{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T03:59:54Z","timestamp":1790654394525,"version":"4.1.0"},"reference-count":60,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2016,8,15]],"date-time":"2016-08-15T00:00:00Z","timestamp":1471219200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM105724"],"award-info":[{"award-number":["R01 GM105724"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000041","name":"American Diabetes Association","doi-asserted-by":"publisher","award":["7\u201015\u2010MI\u201007"],"award-info":[{"award-number":["7\u201015\u2010MI\u201007"]}],"id":[{"id":"10.13039\/100000041","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2016,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      Cerebroside sulfotransferase (\n                      <jats:styled-content style=\"fixed-case\">CST<\/jats:styled-content>\n                      ) catalyzes the production of sulfatide, a major class of myelin\u2010specific lipids.\n                      <jats:styled-content style=\"fixed-case\">CST<\/jats:styled-content>\n                      knockout (\n                      <jats:styled-content style=\"fixed-case\">CST<\/jats:styled-content>\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      ) mice in which sulfatide is completely depleted are born healthy, but display myelin abnormalities and progressive tremors starting at 4\u20136\u00a0weeks of age. Although these phenotypes suggest that sulfatide plays a critical role in myelin maintenance\/function, the underlying mechanisms remain largely unknown. We analyzed the major\n                      <jats:styled-content style=\"fixed-case\">CNS<\/jats:styled-content>\n                      myelin proteins and the major lipids enriched in the myelin in a spatiotemporal manner. We found a one\u2010third reduction of the major compact myelin proteins (myelin basic protein, myelin basic protein, and proteolipid protein,\n                      <jats:styled-content style=\"fixed-case\">PLP<\/jats:styled-content>\n                      ) and an equivalent post\u2010developmental loss of myelin lipids, providing the molecular basis behind the thinner myelin sheaths. Our lipidomics data demonstrated that the observed global reduction of myelin lipid content was not because of an increase of lipid degradation but rather to the reduction of their synthesis by oligodendrocytes. We also showed that sulfatide depletion leads to region\u2010specific effects on non\u2010compact myelin, dramatically affecting the paranode (neurofascin 155) and the major inner tongue myelin protein (myelin\u2010associated glycoprotein). Moreover, we demonstrated that sulfatide promotes the interaction between adjacent\n                      <jats:styled-content style=\"fixed-case\">PLP<\/jats:styled-content>\n                      extracellular domains, evidenced by a progressive decline of high molecular weight\n                      <jats:styled-content style=\"fixed-case\">PLP<\/jats:styled-content>\n                      complexes in\n                      <jats:styled-content style=\"fixed-case\">CST<\/jats:styled-content>\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice, providing an explanation at a molecular level regarding the uncompacted myelin sheaths. Finally, we proposed that the dramatic losses of neurofascin 155 and\n                      <jats:styled-content style=\"fixed-case\">PLP<\/jats:styled-content>\n                      interactions are responsible for the progressive tremors and eventual ataxia. In summary, we unraveled novel molecular insights into the critical role of sulfatide in myelin maintenance\/function.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                        <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc13738-fig-0008-m.png\">\n                          <jats:alt-text>image<\/jats:alt-text>\n                        <\/jats:graphic>\n                      <\/jats:boxed-text>\n                      Cerebroside sulfotransferase (CST) catalyzes the production of sulfatide, a major class of myelin\u2010specific lipids. CST knockout (CST\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      ) mice in which sulfatide is completely depleted are born healthy, but display myelin abnormalities We show in our study that sulfatide depletion leads to losses of myelin proteins and lipids, and impairment of myelin functions, unraveling novel molecular insights into the critical role of sulfatide in myelin maintenance\/function.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/jnc.13738","type":"journal-article","created":{"date-parts":[[2016,7,14]],"date-time":"2016-07-14T21:36:40Z","timestamp":1468532200000},"page":"40-54","source":"Crossref","is-referenced-by-count":70,"title":["Novel molecular insights into the critical role of sulfatide in myelin maintenance\/function"],"prefix":"10.1111","volume":"139","author":[{"given":"Juan Pablo","family":"Palavicini","sequence":"first","affiliation":[{"name":"Center for Metabolic Origins of Disease Sanford 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