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Article: Sphingomyelin synthases and testicular function

TitleSphingomyelin synthases and testicular function
Authors
KeywordsAcrosome formation
Lipid metabolism
Spermatogenesis
Sphingomyelin synthase
Testis
Issue Date2008
PublisherExpert Reviews Ltd. The Journal's web site is located at http://www.future-drugs.com/loi/eem
Citation
Expert Review Of Endocrinology And Metabolism, 2008, v. 3 n. 5, p. 593-601 How to Cite?
AbstractSphingomyelin synthase (SMS) is a cellular enzyme that catalyzes de novo synthesis of sphingomyelin (SM), which is a vital lipid component of cell membranes. Both members of the SMS family, SMS1 and SMS2, are found in mammalian testes and they are located in distinctive subcellular compartments, with SMS1 in the Golgi apparatus and SMS2 in the plasma membrane. At present, the precise function of SMS in the testis remains unknown. Recent studies have demonstrated an unique association of SMS2 with spermatids, particularly near developing acrosomes and the junction restructuring site at the apical ectoplasmic specialization (a testis-specific atypical adherens junction type) and Leydig cells in the rat testis. These data illustrate the possible involvement of SMS2 in spermiogenesis and, perhaps, steroidogenesis in male reproductive function. This review summarizes the latest findings on SMS in the field, particularly its role in testicular function. © 2008 Expert Reviews Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/59987
ISSN
2023 Impact Factor: 2.7
2023 SCImago Journal Rankings: 0.904
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorWong, EWPen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2010-05-31T04:01:27Z-
dc.date.available2010-05-31T04:01:27Z-
dc.date.issued2008en_HK
dc.identifier.citationExpert Review Of Endocrinology And Metabolism, 2008, v. 3 n. 5, p. 593-601en_HK
dc.identifier.issn1744-6651en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59987-
dc.description.abstractSphingomyelin synthase (SMS) is a cellular enzyme that catalyzes de novo synthesis of sphingomyelin (SM), which is a vital lipid component of cell membranes. Both members of the SMS family, SMS1 and SMS2, are found in mammalian testes and they are located in distinctive subcellular compartments, with SMS1 in the Golgi apparatus and SMS2 in the plasma membrane. At present, the precise function of SMS in the testis remains unknown. Recent studies have demonstrated an unique association of SMS2 with spermatids, particularly near developing acrosomes and the junction restructuring site at the apical ectoplasmic specialization (a testis-specific atypical adherens junction type) and Leydig cells in the rat testis. These data illustrate the possible involvement of SMS2 in spermiogenesis and, perhaps, steroidogenesis in male reproductive function. This review summarizes the latest findings on SMS in the field, particularly its role in testicular function. © 2008 Expert Reviews Ltd.en_HK
dc.languageengen_HK
dc.publisherExpert Reviews Ltd. The Journal's web site is located at http://www.future-drugs.com/loi/eemen_HK
dc.relation.ispartofExpert Review of Endocrinology and Metabolismen_HK
dc.subjectAcrosome formationen_HK
dc.subjectLipid metabolismen_HK
dc.subjectSpermatogenesisen_HK
dc.subjectSphingomyelin synthaseen_HK
dc.subjectTestisen_HK
dc.titleSphingomyelin synthases and testicular functionen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1586/17446651.3.5.593en_HK
dc.identifier.scopuseid_2-s2.0-55649110660en_HK
dc.identifier.hkuros165221en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-55649110660&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume3en_HK
dc.identifier.issue5en_HK
dc.identifier.spage593en_HK
dc.identifier.epage601en_HK
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridWong, EWP=23029194700en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK
dc.identifier.citeulike3199512-
dc.identifier.issnl1744-6651-

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