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Additionally, <jats:italic>ECM1<\/jats:italic> gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is not established. Here, we showed that <jats:italic>ECM1<\/jats:italic> gene mutation observed in LP patients significantly suppresses its secretion. As ECM1 has three putative <jats:italic>N<\/jats:italic>\u2010glycosylation sites and most of mutated ECM1 observed in LP patients are defective in these <jats:italic>N<\/jats:italic>\u2010glycosylation sites, we investigated the correlation between LP and <jats:italic>N<\/jats:italic>\u2010glycosylation of ECM1. We identified that the Asn<jats:sup>354<\/jats:sup> and Asn<jats:sup>444<\/jats:sup> residues in ECM1 were <jats:italic>N<\/jats:italic>\u2010glycosylated by mass spectrometry analysis. In addition, an <jats:italic>N<\/jats:italic>\u2010linked glycan at Asn<jats:sup>354<\/jats:sup> negatively regulated secretion of ECM1, contrary to LP patient\u2010derived mutants. These results indicate that the defect of <jats:italic>N<\/jats:italic>\u2010glycosylation in ECM1 is not involved in the aberration of secretion of LP\u2010derived mutated ECM1.<\/jats:p>","DOI":"10.1016\/j.fob.2014.10.004","type":"journal-article","created":{"date-parts":[[2014,10,12]],"date-time":"2014-10-12T14:03:57Z","timestamp":1413122637000},"page":"879-885","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["<i>N<\/i>\u2010Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid 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