| Primary information |
|---|
| SALID | SAL_14944 |
| Biomarker name | Alpha-amylase 1 (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase 1) (Salivary alpha-amylase) |
| Biomarker Type | NA |
| Sampling Method | Age 25-50 |
| Collection Method | Unstimulated. Rest for 15 min before saliva collection (at morning, 2 h after tooth brushing), sitting in an upright position and were asked not to speak |
| Analysis Method | 2-DE + MALDI-TOF/TOF + LC-ESI-MS + nLC-Q-TOF |
| Collection Site | Whole Saliva |
| Disease Category | Dental Disorder |
| Disease/Condition | Periodontitis |
| Disease Subtype | Chronic periodontitis |
| Fold Change/ Concentration | 1.13 |
| Up/Downregulated | Upregulated |
| Exosomal | NA |
| Organism | Homo sapiens |
| PMID | 20215060 |
| Year of Publication | 2010 |
| Biomarker ID | P04745 |
| Biomarker Category | Protein |
| Sequence | NA |
| Title of study | Comparative proteomic analysis of whole saliva from chronic periodontitis patients |
| Abstract of study | Chronic periodontal disease is a chronic inflammatory process affecting tooth supporting tissues in the presence of pathogenic bacterial biofilm. There is some evidence for changes in the protein composition of whole saliva from chronic periodontitis patients, but there have been no studies using a proteomic approach. Hence, the aim of this study was to compare the protein profiles of unstimulated whole saliva from patients with periodontitis and healthy subjects by two complementary approaches (2D-gel electrophoresis and liquid chromatography). Protein spots of interest were analyzed by MALDI-TOF-TOF, and the data was complemented by an ESI-Q-TOF experiment. The analyses revealed that subjects with periodontal disease have increased amounts of blood proteins (serum albumin and hemoglobin) and immunoglobulin, and they have a lower abundance of cystatin compared to the control group. A higher number of protein spots were observed in the periodontitis group, of which most were identified as alpha-amylase. This higher number of alpha-amylase variants seems to be caused by hydrolysis by cysteine proteases under such inflammatory conditions. This approach gives novel insights into alterations of salivary protein in presence of periodontal inflammation and may contribute to the improvement of periodontal diagnosis. |