Source:http://linkedlifedata.com/resource/pubmed/id/15181017
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
2004-8-9
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pubmed:databankReference | |
pubmed:abstractText |
Mammalian germ cells are endowed with a complete set of thioredoxins (Trx), a class of redox proteins located in specific structures of the spermatid and sperm tail. We report here the characterization, under normal and pathological conditions, of a novel thioredoxin with a germ line-restricted expression pattern, named spermatocyte/spermatid-specific thioredoxin-3 (SPTRX-3). The human SPTRX-3 gene maps at 9q32, only 50 kb downstream from the TRX-1 gene from which it probably originated as genomic duplication. Therefore, human SPTRX-3 protein comprises a unique thioredoxin domain displaying high homology with the ubiquitously expressed TRX-1. Among the tissues investigated, Sptrx-3 mRNA is found exclusively in the male germ cells at pachytene spermatocyte and round spermatid stages. Light and electron microscopy show SPTRX-3 protein to be predominately located in the Golgi apparatus of pachytene spermatocytes and round and elongated spermatids, with a transient localization in the developing acrosome of round spermatids. In addition, increased levels of SPTRX-3, possibly caused by overexpression, are observed in morphologically abnormal human spermatozoa from infertile men. In addition, SPTRX-3 is identified as a novel postobstruction autoantigen. In this report, we propose that SPTRX-3 can be used as a specific marker for diverse sperm and testis pathologies. SPTRX-3 is the first thioredoxin specific to the Golgi apparatus, and its function within this organelle might be related to the post-translational modification of proteins required for germ cell-specific functions, such as acrosomal biogenesis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34971-82
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15181017-Acrosome Reaction,
pubmed-meshheading:15181017-Amino Acid Sequence,
pubmed-meshheading:15181017-Animals,
pubmed-meshheading:15181017-Blotting, Northern,
pubmed-meshheading:15181017-Blotting, Western,
pubmed-meshheading:15181017-Cloning, Molecular,
pubmed-meshheading:15181017-DNA, Complementary,
pubmed-meshheading:15181017-Eukaryotic Cells,
pubmed-meshheading:15181017-Flow Cytometry,
pubmed-meshheading:15181017-Gene Library,
pubmed-meshheading:15181017-Genetic Variation,
pubmed-meshheading:15181017-Golgi Apparatus,
pubmed-meshheading:15181017-Humans,
pubmed-meshheading:15181017-Immunoblotting,
pubmed-meshheading:15181017-Immunohistochemistry,
pubmed-meshheading:15181017-In Situ Hybridization,
pubmed-meshheading:15181017-Male,
pubmed-meshheading:15181017-Mice,
pubmed-meshheading:15181017-Microscopy, Electron,
pubmed-meshheading:15181017-Microscopy, Fluorescence,
pubmed-meshheading:15181017-Molecular Sequence Data,
pubmed-meshheading:15181017-Open Reading Frames,
pubmed-meshheading:15181017-RNA, Messenger,
pubmed-meshheading:15181017-Rats,
pubmed-meshheading:15181017-Sequence Homology, Amino Acid,
pubmed-meshheading:15181017-Spermatids,
pubmed-meshheading:15181017-Spermatocytes,
pubmed-meshheading:15181017-Spermatogenesis,
pubmed-meshheading:15181017-Thioredoxins,
pubmed-meshheading:15181017-Tissue Distribution,
pubmed-meshheading:15181017-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Spermatocyte/spermatid-specific thioredoxin-3, a novel Golgi apparatus-associated thioredoxin, is a specific marker of aberrant spermatogenesis.
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pubmed:affiliation |
Center for Biotechnology, Department of Biosciences at NOVUM, Karolinska Institutet, S-14157 Huddinge, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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