Influence of mouse prolactin‐inducible protein in saliva on the aggregation of oral bacteria

Nistor, Andreea; Bowden, G. H.; Blanchard, Anne; Myal, Yvonne

doi:10.1111/j.1399-302x.2009.00543.x

Cited by 19 publications

(22 citation statements)

References 29 publications

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“…These include the small salivary mucin‐7 (MUC7) (MG2), which promotes bacterial agglutination, surfactant protein‐A, proline‐rich proteins, prolactin‐inducible protein and β ‐2‐microglobulin, which is notably present in most (82%) biopsies from aggressive periodontitis patients but largely absent from normal controls and chronic severe periodontitis specimens (Syrjanen et al 1985). Saliva from prolactin‐inducible protein‐knock‐out mice exhibit significantly lower agglutination of oral bacteria than saliva from wild‐type control mice, suggesting that prolactin‐inducible protein contributes to host‐defense of the oral cavity by agglutinating oral bacteria (Nistor et al 2009). The salivary agglutinin/ GP340 / Deleted in Malignant Brain Tumors‐1 ( DMBT1 ) is a large glycoprotein that contains multiple scavenger receptor cysteine‐rich repeats.…”

Section: Functional Families Of Antimicrobial Proteins In the Oral Camentioning

confidence: 99%

Antimicrobial peptides and periodontal disease

Gorr

Abdolhosseini

2011

J Clinic Periodontology

152

158

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Aims: The goal of this review is to identify the antimicrobial proteins in the oral fluids, saliva and gingival crevicular fluid and identify functional families and candidates for antibacterial treatment. Results: Periodontal biofilms initiate a cascade of inflammatory and immune processes that lead to the destruction of gingival tissues and ultimately alveolar bone loss and tooth loss. Treatment of periodontal disease with conventional antibiotics does not appear to be effective in the absence of mechanical debridement. An alternative treatment may be found in antimicrobial peptides and proteins, which can be bactericidal and anti-inflammatory and block the inflammatory effects of bacterial toxins. The peptides have co-evolved with oral bacteria, which have not developed significant peptide resistance. Over 45 antibacterial proteins are found in human saliva and gingival crevicular fluid. The proteins and peptides belong to several different functional families and offer broad protection from invading microbes. Several antimicrobial peptides and proteins (AMPs) serve as templates for the development of therapeutic peptides and peptide mimetics, although to date none have demonstrated efficacy in human trials. Conclusions: Existing and newly identified AMPs may be developed for therapeutic use in periodontal disease or can serve as templates for peptide and peptide mimetics with improved therapeutic indices.

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Section: Functional Families Of Antimicrobial Proteins In the Oral Camentioning

confidence: 99%

Antimicrobial peptides and periodontal disease

Gorr

Abdolhosseini

2011

J Clinic Periodontology

152

158

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“…Of particular interest is the prolactin inducible protein, Pip, a protein first identified by us and shown to be highly abundant in both mouse and human saliva [21,22], and was found to be abundant in all 4 saliva sample pools (2 female pools, 2 male pools). We have previously shown that Pip can aggregate oral bacteria [23] inhibiting their activity. Further, using a Pip knockout mouse model we demonstrated that loss of Pip function had significant effects on both the diversity of the oral flora and abundance of specific bacteria of the oral cavity of the Pip null mouse [24].…”

Section: Resultsmentioning

confidence: 99%

Towards further defining the proteome of mouse saliva

et al. 2015

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BackgroundKnowledge of the mouse salivary proteome is not well documented and as a result, very limited. Currently, several salivary proteins remain unidentified and for some others, their function yet to be determined. The goal of the present study is to utilize mass spectrometry analysis to widen our knowledge of mouse salivary proteins, and through extensive database searches, provide further insight into the array of proteins that can be found in saliva. A comprehensive mouse salivary proteome will also facilitate the development of mouse models to study specific biomarkers of many human diseases.ResultsIndividual saliva samples were collected from male and female mice, and later pooled according to sex. Two pools of saliva from female mice (2 samples/pool) and 2 pools of saliva from male mice were used for analysis utilizing high performance liquid chromatograph mass spectrometry (nano-RPLC-MS/MS). The resulting datasets identified 345 proteins: 174 proteins were represented in saliva obtained from both sexes, as well as 82 others that were more female specific and 89 that were more male specific. Of these sex linked proteins, twelve were identified as exclusively sex-limited; 10 unique to males and 2 unique to females. Functional analysis of the 345 proteins identified 128 proteins with catalytic activity characteristics; indicative of proteins involved in digestion, and 35 proteins associated with stress response, host defense, and wound healing functions. Submission of the list of 345 proteins to the BioMart data mining tool in the Ensembl database further allowed us to identify a total of 283 orthologous human genes, of which, 131 proteins were recently reported to be present in the human salivary proteome.ConclusionsThe present study is the most comprehensive list to date of the proteins that constitute the mouse salivary proteome. The data presented can serve as a useful resource for identifying potentially useful biomarkers of human health and disease.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-015-0068-3) contains supplementary material, which is available to authorized users.

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“…Regarding prolactin-induced proteins, they were observed in higher abundance in 2-DE and in the whole extract of dental biofilm formed in the presence of monosaccharides than in the control and sucrose groups. These proteins are involved in bacterial aggregation [Nistor et al , 2009], and the reason why treatment with the mixture of glucose and fructose allowed the maintenance of these proteins, either by less processing by bacteria or due to the presence of new binding sites for protein in the dental biofilm, requires further studies.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Matrix of Dental Biofilm Formed under Dietary Carbohydrate Exposure

Moi

Cury²,

Dombroski³

et al. 2012

Caries Res

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To evaluate whether protein changes in extracellular matrix of dental biofilm are a unique property of sucrose, this in situ study was conducted using as active control glucose and fructose, the sucrose monosaccharide constituents. Proteins were analyzed by two-dimensional electrophoresis followed by LC-MS/MS after trypsin digestion. Absence or lower abundance of calcium-binding proteins and higher abundance of prolactin-induced proteins were found in biofilm formed in the presence of sucrose or its monosaccharide constituents compared with water, the negative control group. The data suggest that besides sucrose, other dietary carbohydrates may also provoke a change in the protein profile of extracellular matrix of dental biofilm formed.

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Influence of mouse prolactin‐inducible protein in saliva on the aggregation of oral bacteria

Cited by 19 publications

References 29 publications

Antimicrobial peptides and periodontal disease

Antimicrobial peptides and periodontal disease

Towards further defining the proteome of mouse saliva

Proteomic Analysis of Matrix of Dental Biofilm Formed under Dietary Carbohydrate Exposure

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