Abstract
MUC7 is a low molecular weight monomeric mucin secreted by submandibular, sublingual and minor salivary glands. This mucin has been implicated in the non-immune host defense system in the oral cavity since it binds and agglutinates a variety of oral microbes. To investigate interactions between this mucin and other secretory salivary proteins, a submandibular gland prey library was screened with baits encoding the N- and C-terminal regions of MUC7 in the yeast two-hybrid system. The N-terminal region interacted with several secretory salivary proteins, whereas the C-terminal region did not. Interacting proteins included amylase, acidic proline-rich protein 2, basic proline-rich protein 3, lacrimal proline-rich protein 4, statherin and histatin 1. Formation of complexes between these proteins and the N-terminal region of MUC7 was confirmed in Far Western blotting experiments. Interactions between mucin and non-mucin proteins in saliva could protect complex partners from proteolysis, modulate the biological activity of complexed proteins or serve as a delivery system for distribution of secretory salivary proteins throughout the oral cavity.
Original language | English (US) |
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Pages (from-to) | 65-72 |
Number of pages | 8 |
Journal | Biochimica et Biophysica Acta - Molecular Cell Research |
Volume | 1746 |
Issue number | 1 |
DOIs | |
State | Published - Oct 30 2005 |
Externally published | Yes |
Keywords
- MG2
- Mucin
- Protein-protein interaction
- Salivary protein
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology