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Respiratory tract mucins: structure and expression patterns

Davies, Julia LU ; Herrmann, Annkatrin LU ; Russell, Wayne LU ; Svitacheva, Naila LU ; Wickström, Claes LU and Carlstedt, Ingemar LU (2002) In Mucus Hypersecretion in Respiratory Disease (Novartis Foundation Symposia) 248. p.76-93
Abstract
Goblet cells produce mainly MUC5AC, but also MUC5B and some MUC2 in apparently 'irritated' airways. MUC513 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... (More)
Goblet cells produce mainly MUC5AC, but also MUC5B and some MUC2 in apparently 'irritated' airways. MUC513 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. (Less)
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author
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
in
Mucus Hypersecretion in Respiratory Disease (Novartis Foundation Symposia)
volume
248
pages
76 - 93
publisher
John Wiley & Sons
external identifiers
  • pmid:12568489
  • wos:000181919500005
  • scopus:0037674017
ISBN
9780470844786
DOI
10.1002/0470860790.ch6
language
English
LU publication?
yes
id
f720c4bd-06b6-4f32-83f1-2c0b09384ae0 (old id 314860)
date added to LUP
2007-08-15 16:25:23
date last changed
2017-01-01 08:06:21
@inbook{f720c4bd-06b6-4f32-83f1-2c0b09384ae0,
  abstract     = {Goblet cells produce mainly MUC5AC, but also MUC5B and some MUC2 in apparently 'irritated' airways. MUC513 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.},
  author       = {Davies, Julia and Herrmann, Annkatrin and Russell, Wayne and Svitacheva, Naila and Wickström, Claes and Carlstedt, Ingemar},
  isbn         = {9780470844786},
  language     = {eng},
  pages        = {76--93},
  publisher    = {John Wiley & Sons},
  series       = {Mucus Hypersecretion in Respiratory Disease (Novartis Foundation Symposia)},
  title        = {Respiratory tract mucins: structure and expression patterns},
  url          = {http://dx.doi.org/10.1002/0470860790.ch6},
  volume       = {248},
  year         = {2002},
}