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Identification of Protein Components in Human Acquired Enamel Pellicle and Whole Saliva Using Novel Proteomics Approaches
- Source :
- Journal of Biological Chemistry. 278:5300-5308
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- Precursor proteins of the acquired enamel pellicle derive from glandular and non-glandular secretions, which are components of whole saliva. The purpose of this investigation was to gain further insights into the characteristics of proteins in whole saliva and in vivo formed pellicle components. To maximize separation and resolution using only micro-amounts of protein, a two-dimensional gel electrophoresis system was employed. Protein samples from parotid secretion, submandibular/sublingual secretion, whole saliva, and pellicle were subjected to isoelectric focusing followed by SDS-PAGE. Selected protein spots were excised, subjected to "in-gel" trypsin digestion, and examined by mass spectrometry (MS). The data generated, including peptide maps and tandem MS spectra, were analyzed using protein data base searches. Components identified in whole saliva include cystatins (SA-III, SA, and SN), statherin, albumin, amylase, and calgranulin A. Components identified in pellicle included histatins, lysozyme, statherin, cytokeratins, and calgranulin B. The results showed that whole saliva and pellicle have more complex protein patterns than those of glandular secretions. There are some similarities and also distinct differences between the patterns of proteins present in whole saliva and pellicle. MS approaches allowed identification of not only well characterized salivary proteins but also novel proteins not previously identified in pellicle.
- Subjects :
- Proteomics
Dental pellicle
Sensitivity and Specificity
Biochemistry
chemistry.chemical_compound
Dental Enamel Proteins
stomatognathic system
Humans
Calgranulin
Electrophoresis, Gel, Two-Dimensional
Dental Pellicle
Amylase
Protein Precursors
Salivary Proteins and Peptides
Molecular Biology
Gel electrophoresis
biology
Isoelectric focusing
Albumin
Cell Biology
stomatognathic diseases
chemistry
biology.protein
Lysozyme
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 278
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....828f7027448a92eeb7c2b8a54246adc0