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dc.contributor.authorAraya Anupriwanen_US
dc.contributor.authorMatthias Schenken_US
dc.contributor.authorKessiri Kongmanasen_US
dc.contributor.authorRapeepun Vanichviriyakiten_US
dc.contributor.authorDaniela Costa Santosen_US
dc.contributor.authorArman Yaghoubianen_US
dc.contributor.authorFang Liuen_US
dc.contributor.authorAlexander Wuen_US
dc.contributor.authorTrish Bergeren_US
dc.contributor.authorKym F. Faullen_US
dc.contributor.authorPorncharn Saitongdeeen_US
dc.contributor.authorPrapee Sretarugsaen_US
dc.contributor.authorNongnuj Tanphaichitren_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherMahanakorn University of Technologyen_US
dc.contributor.otherOttawa Hospital Research Instituteen_US
dc.contributor.otherUniversity of Ottawa, Canadaen_US
dc.contributor.otherJane & Terry Semel Institute for Neuroscience & Human Behavioren_US
dc.contributor.otherUniversity of California, Davisen_US
dc.identifier.citationEndocrinology. Vol.149, No.8 (2008), 3942-3951en_US
dc.description.abstractArylsulfatase A (AS-A) is a lysosomal enzyme, which catalyzes the desulfation of certain sulfogalactolipids, including sulfogalactosylglycerolipid (SGG), a molecule implicated in cell adhesion. In this report, immunocytochemistry revealed the selective presence of AS-A in the corpus luteum of mouse ovaries. Immunoblotting indicated that mouse corpus luteum AS-A had a molecular mass of 66 kDa, similar to AS-A of other tissues. Corpus luteum AS-A was active, capable of desulfating the artificial substrate, p-nitrocatechol sulfate, at the optimum pH of five. To understand further the role of AS-A in female reproduction, levels of AS-A were determined during corpus luteum development in pseudopregnant mice and during luteolysis after cessation of pseudopregnancy. Immunocytochemistry, immunoblotting and desulfation activity showed that AS-A expression was evident at the onset of pseudopregnancy in the newly formed corpora lutea, and its level increased steadily during gland development. The increase in the expression and activity of AS-A continued throughout luteolysis after the decrease in serum progesterone levels. We also observed the selective presence of SGG on the luteal cell surface in developed corpora lutea, as shown by immunofluorescence of mouse ovary sections as well as high-performance thin-layer chromatography of lipids isolated from mouse and pig corpora lutea. The identity of the "SGG" band on the thin layer silica plate was further validated by electrospray ionization mass spectrometry. Significantly, SGG disappeared in regressing corpora lutea. Therefore, lysosomal AS-A may be involved in cell-surface remodeling during luteolysis by desulfating SGG after its endocytosis and targeting to the lysosome. Copyright © 2008 by The Endocrine Society.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titlePresence of arylsulfatase A and sulfogalactosylglycerolipid in mouse ovaries: Localization to the corpus luteumen_US
Appears in Collections:Scopus 2006-2010

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