Several pathologies of the oral cavity have been associated with stress, so we investigated salivary-induced aggregation during psychological stress. In addition, salivary total protein, alpha-amylase, and secretory immunoglobulin A (s-IgA) were assessed. In this longitudinal study, 28 dental students provided unstimulated whole saliva during 10 minutes before an academic examination and subsequently 2 weeks and 6 weeks later in a nonstress situation. The effect of whole saliva on the aggregation of Streptococcus gordonii (HG 222) was determined spectrophotometrically. The results shows a significant stress-mediated increase of salivary total protein concentration, alpha-amylase activity, amylase/protein ratio, alpha-amylase output, s-IgA concentration, and s-IgA output. There was also a trend for increased total protein output, whereas salivary flow rate was unchanged. The aggregation of S. gordonii in whole saliva collected before examination was 13.1%, whereas the aggregation in whole saliva collected during nonstress was 23.3%. This reduction was statistically significant (p < .01). Furthermore, the decrease in bacterial aggregation was related to the increase in state-anxiety (p < .05). The reduction in aggregation of S. gordonii under stress was not correlated with changes in salivary flow rate, s-IgA concentration, total protein concentration, or alpha-amylase activity. These results suggest that acute psychological stress exerts its influence on both salivary composition and salivary function. Reduced bacterial aggregation may be a contributing factor in the often reported relationship between stress and impaired oral health.

Human saliva is secreted by the three pairs of major salivary glands (parotid, submandibular, and sublingual), and numerous minor ones, e.g. labial, buccal and (glosso)palatine glands. Using individually adapted collection devices, sublingual, submandibular, parotid and palatine secretions of five individuals were collected and analyzed. Electrophoretic analysis revealed that each type of saliva possesses characteristic features, despite interindividual variations. Parotid salivas are characterized by intensely staining amylase and proline-rich protein bands, but contain minute amounts of cystatins, lysozyme and the extra-parotid glycoprotein. Sublingual salivas are characterized by high concentrations of both types of salivary mucins, MG1 and MG2, and contain relatively high levels of lysozyme. Submandibular salivas contain highest concentration of salivary cystatin S. Palatine secretions contain high molecular weight mucins and a relatively high amylase concentration.

Salivary protein, albumin and cystatin concentrations were investigated in subjects with a healthy periodontium and in patients with gingivitis or periodontitis. Protein and albumin concentrations in saliva of individuals with gingivitis or periodontitis were significantly increased compared with healthy subjects. Salivary protein and albumin appeared to be positively correlated in all the groups, which suggests that the increase in salivary protein concentration in subjects with gingivitis or periodontitis is caused by leakage of plasma proteins. Cystatin concentrations in saliva of subjects with periodontitis were significantly increased when compared with the healthy group and the gingivitis group (p < 0.01). In the gingivitis and periodontitis group, salivary cystatin was only weakly correlated with albumin concentrations, which suggests that the increased salivary cystatin activity found in subjects with gingivitis and periodontitis is derived from sources other than plasma.

Cystatins are inhibitors of cysteine proteinases and could play a protective and regulatory role under inflammatory conditions. Since total cystatin activity of whole saliva was increased in periodontal patients (Henskens et al., 1993), we wanted to investigate the types or origins of cystatins involved in this increase. Distinct types of cystatins were identified by isoelectric focusing and immunoblotting with specific antibodies against one of the salivary acidic isoforms, cystatin S. and the widely distributed basic cystatin C. Clarified human whole saliva (CHWS) of healthy subjects contained cystatin S, whereas cystatin C was barely detectable. In contrast, in CHWS of gingivitis and periodontitis patients, both cystatin C and S levels were higher. The origin of cystatin activity was investigated by collecting submandibular (SM), sublingual (SL), and parotid (PAR) saliva from seven subjects with mild gingivitis. Total cystatin activity was about five times higher in SM saliva than in PAR saliva. In SM and SL saliva, both cystatins S and C were demonstrated. In contrast, in PAR samples, solely cystatin C was detectable. The introduction of experimental gingivitis in one periodontally healthy subject resulted in the appearance of a cystatin C band in PAR saliva and in an increase of cystatins S and C in SM saliva. We conclude that the previously observed increase of cystatin activity in whole saliva in inflammatory periodontal disease is, at least in part, due to an increased glandular output of both the isoform cystatin S (pI 4.7) and the basic cystatin C (pI 9.0).

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Extra Parotid Glycoprotein (EP-GP) is a glycoprotein isolated from human saliva, having homologues in several other body fluids. The biological role of EP-GP and its homologues is unknown. Recently, EP-GP was shown to bind in vitro to the bacterium Streptococcus salivarius HB. In contrast, no binding to a number of other oral microorganisms could be demonstrated. In the present study we have determined whether binding of EP-GP to bacteria occurs in vivo in saliva and in other EP-GP containing body fluids. Therefore the presence of EP-GP on bacteria in vivo was determined by analyzing oral, skin and ear floras by confocal fluoresence microscopy using specific antibodies. About 12% of the in vivo oral flora had EP-GP present on their surface, while approximately 5% of the bacteria from ear canal or skin was positive for EP-GP. IgA was detected on approximately 65% of the salivary bacteria, whereas the high-molecular weight mucin (MG1) and cystatin C were not detectable on any oral bacterium. Using a replica-plate assay, a number of EP-GP binding strains in saliva were isolated and identified as Gemella haemolysans, Gemella morbillorium, Streptococcus acidominimus, Streptococcus oralis, Streptococcus salivarius and Streptococcus parasanguis. Bacteria from the ear canal and skin bacteria were identified as Staphylococcus hominis. It is concluded that EP-GP is selectively bound in vivo to several oral and non-oral bacterial species.

In Sjögren's syndrome, salivary glands are affected, resulting in a diminished salivary flow. In the present study, the protein composition, sialic acid content and the amounts of calcium and phosphate of stimulated whole saliva from 43 patients with Sjögren's syndrome, were compared with those of control saliva samples from 17 healthy subjects. The absolute concentrations of albumin, cystatin C. cystatin S. total IgA and total protein, but not amylase, were increased significantly in both primary and secondary Sjögren's syndrome. The output/min of total protein, albumin, amylase, and IgA was, however, decreased in Sjögren patients. These results suggest that the diminished output of salivary defence factors, rather than their absolute concentrations, may be related to the oral health problems seen in Sjögren's syndrome patients.