{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T02:04:20Z","timestamp":1789524260892,"version":"build-2803163510"},"reference-count":132,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,5,19]],"date-time":"2026-05-19T00:00:00Z","timestamp":1779148800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,5,19]],"date-time":"2026-05-19T00:00:00Z","timestamp":1779148800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["HL 161094"],"award-info":[{"award-number":["HL 161094"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008065","name":"Georgia Research Alliance","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["anatomypubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Developmental Dynamics"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>\n                      Fibrillins provide a scaffold for elastic fiber formation, which enables lung recoil and aortic compliance. Abnormal fibrillin microfibrils, as in Marfan syndrome, lead to enlarged alveoli, vascular stiffening, and aneurysms. Our earlier studies suggested that fibrillin function depends on\n                      <jats:italic>O<\/jats:italic>\n                      \u2010glucosylation of its epidermal growth factor (EGF)\u2010like repeats by protein\n                      <jats:italic>O<\/jats:italic>\n                      \u2010glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3). Mice lacking both enzymes (\n                      <jats:italic>Poglut2\/3 DKO<\/jats:italic>\n                      ) die soon after birth. Rare survivors are runted, have digit 2\u20133 syndactyly, and variable eye defects. Here, we wanted to determine whether\n                      <jats:italic>O\u2010<\/jats:italic>\n                      glucosylation was important for fibrillin organization\/function during lung and aorta development.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Fibrillin microfibrils and elastic fibrils were reduced and disorganized in the\n                      <jats:italic>Poglut2\/3 DKO<\/jats:italic>\n                      lung and aorta. In the lung, loss of\n                      <jats:italic>O<\/jats:italic>\n                      \u2010glucosylation impaired airway branching, delayed sacculation, and postnatally caused mildly enlarged alveolar airspaces and reduced lipofibroblasts and capillary endothelial cells. In the ascending aorta, the\n                      <jats:italic>Poglut2\/3 DKO<\/jats:italic>\n                      led to disorganized smooth muscle layers with increased nuclear YAP, potentially indicating a change in matrix stiffness.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>\n                      The lung and aorta defects in\n                      <jats:italic>Poglut2\/3 DKO<\/jats:italic>\n                      resembled mouse\n                      <jats:italic>Fbn1<\/jats:italic>\n                      and\n                      <jats:italic>Ltbp<\/jats:italic>\n                      mutant models, suggesting a common microfibril\u2010driven mechanism. Future studies should examine how loss of fibrillin\n                      <jats:italic>O<\/jats:italic>\n                      \u2010glucosylation affects microfibril\u2010dependent regulation of TGF\u2010\u03b2 and BMP signaling and matrix biomechanics.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/dvdy.70148","type":"journal-article","created":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T04:19:58Z","timestamp":1779250798000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Loss of\n                    <scp>POGLUT2<\/scp>\n                    \/3\u2010mediated\n                    <i>O<\/i>\n                    \u2010glucosylation produces lung and aortic phenotypes reminiscent of fibrillin1 mutants"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2051-9865","authenticated-orcid":false,"given":"Sanjiv","family":"Neupane","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Cell Biology Stony Brook University  Stony Brook New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-5612-936X","authenticated-orcid":false,"given":"Angelina","family":"Almiroudis","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Cell Biology Stony Brook University  Stony Brook New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-4399-1741","authenticated-orcid":false,"given":"Kaitlyn E.","family":"Donnelly","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Cell Biology Stony Brook University  Stony Brook New York 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