Thesis (D.Sc.)--Boston University, Henry M. Goldman School of Dental Medicine, 2004 (Periodontology and Oral Biology). / Includes bibliography (leaves 165-186). / Mucins play an important protective and lubricative function in the oral
cavity. They protect hard and soft tissues from desiccation, mechanical abrasion
and exogenous insults. These functions are related to the structural properties of
the mucin glycoproteins. The major high molecular weight mucin in salivary
secretions has been identified as the MUC5B gene product, which is a large
secreted gel-forming mucin. The major low molecular weight mucin in salivary
secretions has been identified as the MUC7 gene product, which is a small
secreted mucin. Another class of mucin molecules, the membrane-bound
mucins, is structurally and functionally distinct from MUC5B and MUC7. Two of
the membrane-bound mucins, MUC1 and MUC4, are expressed in all major
human salivary glands as well as in buccal epithelial cells. The secreted forms of
these mucins are also found at low levels in saliva. The aims of this study were:
1) to confirm the expression of membrane-bound mucin MUC1 in oral epithelial
cells, 2) to determine whether the membrane-bound mucin MUC1 can form
complexes with the secreted mucin MUC5B and to localize the MUC1 binding
sites on the MUC5B polypeptide backbone and 3) to identify other proteins from
a salivary protein pool which can form heterotypic complexes with MUC1. [TRUNCATED]
| Identifer | oai:union.ndltd.org:bu.edu/oai:open.bu.edu:2144/31302 |
| Date | January 2004 |
| Creators | Wang, Li |
| Publisher | Boston University |
| Source Sets | Boston University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
| Rights | This work is being made available in OpenBU by permission of its author, and is available for research purposes only. All rights are reserved to the author. |
Page generated in 0.002 seconds