MUC16 is produced in tracheal surface epithelium and submucosal glands and is present in secretions from normal human airway and cultured bronchial epithelial cells.
(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:
https://lup.lub.lu.se/record/541114
- author
- Davies, Julia LU ; Kirkham, Sara ; Svitacheva, Naila LU ; Thornton, David J and Carlstedt, Ingemar LU
- organization
- publishing date
- 2007
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Mucosal biology (013212033)
- id
- c7c92a53-0f85-4b25-b504-23e3c64a8867 (old id 541114)
- date added to LUP
- 2016-04-01 17:03:32
- date last changed
- 2022-01-29 00:01:06
@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}},
keywords = {{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 = {{https://lup.lub.lu.se/search/files/4862002/626080.pdf}},
doi = {{10.1016/j.biocel.2007.05.013}},
volume = {{39}},
year = {{2007}},
}