Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031099 (periodontitis)
12,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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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PMID:Cystatins S and C in human whole saliva and in glandular salivas in periodontal health and disease. 792 75

Cystatins are physiological inhibitors of cysteine proteinases and widely distributed in human tissues and fluids including saliva. Cystatins S, SA, SN, and D are only found in glandular saliva and tear fluid whereas cystatin C has been detected in all tested biological fluids. Previous studies demonstrated that total cystatin activity and cystatin C concentration were highest in whole and parotid saliva of periodontitis patients compared to healthy subjects suggesting a response of the salivary glands to an inflammatory condition of the oral cavity. Based on these results we studied a possible change in the concentration of cystatin S, cystatin C, albumin, IgA, amylase activity, and cystatin activity in a whole and parotid saliva of 20 periodontitis patients as a consequence of periodontal treatment. Saliva samples were quantified for cystatins S and C, albumin, and IgA by enzyme-linked immunosorbent assay. Amylase was determined in an activity assay and total cystatin activity was measured towards pa-pain. The clinical condition of the subjects improved significantly after 6 months of periodontal therapy whereas biochemical analyses of whole and parotid saliva indicated that significant changes in salivary protein composition occurred only in whole saliva. Total cystatin activity (P < 0.05) and cystatin C concentration (P < 0.05) of whole saliva samples collected after periodontal treatment decreased to normal healthy control values. Further, concentrations of cystatin S were unchanged during the periodontal treatment process. These results suggest that other sources of cystatins than the parotid gland i.e.; other salivary glands or crevicular fluid, are involved in the decrease of total cystatin activity in whole saliva after periodontal treatment.
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PMID:Effect of periodontal treatment on the protein composition of whole and parotid saliva. 870 50

Cystatins are physiological inhibitors of cysteine proteinases which are widely distributed in human tissues and fluids. In the present study we analysed both the cystatin activity and the different cystatin isoforms in gingival crevicular fluid and saliva samples of nine periodontitis patients. All crevicular fluid samples, which were collected with filter paper points, showed cystatin activity ranging from 7-67 units/mg protein. The mean cystatin activity (24 units/mg protein) was significantly lower (p < 0.05) than that of the saliva samples (mean 93 units/mg protein). The cystatin isoforms in the crevicular fluid were further characterized by immunoblotting with specific antibodies against cystatin C, S, SN and A. While they were clearly present in saliva, cystatin C, cystatin S and cystatin SN could not be detected in any of the crevicular fluid samples. Remarkably, cystatin A was found in all the crevicular fluids as well as in the saliva samples. It is concluded that the cystatin activity found in crevicular fluid is caused, at least partially, by cystatin A. Furthermore, the gingival crevicular fluid is not a major contributor of cystatin C, S and SN activity in saliva.
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PMID:Cystatin A in gingival crevicular fluid of periodontal patients. 940 30