Linked Life Data

15014887

Source:http://linkedlifedata.com/resource/pubmed/id/15014887

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-6-2
pubmed:abstractText
hSMP-1 is a human sperm membrane protein expressed during development. It is a testis-specific component produced during male germ cell differentiation. Proteins that interact with hSMP-1 were identified by the application of the yeast two-hybrid system. One of the components, RanBPM, was found to be associated with hSMP-1 under both in vitro and in vivo conditions. In the human testis, RanBPM is produced in spermatogonia and primary spermatocytes, suggesting expression during the early stages of spermatogenesis; whereas in the rat testis, it is located in round and elongated spermatids, similar to hSMP-1, suggesting expression of both components during spermiogenesis. Images obtained by immunofluorescence and confocal scanning microscopy of CHO-K1 cells co-transfected with pEGFP-C1-hSMP-1 and pDsRed1-Nl-RanBPM revealed that RanBPM and hSMP-1 are distributed in discrete loci throughout the cytoplasm. When superimposed, the stained spots appeared as congruent yellow areas, indicative of co-localization and probable complex formation of these two components. This interaction between hSMP-1 and RanBPM may be involved in the process of male germ cell differentiation. In CHO-Kl cells transfected with pEGFP-Cl-hSMP-1, the exogenously expressed hSMP-1 was found to co-localize with alpha-tubulin. Depolymerization of microtubules can be induced in CHO-Kl cells by cold treatment. In cells transfected with the pEGFP-Cl vector, the dispersed tubulins promptly reassembled upon warming. However, in cells transfected with pEGFP-Cl-hSMP-1, reassembly of the dispersed tubulins was blocked even upon rewarming of the cells. These findings suggest that hSMP-1 interacts with tubulins and thereby may modulate microtubule assembly and/or activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0946-2716
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Springer-Verlag
pubmed:issnType
Print
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
383-8
pubmed:dateRevised
2011-7-8
pubmed:meshHeading
pubmed-meshheading:15014887-Adaptor Proteins, Signal Transducing, pubmed-meshheading:15014887-Animals, pubmed-meshheading:15014887-Antigens, Surface, pubmed-meshheading:15014887-CHO Cells, pubmed-meshheading:15014887-Cloning, Molecular, pubmed-meshheading:15014887-Cricetinae, pubmed-meshheading:15014887-Cytoskeletal Proteins, pubmed-meshheading:15014887-Gene Expression Regulation, Developmental, pubmed-meshheading:15014887-Gene Library, pubmed-meshheading:15014887-HeLa Cells, pubmed-meshheading:15014887-Humans, pubmed-meshheading:15014887-Immunohistochemistry, pubmed-meshheading:15014887-Male, pubmed-meshheading:15014887-Membrane Proteins, pubmed-meshheading:15014887-Microtubule-Organizing Center, pubmed-meshheading:15014887-Nuclear Proteins, pubmed-meshheading:15014887-Precipitin Tests, pubmed-meshheading:15014887-Rats, pubmed-meshheading:15014887-Spermatogenesis, pubmed-meshheading:15014887-Spermatozoa, pubmed-meshheading:15014887-Testis, pubmed-meshheading:15014887-ran GTP-Binding Protein
pubmed:year
2004
pubmed:articleTitle
Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre.
pubmed:affiliation
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, 5 Dong Dan San Tiao, 100005 Beijing, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't