Protein composition of whole and parotid saliva in healthy and periodontitis subjects

Henskens, Yvonne; Keijbus, P.A.M. van den; Veerman, E.C.I.; Weijden, G.A. van der; Timmerman, M.F.; Snoek, C. M.; Velden, U. van der; Amerongen, A. van Nieuw

doi:10.1111/j.1600-0765.1996.tb00464.x

Cited by 119 publications

(110 citation statements)

References 41 publications

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“…Our study is in accordance with other studies which showed an increase in amylase levels in patients with gingivitis and periodontitis [5,13,16,17].…”

Section: Collection Of Salivasupporting

confidence: 82%

“…The increased protein levels in our study in the test groups could be due to the inflammatory process that activates the sympathetic system to enhance the synthesis and secretion of some proteins (as evidenced by increased amylase levels) thereby increasing the protective potential of saliva against the diseases [12,13].…”

Section: Collection Of Salivamentioning

confidence: 99%

“…The increased levels may be due to the response of salivary glands to inflammatory diseases like gingivitis and periodontitis resulting in increased synthesis and secretion of certain acinar proteins like α-amylase so as to enhance the oral defense mechanism [12,13].…”

Section: Collection Of Salivamentioning

confidence: 99%

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Estimation of Levels of Salivary Mucin, Amylase and Total Protein in Gingivitis and Chronic Periodontitis Patients

Kejriwal

Bhandary

Thomas

et al. 2014

JCDR

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Background: Periodontal diseases are a group of inflammatory conditions resulting from interaction between a pathogenic bacterial biofilm and susceptible host's inflammatory response eventually leading to the destruction of periodontal structures and subsequent tooth loss. Hence, investigation of salivary proteins in individuals with periodontal diseases may be useful to enhance the knowledge of their roles in these diseases. Materials and Methods:This case-control study was conducted at A.B. Shetty Memorial Institute of Dental Sciences, Mangalore. The study comprised of 90 patients of age between 25-60 years who were clinically examined and divided into three groups of 30 each: namely clinically healthy, gingivitis and chronic periodontitis. These were classified according to the values of gingival index score, clinical attachment loss and probing pocket depth. Unstimulated saliva was collected and salivary mucin, amylase and total protein levels were determined. Statistical analysis:Results obtained were tabulated and statistically analyzed using ANOVA test and Karl pearson's correlation test. Results:The results of the study showed an increased concentration of salivary mucin, amylase and total protein in gingivitis patients and increased levels of amylase and total protein in saliva of chronic periodontitis patients compared to healthy individuals which were statistically significant. A decrease in mucin concentration was observed in the periodontitis group compared to gingivitis group. A positive correlation was present between salivary mucin, amylase and total protein levels in the three groups.Conclusion: Salivary mucin, amylase and total protein may serve as an important biochemical parameter of inflammation of the periodontium. Also, it can be hypothesized that various enzyme inhibitors might be useful as a part of host modulation therapy in the treatment of periodontal diseases.

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“…Our study is in accordance with other studies which showed an increase in amylase levels in patients with gingivitis and periodontitis [5,13,16,17].…”

Section: Collection Of Salivasupporting

confidence: 82%

Section: Collection Of Salivamentioning

confidence: 99%

See 1 more Smart Citation

Estimation of Levels of Salivary Mucin, Amylase and Total Protein in Gingivitis and Chronic Periodontitis Patients

Kejriwal

Bhandary

Thomas

et al. 2014

JCDR

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“…There is some discordance among the reported levels of cystatin mRNAs, protein concentrations, and cystatin activity (Henskens et al, 1996a,c;Dickinson et al, 2002), suggesting a contribution of post-translational and post-secretion events (such as N-terminal processing) to overall inhibitory capacity. Also, for parotid Table 2 in Henskens et al (1996a).…”

Section: (Ii) Papain-like Cp Inhibitory Activities Of Human Type 2 Cymentioning

confidence: 99%

Salivary (SD-Type)Cystatins:OverOneBillionYears in theMaking—But toWhatPurpose?

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

103

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The cystatin superfamily is comprised of a large group of ancestrally related proteins, most of which are potent inhibitors of cysteine peptidases (CPs). Human saliva contains relatively abundant proteins that are related ancestrally in sequence to the cystatin superfamily. These proteins are now commonly referred to as 'salivary cystatins', although this is something of a misnomer (see below). It has been several years since the publication of the last comprehensive reviews that focused on the salivary cystatins (Bobek and Levine, 1992;Henskens et al., 1996c). Since then, significant advances have been made regarding the gene organization, protein structure, and properties of human and rat proteins. Therefore, a major purpose of this article is to review this recent work. What is the function of the 'salivary cystatins'? Despite a great deal of research effort, we still do not have a definitive answer to this question. A major impediment is the lack of a disease to associate with a specific defect in a gene: Functionality must be inferred from circumstantial evidence. A central premise of this review is that clues to 'salivary cystatin' function are contained within their phylogenetic history, and that by looking at established or likely functions of their 'siblings' and 'cousins', one can assess the likelihood of this function(s) continuing into the 'salivary cystatins'. A comprehensive review of the large cystatin superfamily is beyond the scope of a single article. This review will aim to outline the main branches of the superfamily and the common elements of their structure and function, but will pay closest attention to the nearest relatives of the 'salivary cystatins'.(1) BACKGROUND Scission of peptide bonds is an essential reaction in living cells, and there is a considerable number of peptidases that catalyze this reaction with various degrees of specificity. CPs use a cysteine residue in the active site as the nucleophile in the reaction (see Dickinson, 2002, and references therein). Release of proteolytic enzymes outside of their normal compartment has the potential to cause serious degradation and pathology-an effect taken advantage of by pathogenic organisms from a wide range of phyla. Therefore, control of proteolytic enzyme activity is mandatory. Building upon a very early report (see Barrett et al., 1986, for a review of this earlier literature) of a bovine trypsin inhibitor in chicken egg white, a search for egg white inhibitors of plant proteinases (the CPs ficin and papain) identified a relatively small (12.7 kDa) protein that was a potent inhibitor (Ki = 10 nM). The term cystatin was coined for this protein, which was shown also to inhibit mammalian CPs of the papain superfamily, including cathepsins B, C, H, and L. Cystatins form 1:1 reversible complexes with CPs, in competition with the substrate, but in some cases the binding is so tight as to be physiologically irreversible. (2) THE CYSTATIN SUPERFAMILYExamination of mammalian tissues and serum revealed several CP inhibitors ranging in si...

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“…A possible role for cystatin C in bone resorption in vitro was investigated by Lerner and Grubb (1992) by analyzing the parathyroid hormone stimulated release of 45 Ca and 3 H from prelabeled mouse calvarial bones. Using recombinant cystatin C they showed a significant reduction in the release of 45 Ca and 3 H. 1991Barka etal., 1992Keppler etal., 1994Henskens era/., 1994,1996bBabnik etal., 1988Skaleric et a/., 1989Buttle et a/., 19901991Warfelefa/.,19871991Chapman etal., 1990 Lenarcic ef a/., 1988a Bollengier ef a/., 1987;MacPherson.1965Lofbergefa/,,1980 Grubber a/., 1984 Ghiso era/., 1986 Löfberg and Grubb, 1979Brzinefa/,,1984Kabandaefa/,,1994Lerner and Grubb, 1992Korantefa/,,1986Collins and Grubb, 1991Bjorckefa/.,1990Bjorckefa/,,1989 …”

Section: Inflammatory Diseasesmentioning

confidence: 99%

Review

1996

Biological Chemistry Hoppe-Seyler

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Proteolytic enzymes have many physiological functions in plants, bacteria, viruses, protozoa and mammals. They play a role in processes such as food digestion, complement activation or blood coagulation. The action of proteolytic enzymes is biologically controlled by proteinase inhibitors and increasing attention is being paid to the physiological significance of these natural inhibitors in pathological processes. The reason for this growing interest is that uncontrolled proteolysis can lead to irreversible damage e.g. in chronic inflammation or tumor metastasis. This review focusses on the possible role of the cystatins, natural and specific inhibitors of the cysteine proteinases, in pathological processes. Key words: Cystatins / Cysteine proteinases / Inflammation / Inhibitors / Pathological processes. Cysteine ProteinasesCysteine Proteinases, synonymous with thiol proteinases, are small proteins with molecular masses varying from 23 to 24 kDa and with two catalytic residues, Cys25 and His159, which are involved in the hydrolytic reaction. Cysteine proteinases catalyze the hydrolysis of various polypeptide substrates and are most active under reducing and mildly acidic conditions (pH 5 -6.5). They have been detected in and isolated from a large number of biological sources including plants, bacteria, animals and humans. Bacterial cysteine proteinases are produced by Clostridium histolyticum, named clostripain, by hemolytic group A streptococci and by the pathogenic anaerobic Porphyromonas gingivalis, a bacterium associated with periodontitis. Bacterial cysteine proteinases probably play a role in the penetration of normal tissues by the bacteria and in the food digestion. Viral cysteine proteinases from picornaviruses, e.g. the poliovirus and rhinovirus type I, are involved in proteolytic cleavage of precursor proteins for virus replication and for the production of new virus particles. A virus-coded cysteine proteinase is involved in this process (Kay and Dunn, 1990; Körant et a/., 1985;. HIV-I also needs proteolytic processing by cysteine proteinases to regulate the expression of viral proteins (Guy ef a/., 1991). Protozoal cysteine proteinases are produced by a number of protozoan parasites to facilitate host invasion, metabolize host proteins, to degrade the host immune molecules or to use them for intracellular replication. Cysteine proteinases are produced by e.g. Trypanosoma cruzi, the causative agent of American trypanosomiasis or by Leishmania species, causing one of the six major parasitic diseases. Furthermore, human malarial parasites produce a broad scala of proteinases including cysteine proteinase which are involved in erythrocyte invasion and rupture (McKerrow, 1993). Mammalian cysteine proteinases are present in the lysosomes of cells. Lysosomes contain different cysteine proteinases, the most important being the cathepsins B, H, L and S Kirschke, 1981, Barrett et a/., 1988). These cathepsins have common ancestors and are related to papain. Cathepsin B has been detected in every tissue or cel...

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Protein composition of whole and parotid saliva in healthy and periodontitis subjects

Cited by 119 publications

References 41 publications

Estimation of Levels of Salivary Mucin, Amylase and Total Protein in Gingivitis and Chronic Periodontitis Patients

Estimation of Levels of Salivary Mucin, Amylase and Total Protein in Gingivitis and Chronic Periodontitis Patients

Salivary (SD-Type)Cystatins:OverOneBillionYears in theMaking—But toWhatPurpose?

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