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In addition to modulated levels of mucin gene transcription, translational and post-translational biosynthetic processes also exert significant influence upon mucin function. Mucins are massive macromolecules with numerous functional domains that contribute to their structural composition and biophysical properties. Single MUC5AC and MUC5B apoproteins have molecular masses of &amp;gt;400\u2005kDa, and von Willebrand factor D-like as well as other cysteine-rich domain segments contribute to mucin polymerization and flexibility, thus increasing apoprotein length and complexity. Additional domains serve as sites for O-glycosylation, which increase further mucin mass several-fold. Glycosylation is a defining process for mucins that is specific with respect to additions of glycans to mucin apoprotein backbones, and glycan additions influence the physical properties of the mucins via structural modifications as well as charge interactions. Ultimately, through their tight regulation and complex assembly, airway mucins follow the biological rule of \u2018form fits function\u2019 in that their structural organization influences their role in lung homeostatic mechanisms.<\/jats:p>","DOI":"10.1042\/bst20170455","type":"journal-article","created":{"date-parts":[[2018,5,25]],"date-time":"2018-05-25T06:15:23Z","timestamp":1527228923000},"page":"707-719","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":61,"title":["Role of mucins in lung homeostasis: regulated expression and biosynthesis in health and disease"],"prefix":"10.1042","volume":"46","author":[{"given":"Breanna A.","family":"Symmes","sequence":"first","affiliation":[{"name":"Division of Pulmonary Sciences and Critical Care Medicine, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adrianne L.","family":"Stefanski","sequence":"additional","affiliation":[{"name":"Division of Pulmonary Sciences and Critical Care Medicine, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chelsea M.","family":"Magin","sequence":"additional","affiliation":[{"name":"Division of Pulmonary Sciences and Critical Care Medicine, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."},{"name":"Department of Bioengineering, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5600-7314","authenticated-orcid":false,"given":"Christopher M.","family":"Evans","sequence":"additional","affiliation":[{"name":"Division of Pulmonary Sciences and Critical Care Medicine, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."},{"name":"Department of Immunology, University of Colorado Denver School of Medicine, 12700 E. 19th Avenue, Aurora, CO 80045, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2018,5,25]]},"reference":[{"key":"2021111818063083900_BST-2017-0455CC1","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1172\/JCI15217","article-title":"Mucus clearance as a primary innate defense mechanism for mammalian airways","volume":"109","author":"Knowles","year":"2002","journal-title":"J. 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