Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa

35 páginas, 8 figuras.

Detalles Bibliográficos
Autores: Miranda-Vizuete, Antonio, Ljung, Johanna, Damdimopoulos, Anastasios E., Gustafsson, Jan-Åke, Oko, Richard, Pelto-Huikko, Markku, Spyrou, Giannis
Tipo de recurso: artículo
Fecha de publicación:2001
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/47441
Acceso en línea:http://hdl.handle.net/10261/47441
Access Level:acceso abierto
Palabra clave:Amino acid sequence
Chromosomes
Immunohistochemistry
Membrane proteins
Recombinant protein
Spermatozoa
Thioredoxin
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spelling Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human SpermatozoaMiranda-Vizuete, AntonioLjung, JohannaDamdimopoulos, Anastasios E.Gustafsson, Jan-ÅkeOko, RichardPelto-Huikko, MarkkuSpyrou, GiannisAmino acid sequenceChromosomesImmunohistochemistryMembrane proteinsRecombinant proteinSpermatozoaThioredoxin35 páginas, 8 figuras.Thioredoxins (Trx) are small ubiquitous proteins that participate in different cellular processes via redox-mediated reactions. We report here the identification and characterization of a novel member of the thioredoxin family in humans, named Sptrx (sperm-specific trx), the first with a tissue-specific distribution, located exclusively in spermatozoa. Sptrx open reading frame encodes for a protein of 486 amino acids composed of two clear domains: an N-terminal domain consisting of 23 highly conserved repetitions of a 15-residue motif and a C-terminal domain typical of thioredoxins. Northern analysis and in situ hybridization shows that Sptrx mRNA is only expressed in human testis, specifically in round and elongating spermatids. Immunostaining of human testis sections identified Sptrx protein in spermatids, while immunofluorescence and immunogold electron microscopy analysis demonstrated Sptrx localization in the cytoplasmic droplet of ejaculated sperm. Sptrx appears to have a multimeric structure in native conditions and is able to reduce insulin disulfide bonds in the presence of NADPH and thioredoxin reductase. During mammalian spermiogenesis in testis seminiferous tubules and later maturation in epididymis, extensive reorganization of disulfide bonds is required to stabilize cytoskeletal sperm structures. However, the molecular mechanisms that control these processes are not known. The identification of Sptrx with an expression pattern restricted to the postmeiotic phase of spermatogenesis, when the sperm tail is organized, suggests that Sptrx might be an important factor in regulating critical steps of human spermiogenesis.This work was supported by grants from the Swedish Medical Research Council (Projects 03P-14096-01A, 03X-14041-01A, and 13X-10370), the Åke Wibergs Stiftelse, the Karolinska Institutet, the Södertörns Högskola, the Marie Curie Research Training Grants (contract ERBFMBICT972824), the Medical Research Fund of Tampere University Hospital, and Natural Sciences and Engineering Research Council of Canada (to R. O.).Peer reviewedAmerican Society for Biochemistry and Molecular Biology201220122001info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/47441reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1074/jbc.M101760200info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/474412026-05-22T06:33:51Z
dc.title.none.fl_str_mv Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
title Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
spellingShingle Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
Miranda-Vizuete, Antonio
Amino acid sequence
Chromosomes
Immunohistochemistry
Membrane proteins
Recombinant protein
Spermatozoa
Thioredoxin
title_short Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
title_full Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
title_fullStr Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
title_full_unstemmed Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
title_sort Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa
dc.creator.none.fl_str_mv Miranda-Vizuete, Antonio
Ljung, Johanna
Damdimopoulos, Anastasios E.
Gustafsson, Jan-Åke
Oko, Richard
Pelto-Huikko, Markku
Spyrou, Giannis
author Miranda-Vizuete, Antonio
author_facet Miranda-Vizuete, Antonio
Ljung, Johanna
Damdimopoulos, Anastasios E.
Gustafsson, Jan-Åke
Oko, Richard
Pelto-Huikko, Markku
Spyrou, Giannis
author_role author
author2 Ljung, Johanna
Damdimopoulos, Anastasios E.
Gustafsson, Jan-Åke
Oko, Richard
Pelto-Huikko, Markku
Spyrou, Giannis
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Amino acid sequence
Chromosomes
Immunohistochemistry
Membrane proteins
Recombinant protein
Spermatozoa
Thioredoxin
topic Amino acid sequence
Chromosomes
Immunohistochemistry
Membrane proteins
Recombinant protein
Spermatozoa
Thioredoxin
description 35 páginas, 8 figuras.
publishDate 2001
dc.date.none.fl_str_mv 2001
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/47441
url http://hdl.handle.net/10261/47441
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1074/jbc.M101760200
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869425293500874752
score 15.811543

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