Source:http://linkedlifedata.com/resource/pubmed/id/11466217
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-7-23
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| pubmed:abstractText |
The MSJ-1 gene encodes a murine DnaJ homologue that is expressed specifically in adult testis. DnaJ proteins act as cochaperones of Hsp70 proteins in promoting diverse cellular functions. In this study we used recombinant MSJ-1 proteins to produce MSJ-1 antiserum and to carry out in vitro binding assays. In a wide immunoscreening of mouse tissues, affinity-purified MSJ-1 antibodies recognize a unique protein of 30 kDa in male germ cells only. MSJ-1 is able to interact with the testis-specific Hsp70-2 protein and can be coimmunoprecipitated with Hsp70-2 from spermatogenic cells; binding of these two chaperones is consistent with the presence of a third component, which is so far unknown. MSJ-1 is weakly detected in early round spermatids, and its protein content increases in cytodifferentiating spermatids where it colocalizes with the developing acrosome and their postnuclear region. Hsp70-2, which is known to be highly expressed in meiotic cells, shows a subcellular localization in late differentiating spermatids that overlaps that of MSJ-1. MSJ-1 is also maintained in testicular and epididymal spermatozoa, where it sharply demarcates into two distinct cell areas; the outer surface of the acrosomal vesicle, and the centrosomal area. On the whole, our findings are consistent with a role for MSJ-1 in acrosome formation and centrosome adjustment during spermatid development, whereas its presence in mature spermatozoa suggests a special function during fertilization, shortly afterward, or both.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dnajb3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0006-3363
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
65
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
488-95
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11466217-Aging,
pubmed-meshheading:11466217-Animals,
pubmed-meshheading:11466217-Fluorescent Antibody Technique,
pubmed-meshheading:11466217-HSP40 Heat-Shock Proteins,
pubmed-meshheading:11466217-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11466217-Haploidy,
pubmed-meshheading:11466217-Heat-Shock Proteins,
pubmed-meshheading:11466217-Immunoblotting,
pubmed-meshheading:11466217-Immunohistochemistry,
pubmed-meshheading:11466217-Immunosorbent Techniques,
pubmed-meshheading:11466217-Male,
pubmed-meshheading:11466217-Meiosis,
pubmed-meshheading:11466217-Mice,
pubmed-meshheading:11466217-Microscopy, Confocal,
pubmed-meshheading:11466217-Microscopy, Fluorescence,
pubmed-meshheading:11466217-Spermatids,
pubmed-meshheading:11466217-Spermatozoa,
pubmed-meshheading:11466217-Testis
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| pubmed:year |
2001
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| pubmed:articleTitle |
MSJ-1, a mouse testis-specific DnaJ protein, is highly expressed in haploid male germ cells and interacts with the testis-specific heat shock protein Hsp70-2.
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| pubmed:affiliation |
Department of Biology, University of Milano, 20133 Milano, Italy. giovanni.berruti@unimi.it
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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