Presence of arylsulfatase A and sulfogalactosylglycerolipid in mouse ovaries: Localization to the corpus luteum

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

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3942-3951
Number of pages10
JournalEndocrinology
Volume149
Issue number8
DOIs
Publication statusPublished - Aug 2008
Externally publishedYes

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

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