Salivary enzymes as diagnostic markers for detection of gingival/periodontal disease and their correlation with the severity of the disease

Abstract

Context:Host responses to periodontal disease include the production of different enzymes released by stromal, epithelial or inflammatory cells. Important enzymes associated with cell injury and cell death are aspartate aminotransferase, alanine aminotransferase (AST, ALT), alkaline phosphatase, acidic phosphatase (ALP, ACP), and gama glutamyl transferase (GGT). Changes in enzymatic activity reflect metabolic changes in the gingiva and periodontium, in the inflammation.Aims:In this article we examined the activity of AST, ALT, GGT, ALP, and ACP in the saliva from patients with periodontal disease, before and after periodontal treatment (experimental group — 20 gingivitis patients and 20 periodontitis patients), and in the saliva from healthy subjects (control group — 20 samples).Settings and Design:Periodontal disease was determined based on the clinical parameters (gingival index (GI), probing depth (PD), and clinical attachment loss (CAL)). Patients with periodontal disease were under conventional periodontal treatment.Materials and Methods:The stimulated saliva of the patient was collected in a sterile test tube and analyzed using the Automatic Analyzer.Results:The obtained results showed statistically significant increased activity of AST, ALT, GGT, ALP, and ACP in the saliva from patients with periodontal disease, in relation to the control group. A significant reduction in the enzyme levels was seen after conventional periodontal therapy.Conclusions:Based on these results, it can be assumed that the salivary enzymes (AST, ALT, GGT, ALP, and ACP) can be considered as biochemical markers for evaluating the diagnosis and prognosis of the functional condition of periodontal tissues in disease and health, and in the evaluation of the therapy effects in periodontal disease.

Comparison of Salivary pH, Buffering Capacity and Alkaline Phosphatase in Smokers and Healthy Non-Smokers: Retrospective cohort study

“…20 Furthermore, various studies have shown that altered salivary pH, BC and ALP levels are associated with the formation or development of dental caries, gingivitis, periodontitis, human immunodeficiency virus (HIV) infection, diabetes, orthodontic tooth movements, cancer, abdominal inflammatory diseases and the early onset of menopause. 3,4,12,13,[21][22][23][24][25][26][27][28][29] In the current study, salivary pH was lower among smokers in comparison to non-smokers; although the mean values found seem to reflect a minimal difference between the two groups (7.42 versus 7.52, respectively), even very small alterations in pH can influence salivary enzyme activity. 6 Additionally, BC was significant lower among smokers in the current study.…”

“…23 Higher salivary ALP levels have also been found among individuals with periodontal disease, pancreatitis and appendicitis, with treatment of the disease resulting in lowered enzyme levels. 3,4,29 Therefore, non-invasive assessment of ALP levels may be useful in the diagnosis and prognosis of periodontal tissue function and treatment monitoring of abdominal inflammatory diseases. 3,29 Smoking has been found to cause periodontal disease and bone destruction.…”

“…3,4,29 Therefore, non-invasive assessment of ALP levels may be useful in the diagnosis and prognosis of periodontal tissue function and treatment monitoring of abdominal inflammatory diseases. 3,29 Smoking has been found to cause periodontal disease and bone destruction. 32 However, in the current study, smokers with periodontal disease were not included and specific side-effects of smoking on the oral mucosa were not evaluated.…”

“…ALP most commonly correlates with bone metabolism and is present in the osteoblast cell membrane and polymorphonuclear leukocyte granules. 3 Destructive processes in the alveolar bone can lead to increased ALP activity. 4,5 A key factor in enzyme functionality is pH, with the optimum pH for ALP activity being ≈ 7.4.…”

“…1 Alkaline phosphatase (ALP) is an intracellular enzyme present in the saliva and most tissues, organs and bones, including the epithelial, inflammatory cells, bacterial organisms and mineralising tissue cells. [3][4][5] The enzyme is related to cell injury and death. ALP most commonly correlates with bone metabolism and is present in the osteoblast cell membrane and polymorphonuclear leukocyte granules.…”