{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,10]],"date-time":"2025-11-10T17:13:51Z","timestamp":1762794831553,"version":"build-2065373602"},"reference-count":43,"publisher":"Wiley","issue":"21","license":[{"start":{"date-parts":[[2025,8,6]],"date-time":"2025-08-06T00:00:00Z","timestamp":1754438400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["24K09368"],"award-info":[{"award-number":["24K09368"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2025,11]]},"abstract":"<jats:p>\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylation is a protein glycosylation that regulates the functions of target proteins. Although it has been reported that a disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAMTS1), an important spermatogenesis factor, is\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylated, the roles of\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylation in ADAMTS1 in testicular cells are still unclear. In this study, we found that ADAMTS1 is\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylated at Trp\n                    <jats:sup>562<\/jats:sup>\n                    and Trp\n                    <jats:sup>565<\/jats:sup>\n                    in testis germ NEC8 cells. To determine the roles of\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylation in ADAMTS1, we established cells expressing a\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylation\u2010defective ADAMTS1, in which\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylated tryptophan residues were replaced with phenylalanine residues (ADAMTS1\/2WF). Processing and secretion of ADAMTS1\/2WF were both inhibited compared to those of wild\u2010type. Moreover, wild\u2010type ADAMTS1 degraded aggrecan, whereas ADAMTS1\/2WF could not. These results indicate the impact of\n                    <jats:italic>C<\/jats:italic>\n                    \u2010mannosylation on ADAMTS1 function.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70133","type":"journal-article","created":{"date-parts":[[2025,8,6]],"date-time":"2025-08-06T17:53:16Z","timestamp":1754502796000},"page":"3113-3123","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["<i>C<\/i>\n                    \u2010mannosylation promotes\n                    <scp>ADAMTS1<\/scp>\n                    activation and secretion in human testicular germ cell tumor\n                    <scp>NEC8<\/scp>\n                    cells"],"prefix":"10.1002","volume":"599","author":[{"given":"Takato","family":"Kobayashi","sequence":"first","affiliation":[{"name":"Department of Applied Chemistry Faculty of Science and Technology, Keio University  Yokohama 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