{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T19:17:05Z","timestamp":1790709425616,"version":"4.1.0"},"reference-count":38,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2019,12,25]],"date-time":"2019-12-25T00:00:00Z","timestamp":1577232000000},"content-version":"vor","delay-in-days":7908,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M\u00e9dicale","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004794","name":"Centre National de la Recherche Scientifique","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004794","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100013415","name":"Conseil R\u00e9gional Midi-Pyr\u00e9n\u00e9es","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100013415","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007391","name":"Association pour la Recherche sur le Cancer","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007391","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[1998,5]]},"abstract":"<jats:p>\n                    High endothelial venules (HEVs) are specialized postcapillary venules found in lymphoid organs and chronically inflamed tissues that support high levels of lymphocyte extravasation from the blood. Studies with chlorate, a metabolic inhibitor of sulfation, had previously revealed that production of PAPS (3\u2032\u2010phosphoadenosine\u20105\u2032\u2010phosphosulfate), the high\u2010energy donor of sulfate, is required for sulfation and high\u2010affinity recognition of HEV sialomucins GlyCAM\u20101 and CD34 by the lymphocyte homing receptor L\u2010selectin. Here, we report the molecular characterization of a novel 2.5 kb human cDNA from MECA\u201079\n                    <jats:sup>+<\/jats:sup>\n                    HEV\u2010derived endothelial cells that encodes the target of chlorate, PAPS synthetase, a multifunctional enzyme containing domains for both ATP sulfurylase and adenosine\u20105\u2032\u2010phosphosulfate kinase. Functional expression of the isolated cDNA in Chinese hamster ovary cells results in high levels of PAPS synthesis, which is abolished by treatment of the transfected cells with chlorate. Northern blot analysis reveals a wide tissue distribution of PAPS synthetase mRNA in the human body, suggesting that human PAPS synthetase may be important for sulfation not only of HEV sialomucins, but also of many other molecules, including mucins such as the P\u2010selectin ligand PSGL\u20101, proteoglycans, hormones, neurotransmitters, drugs, and xenobiotics.\n                  <\/jats:p>","DOI":"10.1096\/fasebj.12.7.603","type":"journal-article","created":{"date-parts":[[2018,1,25]],"date-time":"2018-01-25T04:52:29Z","timestamp":1516855949000},"page":"603-612","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":51,"title":["Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase\n                    <sup>1<\/sup>"],"prefix":"10.1096","volume":"12","author":[{"given":"Jean\u2010Philippe","family":"Girard","sequence":"first","affiliation":[{"name":"Laboratoire de Biologie Mol\u00e9culaire Eucaryote du CNRS  31062 Toulouse France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Espen S.","family":"Baekkevold","sequence":"additional","affiliation":[{"name":"LIIPAT, Institute of Pathology University of Oslo  Rikshospitalet Oslo Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francois","family":"Amalric","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Mol\u00e9culaire Eucaryote du CNRS  31062 Toulouse France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,12,25]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(94)90337-9"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.272.5258.60"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-5699(95)80023-9"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/1074-7613(95)90162-0"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.3109\/10739689609148303"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/304030a0"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/1074-7613(94)90076-0"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(92)90612-G"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.7692600"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/366695a0"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V84.8.2554.2554"},{"key":"e_1_2_8_13_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.131.1.261"},{"key":"e_1_2_8_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/361555a0"},{"key":"e_1_2_8_15_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.180.6.2219"},{"key":"e_1_2_8_16_1","first-page":"1688","article-title":"The human peripheral lymph node vascular addressin. An inducible endothelial antigen involved in lymphocyte homing","volume":"143","author":"Michie S. A.","year":"1993","journal-title":"Am. J. Pathol."},{"key":"e_1_2_8_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.20.12035"},{"key":"e_1_2_8_18_1","doi-asserted-by":"crossref","first-page":"7374","DOI":"10.1016\/S0021-9258(18)48247-6","article-title":"Co\u2010purification and characterization of ATP\u2010sulfurylase and adenosine\u20105\u2032\u2010phosphosulfate kinase from rat chondrosarcoma","volume":"262","author":"Geller D. H.","year":"1987","journal-title":"J. Biol. 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