Presence of Arylsulfatase A and Sulfogalactosylglycerolipid in Mouse Ovaries: Localization to the Corpus Luteum
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...
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| creator | Anupriwan, Araya Schenk, Matthias Kongmanas, Kessiri Vanichviriyakit, Rapeepun Costa Santos, Daniela Yaghoubian, Arman Liu, Fang Wu, Alexander Berger, Trish Faull, Kym F Saitongdee, Porncharn Sretarugsa, Prapee Tanphaichitr, Nongnuj |
| description | 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. |
| doi_str_mv | 10.1210/en.2008-0281 |
| format | Article |
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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.</description><identifier>ISSN: 0013-7227</identifier><identifier>EISSN: 1945-7170</identifier><identifier>DOI: 10.1210/en.2008-0281</identifier><identifier>PMID: 18420734</identifier><identifier>CODEN: ENDOAO</identifier><language>eng</language><publisher>Bethesda, MD: Endocrine Society</publisher><subject>Animals ; Antigens, Surface - metabolism ; Arylsulfatase ; Biological and medical sciences ; Cell adhesion ; Cell adhesion molecules ; Cell surface ; Cerebroside-sulfatase ; Cerebroside-Sulfatase - metabolism ; Corpus luteum ; Corpus Luteum - enzymology ; Corpus Luteum - growth & development ; Corpus Luteum - metabolism ; Endocytosis ; Female ; Fundamental and applied biological sciences. Psychology ; Galactolipids - metabolism ; Immunoblotting ; Immunocytochemistry ; Immunofluorescence ; Ionization ; Lipids ; Localization ; Luteolysis - metabolism ; Lysosomes - metabolism ; Male ; Mass spectrometry ; Mass spectroscopy ; Mice ; Mice, Inbred ICR ; Ovaries ; Ovary - enzymology ; Ovary - metabolism ; Progesterone ; Pseudopregnancy ; Pseudopregnancy - enzymology ; Pseudopregnancy - metabolism ; Silica ; Substrates ; Sulfates - metabolism ; Swine ; Thin layer chromatography ; Tissue Distribution ; Vertebrates: endocrinology</subject><ispartof>Endocrinology (Philadelphia), 2008-08, Vol.149 (8), p.3942-3951</ispartof><rights>Copyright © 2008 by the Endocrine Society 2008</rights><rights>2008 INIST-CNRS</rights><rights>Copyright © 2008 by the Endocrine Society</rights><rights>Copyright © 2008 by The Endocrine Society 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-80037713f27e008a35c3be2a433bc135d1d4b80d4b4436c7b8f1c98dbd4abb653</citedby><cites>FETCH-LOGICAL-c516t-80037713f27e008a35c3be2a433bc135d1d4b80d4b4436c7b8f1c98dbd4abb653</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20527744$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18420734$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anupriwan, Araya</creatorcontrib><creatorcontrib>Schenk, Matthias</creatorcontrib><creatorcontrib>Kongmanas, Kessiri</creatorcontrib><creatorcontrib>Vanichviriyakit, Rapeepun</creatorcontrib><creatorcontrib>Costa Santos, Daniela</creatorcontrib><creatorcontrib>Yaghoubian, Arman</creatorcontrib><creatorcontrib>Liu, Fang</creatorcontrib><creatorcontrib>Wu, Alexander</creatorcontrib><creatorcontrib>Berger, Trish</creatorcontrib><creatorcontrib>Faull, Kym F</creatorcontrib><creatorcontrib>Saitongdee, Porncharn</creatorcontrib><creatorcontrib>Sretarugsa, Prapee</creatorcontrib><creatorcontrib>Tanphaichitr, Nongnuj</creatorcontrib><title>Presence of Arylsulfatase A and Sulfogalactosylglycerolipid in Mouse Ovaries: Localization to the Corpus Luteum</title><title>Endocrinology (Philadelphia)</title><addtitle>Endocrinology</addtitle><description>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.</description><subject>Animals</subject><subject>Antigens, Surface - metabolism</subject><subject>Arylsulfatase</subject><subject>Biological and medical sciences</subject><subject>Cell adhesion</subject><subject>Cell adhesion molecules</subject><subject>Cell surface</subject><subject>Cerebroside-sulfatase</subject><subject>Cerebroside-Sulfatase - metabolism</subject><subject>Corpus luteum</subject><subject>Corpus Luteum - enzymology</subject><subject>Corpus Luteum - growth & development</subject><subject>Corpus Luteum - metabolism</subject><subject>Endocytosis</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactolipids - metabolism</subject><subject>Immunoblotting</subject><subject>Immunocytochemistry</subject><subject>Immunofluorescence</subject><subject>Ionization</subject><subject>Lipids</subject><subject>Localization</subject><subject>Luteolysis - metabolism</subject><subject>Lysosomes - metabolism</subject><subject>Male</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Ovaries</subject><subject>Ovary - enzymology</subject><subject>Ovary - metabolism</subject><subject>Progesterone</subject><subject>Pseudopregnancy</subject><subject>Pseudopregnancy - enzymology</subject><subject>Pseudopregnancy - metabolism</subject><subject>Silica</subject><subject>Substrates</subject><subject>Sulfates - metabolism</subject><subject>Swine</subject><subject>Thin layer chromatography</subject><subject>Tissue Distribution</subject><subject>Vertebrates: endocrinology</subject><issn>0013-7227</issn><issn>1945-7170</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUuLFDEUhYMoTju6cy0BETfWmFd10i6EpvEFLSOo65BK3erJUJ3U5DHQ_nrTdDGjoJuESz7OPScHoeeUXFBGyVvwF4wQ1RCm6AO0oCvRNpJK8hAtCKG8kYzJM_Qkpes6CiH4Y3RGlWBEcrFA4VuEBN4CDgNex8OYyjiYbBLgNTa-x9_rHHZmNDaHdBh348FCDKObXI-dx19DqejlrYkO0ju8DdaM7pfJLnicA85XgDchTiXhbclQ9k_Ro8GMCZ7N9zn6-fHDj83nZnv56ctmvW1sS5e5UYRwKSkfmIQazvDW8g6YEZx3lvK2p73oFKlHDbS0slMDtSvVd70wXbds-Tl6f9KdSreH3oLP0Yx6im5v4kEH4_TfL95d6V241UwoxaisAi9ngRhuCqSsr0OJvnrWnHLSrthypSr15kTZGFKKMNxtoEQf69Hg9bEefayn4i_-dHUPz31U4NUMmFR_cojGW5fuOEZaJqU4cq9PXCjT_1Y280p-IsH3wUbnYaqNp_s0_zT6G3MXtv4</recordid><startdate>20080801</startdate><enddate>20080801</enddate><creator>Anupriwan, Araya</creator><creator>Schenk, Matthias</creator><creator>Kongmanas, Kessiri</creator><creator>Vanichviriyakit, Rapeepun</creator><creator>Costa Santos, Daniela</creator><creator>Yaghoubian, Arman</creator><creator>Liu, Fang</creator><creator>Wu, Alexander</creator><creator>Berger, Trish</creator><creator>Faull, Kym F</creator><creator>Saitongdee, Porncharn</creator><creator>Sretarugsa, Prapee</creator><creator>Tanphaichitr, Nongnuj</creator><general>Endocrine Society</general><general>Oxford University Press</general><general>The Endocrine Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>20080801</creationdate><title>Presence of Arylsulfatase A and Sulfogalactosylglycerolipid in Mouse Ovaries: Localization to the Corpus Luteum</title><author>Anupriwan, Araya ; Schenk, Matthias ; Kongmanas, Kessiri ; Vanichviriyakit, Rapeepun ; Costa Santos, Daniela ; Yaghoubian, Arman ; Liu, Fang ; Wu, Alexander ; Berger, Trish ; Faull, Kym F ; Saitongdee, Porncharn ; Sretarugsa, Prapee ; Tanphaichitr, Nongnuj</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-80037713f27e008a35c3be2a433bc135d1d4b80d4b4436c7b8f1c98dbd4abb653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Antigens, Surface - metabolism</topic><topic>Arylsulfatase</topic><topic>Biological and medical sciences</topic><topic>Cell adhesion</topic><topic>Cell adhesion molecules</topic><topic>Cell surface</topic><topic>Cerebroside-sulfatase</topic><topic>Cerebroside-Sulfatase - metabolism</topic><topic>Corpus luteum</topic><topic>Corpus Luteum - enzymology</topic><topic>Corpus Luteum - growth & development</topic><topic>Corpus Luteum - metabolism</topic><topic>Endocytosis</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactolipids - metabolism</topic><topic>Immunoblotting</topic><topic>Immunocytochemistry</topic><topic>Immunofluorescence</topic><topic>Ionization</topic><topic>Lipids</topic><topic>Localization</topic><topic>Luteolysis - metabolism</topic><topic>Lysosomes - metabolism</topic><topic>Male</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Ovaries</topic><topic>Ovary - enzymology</topic><topic>Ovary - metabolism</topic><topic>Progesterone</topic><topic>Pseudopregnancy</topic><topic>Pseudopregnancy - enzymology</topic><topic>Pseudopregnancy - metabolism</topic><topic>Silica</topic><topic>Substrates</topic><topic>Sulfates - metabolism</topic><topic>Swine</topic><topic>Thin layer chromatography</topic><topic>Tissue Distribution</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anupriwan, Araya</creatorcontrib><creatorcontrib>Schenk, Matthias</creatorcontrib><creatorcontrib>Kongmanas, Kessiri</creatorcontrib><creatorcontrib>Vanichviriyakit, Rapeepun</creatorcontrib><creatorcontrib>Costa Santos, Daniela</creatorcontrib><creatorcontrib>Yaghoubian, Arman</creatorcontrib><creatorcontrib>Liu, Fang</creatorcontrib><creatorcontrib>Wu, Alexander</creatorcontrib><creatorcontrib>Berger, Trish</creatorcontrib><creatorcontrib>Faull, Kym F</creatorcontrib><creatorcontrib>Saitongdee, Porncharn</creatorcontrib><creatorcontrib>Sretarugsa, Prapee</creatorcontrib><creatorcontrib>Tanphaichitr, Nongnuj</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Endocrinology (Philadelphia)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anupriwan, Araya</au><au>Schenk, Matthias</au><au>Kongmanas, Kessiri</au><au>Vanichviriyakit, Rapeepun</au><au>Costa Santos, Daniela</au><au>Yaghoubian, Arman</au><au>Liu, Fang</au><au>Wu, Alexander</au><au>Berger, Trish</au><au>Faull, Kym F</au><au>Saitongdee, Porncharn</au><au>Sretarugsa, Prapee</au><au>Tanphaichitr, Nongnuj</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Presence of Arylsulfatase A and Sulfogalactosylglycerolipid in Mouse Ovaries: Localization to the Corpus Luteum</atitle><jtitle>Endocrinology (Philadelphia)</jtitle><addtitle>Endocrinology</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>149</volume><issue>8</issue><spage>3942</spage><epage>3951</epage><pages>3942-3951</pages><issn>0013-7227</issn><eissn>1945-7170</eissn><coden>ENDOAO</coden><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.</abstract><cop>Bethesda, MD</cop><pub>Endocrine Society</pub><pmid>18420734</pmid><doi>10.1210/en.2008-0281</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Endocrinology (Philadelphia), 2008-08, Vol.149 (8), p.3942-3951 |
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| subjects | Animals Antigens, Surface - metabolism Arylsulfatase Biological and medical sciences Cell adhesion Cell adhesion molecules Cell surface Cerebroside-sulfatase Cerebroside-Sulfatase - metabolism Corpus luteum Corpus Luteum - enzymology Corpus Luteum - growth & development Corpus Luteum - metabolism Endocytosis Female Fundamental and applied biological sciences. Psychology Galactolipids - metabolism Immunoblotting Immunocytochemistry Immunofluorescence Ionization Lipids Localization Luteolysis - metabolism Lysosomes - metabolism Male Mass spectrometry Mass spectroscopy Mice Mice, Inbred ICR Ovaries Ovary - enzymology Ovary - metabolism Progesterone Pseudopregnancy Pseudopregnancy - enzymology Pseudopregnancy - metabolism Silica Substrates Sulfates - metabolism Swine Thin layer chromatography Tissue Distribution Vertebrates: endocrinology |
| title | Presence of Arylsulfatase A and Sulfogalactosylglycerolipid in Mouse Ovaries: Localization to the Corpus Luteum |
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