Title: Respiratory Tract Mucins: Structure and Expression Patterns
Abstract: Respiratory Tract Mucins: Structure and Expression Patterns Julia R. Davies, Julia R. Davies Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorAnnkatrin Herrmann, Annkatrin Herrmann Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorWayne Russell, Wayne Russell Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorNaila Svitacheva, Naila Svitacheva Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorClaes Wickström, Claes Wickström Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorIngemar Carlstedt, Ingemar Carlstedt Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, Sweden This paper was presented at the symposium by Ingemar Carlstedt, to whom correspondence should be addressed.Search for more papers by this author Julia R. Davies, Julia R. Davies Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorAnnkatrin Herrmann, Annkatrin Herrmann Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorWayne Russell, Wayne Russell Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorNaila Svitacheva, Naila Svitacheva Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorClaes Wickström, Claes Wickström Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, SwedenSearch for more papers by this authorIngemar Carlstedt, Ingemar Carlstedt Mucosal Biology Group, Department of Cell and Molecular Biology, Lund University, BMC, C13, S-221 84, Lund, Sweden This paper was presented at the symposium by Ingemar Carlstedt, to whom correspondence should be addressed.Search for more papers by this author Book Editor(s):Derek J. Chadwick, Derek J. Chadwick OrganizerSearch for more papers by this authorJamie A. Goode, Jamie A. GoodeSearch for more papers by this author First published: 15 December 2002 https://doi.org/10.1002/0470860790.ch6Citations: 42Book Series:Novartis Foundation Symposia Series Editor(s): Novartis Foundation, Novartis FoundationSearch for more papers by this author AboutPDFPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShareShare a linkShare onEmailFacebookTwitterLinkedInRedditWechat Summary Goblet cells produce mainly MUC5AC, but also MUC5B and some MUC2 in apparently 'irritated' airways. MUC5B dominates in the submucosal glands although a little MUC5AC and MUC7 are usually present. MUC4 originates from the ciliated cells. After separation into a gel and a sol phase, lysozyme and lactoferrin are enriched in the salivary gel phase suggesting that mucus may act as a matrix for 'protective' proteins on the mucosal surface. A salivary MUC5B N-terminal fragment consistent with a cleavage event in the D′ domain was detected with antibodies against various N-terminal peptide sequences suggesting that assembly of MUC5B occurs through a mechanism similar to that of the von Willebrand factor. Identification of additional cleavage sites C-terminal to the D′ domain suggests that most of the N-terminal low-glycosylated part of MUC5B may be removed without affecting the oligomeric nature of the mucin. Possibly, the generation of mucins with different macromolecular properties through proteolytic 'processing' is one way of adapting the mucus polymer matrix to meet local physiological demands. Monomeric mucins that appear to turn over rapidly in the airway epithelium have been identified using radiolabelled mucin precursors. 'Shedding' of such mucins after microbe attachment may prevent colonization of epithelial surfaces. Citing Literature Mucus Hypersecretion in Respiratory Disease: Novartis Foundation Symposium 248, Volume 248 RelatedInformation
Publication Year: 2002
Publication Date: 2002-12-15
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 58
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