.M. Katschinski, The hypoxic testis and post-meiotic expression of PAS domain proteins. Semin. Cell. Dev. Biol., 16,( 2005 ), 547 – 553.en_US
dc.identifier.citedreferenceR. Depping, S. Hagele, K.F. Wagner, R.J. Wiesner, G. Camenisch, R.H. Wenger, D.M. Katschinski, A dominant-negative isoform of hypoxia-inducible factor-1α specifically expressed in human testis. Biol. Reprod., 17,( 2004 ), 331 – 339.en_US
dc.identifier.citedreferenceH.H. Marti, D.M. Katschinski, K.F. Wagner, L. Schaffer, B. Stier, R.H. Wenger, Isoform-specific expression of hypoxia-inducible factor-1α during the late stages of mouse spermiogenesis. Mol. Endocrinol., 16,( 2002 ), 234 – 243.en_US
dc.identifier.citedreferenceM.H. Modarressi, B. Behnam, M. Cheng, K.E. Taylor, J. Wolfe, F.A. van der Hoorn, Tsga10 encodes a 65-kilodalton protein that is processed to the 27-kilodalton fibrous sheath protein. Biol. Reprod., 70,( 2004 ), 608 – 615.en_US
dc.identifier.citedreferenceB. Behnam, M.H. Modarressi, V. Conti, K.E. Taylor, A. Puliti, J. Wolfe, Expression of Tsga10 sperm tail protein in embryogenesis and neural development: from cilium to cell division. Biochem. Biophys. Res. Commun., 344,( 2006 ), 1102 – 1110.en_US
dc.identifier.citedreferenceH.E. Ryan, M. Poloni, W. McNulty, D. Elson, M. Gassmann, J.M. Arbeit, R.S. Johnson, Hypoxia-inducible factor-1α is a positive factor in solid tumor growth. Cancer Res., 60,( 2000 ), 4010 – 4015.en_US
dc.identifier.citedreferenceT. Linden, D.M. Katschinski, K. Eckhardt, A. Scheid, H. Pagel, R.H. Wenger, The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis. Faseb J., 17,( 2003 ), 761 – 763.en_US
dc.identifier.citedreferenceE.M. Eddy, K. Toshimori, D.A. O’Brien, Fibrous sheath of mammalian spermatozoa. Microsc. Res. Tech., 61,( 2003 ), 103 – 115.en_US
dc.identifier.citedreferenceK. Nakamura, Rhophilin, a small GTPase Rho-binding protein, is abundantly expressed in the mouse testis and localized in the principal piece of the sperm tail. FEBS Lett., 445,( 1999 ), 9 – 13.en_US
dc.identifier.citedreferenceA. Fujita, K. Nakamura, T. Kato, N. Watanabe, T. Ishizaki, K. Kimura, A. Mizoguchi, S. Narumiya, Ropporin, a sperm-specific binding protein of rhophilin, that is localized in the fibrous sheath of sperm flagella. J. Cell Sci., 113,( 2000 ), 103 – 112.en_US
dc.identifier.citedreferenceH.E. Chemes, Phenotypes of sperm pathology: genetic and acquired forms in infertile men. J. Androl., 21,( 2000 ), 799 – 808.en_US
dc.identifier.citedreferenceJ.C. Luo, M. Shibuya, A variant of nuclear localization signal of bipartite-type is required for the nuclear translocation of hypoxia inducible factors (1α, 2α and 3α). Oncogene, 20,( 2001 ), 1435 – 1444.en_US
dc.identifier.citedreferenceP.J. Kallio, K. Okamoto, S. O’Brien, P. Carrero, Y. Makino, H. Tanaka, L. Poellinger, Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α. EMBO J., 17,( 1998 ), 6573 – 6586.en_US
dc.identifier.citedreferenceD. Chilov, G. Camenisch, I. Kvietikova, U. Ziegler, M. Gassmann, R.H. Wenger, Induction and nuclear translocation of hypoxia-inducible factor-1 (HIF- 1): heterodimerization with ARNT is not necessary for nuclear accumulation of HIF-1α. J. Cell Sci., 112,( 1999 ), 1203 – 1212.en_US
dc.identifier.citedreferenceT. Hofer, I. Desbaillets, G. Hopfl, M. Gassmann, R.H. Wenger, Dissecting hypoxia-dependent and hypoxia-independent steps in the HIF-1α activation cascade: implications for HIF-1alpha gene therapy. Faseb J., 15,( 2001 ), 2715 – 2717.en_US
dc.identifier.citedreferenceJ.D. Powell, R. Elshtein, D.J. Forest, M.A. Palladino, Stimulation of hypoxia-inducible factor-1α (HIF-1α) protein in the adult rat testis following ischemic injury occurs without an increase in HIF-1α messenger RNA expression. Biol. Reprod., 67,( 2002 ), 995 – 1002.en_US
dc.identifier.citedreferenceF. Kilinc, F. Kayaselcuk, C. Aygun, S. Guvel, T. Egilmez, H. Ozkardes, Experimental varicocele induces hypoxia inducible factor-1α, vascular endothelial growth factor expression and angiogenesis in the rat testis. J. Urol., 172,( 2004 ), 1188 – 1191.en_US
dc.identifier.citedreferenceR. Tanaka, Over-expression of the testis-specific gene TSGA10 in cancers and its immunogenicity. Microbiol. Immunol., 48,( 2004 ), 339 – 345.en_US
dc.identifier.citedreferenceS.M. Theinert, M.M. Pronest, K. Peris, W. Sterry, P. Walden, Identification of the testis-specific protein 10 (TSGA10) as serologically defined tumour-associated antigen in primary cutaneous T-cell lymphoma. Br. J. Dermatol., 153,( 2005 ), 639 – 641.en_US
dc.identifier.citedreferenceMobasheri, M.B., Modarressi, M.H., Shabani, M., Asgarian, H., Sharifian, R.A., Vossough, P. and Shokri, F. (2006) Expression of the testis-specific gene, TSGA10, in Iranian patients with acute lymphoblastic leukemia (ALL). Leuk. Res., in press, doi:10.1016/j.leukres.2005.11.012.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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