{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T09:56:00Z","timestamp":1774691760358,"version":"3.50.1"},"reference-count":27,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T00:00:00Z","timestamp":1767744000000},"content-version":"vor","delay-in-days":9,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007449","name":"Takeda Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007449","id-type":"DOI","asserted-by":"publisher"}]},{"name":"JSPS KAKENHI","award":["JP23K06645"],"award-info":[{"award-number":["JP23K06645"]}]},{"DOI":"10.13039\/100009578","name":"Mizutani Foundation for Glycoscience","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009578","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015120","name":"DAIKO FOUNDATION","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100015120","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,12,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Oligosaccharyltransferase (OST), which is a multi-membrane protein complex that catalyzes asparagine-linked glycosylation (N-glycosylation) in the endoplasmic reticulum (ER), is a potential target to eradicate refractory cancer. Mammals express two distinct OST isoforms (OST-A and OST-B) that exhibit different acceptor site specificity to maximize N-glycosylation efficiency; however, the role of individual OST isoforms in tumor progression is not fully understood. Here, using mouse melanoma model, we showed that gene-edited knockout of either one of the OST isoforms did not compromise subcutaneous tumor growth, while their co-expression was required for efficient experimental lung metastasis. We further showed that the cytosolic N-terminal region of Stt3a, which is the catalytic subunit of OST-A, was critical for the N-glycosylation reaction and lung metastasis. This study opens a novel avenue for selective manipulation of OST-A activity, which might offer potential therapeutic strategies for metastatic cancers.<\/jats:p>","DOI":"10.1093\/glycob\/cwag003","type":"journal-article","created":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T12:45:45Z","timestamp":1767789945000},"source":"Crossref","is-referenced-by-count":1,"title":["Functional inactivation of oligosaccharyltransferase a isoform suppresses tumor metastasis"],"prefix":"10.1093","volume":"36","author":[{"given":"Yang","family":"Shi","sequence":"first","affiliation":[{"name":"Department of Glyco-Oncology and Medical Biochemistry, Research Center, Osaka International Cancer Institute, 3-1-69 Otemae, Chuo-ku , Osaka 541-8567 ,","place":["Japan"]},{"name":"Department of Molecular Oncology, Graduate School of Medicine, The University of Osaka, 1-7 Yamada-oka, Suita , Osaka 565-0871 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu","family":"Mizote","sequence":"additional","affiliation":[{"name":"Department of Cancer Immunotherapy, Research Center, Osaka International Cancer Institute, 3-1-69 Otemae, Chuo-ku , Osaka 541-8567 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akinobu","family":"Honda","sequence":"additional","affiliation":[{"name":"Glycometabolic Biochemistry Laboratory, RIKEN Pioneering Research Institute, RIKEN, 2-1 Hirosawa, Wako , Saitama 351-0198 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1030-7631","authenticated-orcid":false,"given":"Tadashi","family":"Suzuki","sequence":"additional","affiliation":[{"name":"Glycometabolic Biochemistry Laboratory, RIKEN Pioneering Research Institute, RIKEN, 2-1 Hirosawa, Wako , Saitama 351-0198 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hideaki","family":"Tahara","sequence":"additional","affiliation":[{"name":"Department of Cancer Immunotherapy, Research Center, Osaka International Cancer Institute , 3-1-69 Otemae, Chuo-ku, Osaka 541-8567 ,","place":["Japan"]},{"name":"Center for Clinical Research, Osaka International Cancer Institute , 3-1-69 Otemae, Chuo-ku, Osaka 541-8567 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoyuki","family":"Taniguchi","sequence":"additional","affiliation":[{"name":"Department of Glyco-Oncology and Medical Biochemistry, Research Center, Osaka International Cancer Institute , 3-1-69 Otemae, Chuo-ku, Osaka 541-8567 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1818-9633","authenticated-orcid":false,"given":"Yoichiro","family":"Harada","sequence":"additional","affiliation":[{"name":"Department of Glyco-Oncology and Medical Biochemistry, Research Center, Osaka International Cancer Institute , 3-1-69 Otemae, Chuo-ku, Osaka 541-8567 ,","place":["Japan"]},{"name":"Department of Molecular Oncology, Graduate School of Medicine, The University of Osaka , 1-7 Yamada-oka, Suita, Osaka 565-0871 ,","place":["Japan"]},{"name":"Institute for Glyco-core Research, Nagoya University, Furo-cho, Chikusa-ku , Nagoya 464-8601 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2026,1,7]]},"reference":[{"key":"2026012614270030500_ref1","doi-asserted-by":"publisher","DOI":"10.3390\/cells13050395","article-title":"Benefits and pitfalls of a glycosylation inhibitor tunicamycin in the therapeutic implication of 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