Abstract

The purpose of this investigation is to continue our characterization of the structural domains of the higher and lower molecular weight human salivary mucins. Structural comparisons of these molecules will be made between two groups: (a) caries susceptible versus caries resistant subjects and (b) individuals with cystic fibrosis versus normals. The proposed studies wil utilize basic biochemical methods in carbohydrate and protein chemistry and recombinant DNA technology. In particular, techniques of periodate oxidation, methylation analyses by GC/mass spectroscopy, exoglycosidase digestion, and NMR spectroscopy will be used to delineate oligosaccharide structures. Automated peptide sequencing and recombinant DNA techniques will be used to define the peptide sequences. The information to be obtained could ultimately provide an insight regarding (a) the role of salivary mucins in oral clearance and adherence phenomena; (b) the mechanisms by which the host can intrinsically regulate resistance to dental caries; and (c) the changes which occur in mucins in exocrine secretions in cystic fibrosis. Such knowledge could ultimately lead to modalities useful in both the prevention and treatment of diseases manifest in the oral cavity.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Research Project (R01)
Project #
5R01DE004971-10
Application #
3219204
Study Section
Oral Biology and Medicine Study Section (OBM)
Project Start
1979-01-01
Project End
1988-05-31
Budget Start
1988-01-01
Budget End
1988-05-31
Support Year
10
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
State University of New York at Buffalo
Department
Type
Schools of Dentistry/Oral Hygn
DUNS #
038633251
City
Buffalo
State
NY
Country
United States
Zip Code
14260

  Publications

Al-Hashimi, I; Levine, M J (1989) Characterization of in vivo salivary-derived enamel pellicle. Arch Oral Biol 34:289-95
Loomis, R E; Tseng, C C; Bergey, E J et al. (1988) N.m.r. and computer-simulated conformational analyses of a nonapeptide found in a human salivary proline-rich glycoprotein. Int J Pept Protein Res 32:130-40
Loomis, R E; Tseng, C C; Levine, M J (1988) N.m.r. analyses of the histidine microenvironments in a human salivary proline-rich glycoprotein. Int J Pept Protein Res 32:123-9
Al-Hashimi, I; Dickinson, D P; Levine, M J (1988) Purification, molecular cloning, and sequencing of salivary cystatin SA-1. J Biol Chem 263:9381-7
Levine, M J; Reddy, M S; Tabak, L A et al. (1987) Structural aspects of salivary glycoproteins. J Dent Res 66:436-41
Loomis, R E; Bhandary, K K; Tseng, C C et al. (1987) Nuclear magnetic resonance spectroscopic and computer-stimulated structural analyses of a heptapeptide sequence found around the N-glycosylation site of a proline-rich glycoprotein from human parotid saliva. Biophys J 51:193-203
Aguirre, A; Levine, M J; Cohen, R E et al. (1987) Immunochemical quantitation of alpha-amylase and secretory IgA in parotid saliva from people of various ages. Arch Oral Biol 32:297-301
Loomis, R E; Prakobphol, A; Levine, M J et al. (1987) Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva. Arch Biochem Biophys 258:452-64
Al-Hashimi, I; Drinnan, A J; Uthman, A A et al. (1987) Oral amyloidosis: two unusual case presentations. Oral Surg Oral Med Oral Pathol 63:586-91
Hatton, M N; Levine, M J; Margarone, J E et al. (1987) Lubrication and viscosity features of human saliva and commercially available saliva substitutes. J Oral Maxillofac Surg 45:496-9

Showing the most recent 10 out of 19 publications