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MUC16 is produced in tracheal surface epithelium and submucosal glands and is present in secretions from normal human airway and cultured bronchial epithelial cells.

Davies, Julia LU ; Kirkham, Sara; Svitacheva, Naila LU ; Thornton, David J and Carlstedt, Ingemar LU (2007) In International Journal of Biochemistry & Cell Biology 39(10). p.1943-1954
Abstract
The gel-forming MUC5AC and MUC5B mucins have been identified as major components of human airway mucus but it is not known whether additional mucin species, possibly with other functions, are also present. MUC16 mucin is a well-known serum marker for ovarian cancer, but the molecule has also been found on the ocular surface and in cervical secretions suggesting that it may play a role on the normal mucosal surface. In this investigation, the LUM16-2 antiserum (raised against a sequence in the N-terminal repeat domain) recognized MUC16 in goblet and submucosal gland mucous cells as well as on the epithelial surface of human tracheal tissue suggesting that the mucin originates from secretory cells. MUC16 mucin was present in ‘normal’... (More)
The gel-forming MUC5AC and MUC5B mucins have been identified as major components of human airway mucus but it is not known whether additional mucin species, possibly with other functions, are also present. MUC16 mucin is a well-known serum marker for ovarian cancer, but the molecule has also been found on the ocular surface and in cervical secretions suggesting that it may play a role on the normal mucosal surface. In this investigation, the LUM16-2 antiserum (raised against a sequence in the N-terminal repeat domain) recognized MUC16 in goblet and submucosal gland mucous cells as well as on the epithelial surface of human tracheal tissue suggesting that the mucin originates from secretory cells. MUC16 mucin was present in ‘normal’ respiratory tract mucus as well as in secretions from normal human bronchial epithelial (NHBE) cells. MUC16 from NHBE cells was a high-molecular-mass, monomeric mucin which gave rise to large glycopeptides after proteolysis. N- and C-terminal fragments of the molecule were separated on gel electrophoresis showing that the MUC16 apoprotein undergoes a cleavage between these domains, possibly in the SEA domain as demonstrated for other transmembrane mucins; MUC1 and MUC3. After metabolic labeling of NHBE cells, most of the secreted monomeric, high-molecular-mass [35S]sulphate-labelled molecules were immunoprecipitated with the OC125 antibody indicating that MUC16 is the major [35S]sulphate-labelled mucin in NHBE cell secretions. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
epithelium, MUC16, submucosal, glands, bronchial, epithelial
in
International Journal of Biochemistry & Cell Biology
volume
39
issue
10
pages
1943 - 1954
publisher
Elsevier
external identifiers
  • wos:000249943500019
  • scopus:34548201282
ISSN
1878-5875
DOI
10.1016/j.biocel.2007.05.013
language
English
LU publication?
yes
id
c7c92a53-0f85-4b25-b504-23e3c64a8867 (old id 541114)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17604678&dopt=Abstract
date added to LUP
2007-12-06 14:49:27
date last changed
2017-10-22 04:48:22
@article{c7c92a53-0f85-4b25-b504-23e3c64a8867,
  abstract     = {The gel-forming MUC5AC and MUC5B mucins have been identified as major components of human airway mucus but it is not known whether additional mucin species, possibly with other functions, are also present. MUC16 mucin is a well-known serum marker for ovarian cancer, but the molecule has also been found on the ocular surface and in cervical secretions suggesting that it may play a role on the normal mucosal surface. In this investigation, the LUM16-2 antiserum (raised against a sequence in the N-terminal repeat domain) recognized MUC16 in goblet and submucosal gland mucous cells as well as on the epithelial surface of human tracheal tissue suggesting that the mucin originates from secretory cells. MUC16 mucin was present in ‘normal’ respiratory tract mucus as well as in secretions from normal human bronchial epithelial (NHBE) cells. MUC16 from NHBE cells was a high-molecular-mass, monomeric mucin which gave rise to large glycopeptides after proteolysis. N- and C-terminal fragments of the molecule were separated on gel electrophoresis showing that the MUC16 apoprotein undergoes a cleavage between these domains, possibly in the SEA domain as demonstrated for other transmembrane mucins; MUC1 and MUC3. After metabolic labeling of NHBE cells, most of the secreted monomeric, high-molecular-mass [35S]sulphate-labelled molecules were immunoprecipitated with the OC125 antibody indicating that MUC16 is the major [35S]sulphate-labelled mucin in NHBE cell secretions.},
  author       = {Davies, Julia and Kirkham, Sara and Svitacheva, Naila and Thornton, David J and Carlstedt, Ingemar},
  issn         = {1878-5875},
  keyword      = {epithelium,MUC16,submucosal,glands,bronchial,epithelial},
  language     = {eng},
  number       = {10},
  pages        = {1943--1954},
  publisher    = {Elsevier},
  series       = {International Journal of Biochemistry & Cell Biology},
  title        = {MUC16 is produced in tracheal surface epithelium and submucosal glands and is present in secretions from normal human airway and cultured bronchial epithelial cells.},
  url          = {http://dx.doi.org/10.1016/j.biocel.2007.05.013},
  volume       = {39},
  year         = {2007},
}