Open AccessHuman neutrophil elastase releases cell surface mucins from primary cultures of hamster tracheal epithelial cells.
Author(s) -
Kwang C. Kim,
Kojiro Wasano,
Richard M. Niles,
Jonathan E. Schuster,
Phillip J. Stone,
Jerome S. Brody
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.24.9304
Subject(s) - mucin , neutrophil elastase , hamster , elastase , muc1 , chemistry , microbiology and biotechnology , in vitro , cell culture , in vivo , biology , biochemistry , immunology , inflammation , enzyme , genetics
Primary hamster tracheal epithelial cells growing on a collagen gel matrix produce high molecular weight mucins indistinguishable from mucins produced in vivo. Using a modified version of these confluent cultures, we have demonstrated here that (i) release of mucins can be stimulated by human neutrophil elastase (HNE; EC 3.4.21.37); (ii) HNE can degrade mucins, and both mucin release and degradation by HNE require an active catalytic site; and (iii) there are at least two pools of mucins in these cells: one is a rapidly turning-over spontaneously releasable constitutive pool, the other is a slowly turning-over HNE-releasable pool. We provide evidence that the HNE-releasable mucins are membrane bound and associated with the secretory cell apical surface.