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Article: Cellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testes

TitleCellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testes
Authors
Issue Date2007
PublisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
Citation
Journal Of Endocrinology, 2007, v. 192 n. 1, p. 17-32 How to Cite?
AbstractSphingomyelin synthase 2 (SMS2) is an enzyme that catalyzes the conversion of phosphatidylcholine and ceramide to sphingomyelin and diacylglycerol, and it is crucial to cellular lipid metabolism. Using the technique of subtraction hybridization, we have isolated a full-length cDNA encoding SMS2 from rat testes, which shared 93 and 87% identity at the nucleotide level with SMS2 in mice and humans respectively. A specific polyclonal antibody was prepared against a 20 amino acid peptide of NH 2-FSWPLSWPPGCFKSSCKKYS-COOH near the C-terminus of SMS2. Studies by RT-PCR and immunoblotting have shown that the expression of SMS2 was limited to late round spermatids and elongating spermatids, but it was not detected in late elongate spermatids and Sertoli cells. Furthermore, SMS2 was shown to associate with the developing acrosome beginning in late round spermatid through elongating spermatids (but not late elongate spermatids) and the cell membrane in studies using fluorescent microscopy and immunohistochemistry. These data were further confirmed by studies using immunogold electron microscopy. The expression of SMS2 in the seminiferous epithelium is stage-specific with its highest expression detected in the acrosome region in late round spermatids from stages VIII-IX, and also in the acrosome in elongating spermatids with diminished intensity in stages X-V; however, it was not found in the acrosome in elongate spermatids in stages VI-VIII. Collectively, these results suggest that SMS2 may play a crucial role in the lipid metabolism in acrosome formation and the plasma membrane restructuring from late round spermatids to early elongating spermatids. © 2007 Society for Endocrinology.
Persistent Identifierhttp://hdl.handle.net/10722/84384
ISSN
2015 Impact Factor: 4.498
2015 SCImago Journal Rankings: 1.910
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorXia, Wen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2010-09-06T08:52:18Z-
dc.date.available2010-09-06T08:52:18Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Endocrinology, 2007, v. 192 n. 1, p. 17-32en_HK
dc.identifier.issn0022-0795en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84384-
dc.description.abstractSphingomyelin synthase 2 (SMS2) is an enzyme that catalyzes the conversion of phosphatidylcholine and ceramide to sphingomyelin and diacylglycerol, and it is crucial to cellular lipid metabolism. Using the technique of subtraction hybridization, we have isolated a full-length cDNA encoding SMS2 from rat testes, which shared 93 and 87% identity at the nucleotide level with SMS2 in mice and humans respectively. A specific polyclonal antibody was prepared against a 20 amino acid peptide of NH 2-FSWPLSWPPGCFKSSCKKYS-COOH near the C-terminus of SMS2. Studies by RT-PCR and immunoblotting have shown that the expression of SMS2 was limited to late round spermatids and elongating spermatids, but it was not detected in late elongate spermatids and Sertoli cells. Furthermore, SMS2 was shown to associate with the developing acrosome beginning in late round spermatid through elongating spermatids (but not late elongate spermatids) and the cell membrane in studies using fluorescent microscopy and immunohistochemistry. These data were further confirmed by studies using immunogold electron microscopy. The expression of SMS2 in the seminiferous epithelium is stage-specific with its highest expression detected in the acrosome region in late round spermatids from stages VIII-IX, and also in the acrosome in elongating spermatids with diminished intensity in stages X-V; however, it was not found in the acrosome in elongate spermatids in stages VI-VIII. Collectively, these results suggest that SMS2 may play a crucial role in the lipid metabolism in acrosome formation and the plasma membrane restructuring from late round spermatids to early elongating spermatids. © 2007 Society for Endocrinology.en_HK
dc.languageengen_HK
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.orgen_HK
dc.relation.ispartofJournal of Endocrinologyen_HK
dc.rightsJournal of Endocrinology. Copyright © Society for Endocrinology.en_HK
dc.titleCellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-0795&volume=192&spage=17&epage=32&date=2007&atitle=Cellular+localization+of+sphingomyelin+synthase+2+in+the+seminiferous+epithelium+of+adult+rat+testesen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1677/JOE-06-0002en_HK
dc.identifier.pmid17210739-
dc.identifier.scopuseid_2-s2.0-33947371349en_HK
dc.identifier.hkuros136469en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33947371349&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume192en_HK
dc.identifier.issue1en_HK
dc.identifier.spage17en_HK
dc.identifier.epage32en_HK
dc.identifier.isiWOS:000244958100003-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridXia, W=8672244100en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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