Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: Presence of arylsulfatase A and sulfogalactosylglycerolipid in mouse ovaries: Localization to the corpus luteum
Authors: Araya Anupriwan
Matthias Schenk
Kessiri Kongmanas
Rapeepun Vanichviriyakit
Daniela Costa Santos
Arman Yaghoubian
Fang Liu
Alexander Wu
Trish Berger
Kym F. Faull
Porncharn Saitongdee
Prapee Sretarugsa
Nongnuj Tanphaichitr
Mahidol University
Mahanakorn University of Technology
Ottawa Hospital Research Institute
University of Ottawa, Canada
Jane & Terry Semel Institute for Neuroscience & Human Behavior
University of California, Davis
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Aug-2008
Citation: Endocrinology. Vol.149, No.8 (2008), 3942-3951
Abstract: Arylsulfatase 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.
ISSN: 00137227
Appears in Collections:Scopus 2006-2010

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.