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Submitted on February 28, 2008
Accepted on March 31, 2008
Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand; Department of Anatomy, Faculty of Veterinary Medicine, Mahanakorn University of Technology, Bangkok, Thailand; Chronic Disease Program, Ottawa Health Research Institute, Ottawa, ON, Canada; Department of Biochemistry/Microbiology/Immunology, University of Ottawa, Ottawa, ON, Canada; Pasarow Mass Spectrometry Laboratory, Department of Psychiatry and Biobehavioral Sciences and the Semel-Neuropsychiatric Institute for Neuroscience and Human Behavior, University of California Los Angeles, Los Angeles, CA, U.S.A.; Department of Animal Science, University of California Davis, Davis, CA, U.S.A.; Department of Obstetrics/Gynecology, University of Ottawa, Ottawa, ON, Canada
* To whom correspondence should be addressed. E-mail: ntanphaichitr{at}ohri.ca.
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 5. To further understand 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 rose steadily during gland development. The increase in the expression and activity of AS-A continued throughout luteolysis following 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 following its endocytosis and targeting to the lysosome.
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