Pellicle Precursor Protein Crosslinking: Characterization of an Adduct between Acidic Proline-rich Protein (PRP-1) and Statherin Generated by Transglutaminase

Yao, Yuan; Lamkin, Mark; Oppenheim, F. G.

doi:10.1177/00220345000790040801

Cited by 43 publications

(39 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, in the guanidine extract three phosphorylated peptides were detected while a much higher number of these species (n = 9) were observable on the TFA fraction (identified as fragments i 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim www.jss-journal.com of statherin, acidic PRPs, collagen and basic salivary proline-rich protein 4 allele L). The ability of statherin and of acidic PRPs to adsorb to enamel surface has been extensively described [5,13,21,23,28,30]. Most of the identified species in this work were fragments and were resultant of the degradation from intact species that are also present on AEP.…”

Section: Discussionmentioning

confidence: 75%

“…Within 30 min, the thickness layer of the biofilm increases, most probably, by the adsorption of other proteins through protein -protein interaction, forming globular structures usually assigned as micelle-like structures [10,11]. Enamel acquired pellicle formation is a dynamic process since, under in vivo conditions, the enamel surface is continuously exposed to whole saliva with new species, its inherent proteolytic activity [12] and to enzymatic crosslinking (mainly via transglutaminase activity) [13,14]. This exposure leads to time course modifications of the adsorbed species with the presence of unique molecular forms.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

Vitorino

Calheiros-Lobo²,

Duarte

et al. 2008

J of Separation Science

View full text Add to dashboard Cite

The present study proposes a strategy for human in vivo acquired enamel pellicle (AEP) peptidome characterisation based on sequential extraction with guanidine and TFA followed by MALDI-TOF/TOF identification. Three different nanoscale analytical approaches were used: samples were subjected to tryptic digestion followed by nano-HPLC and mass spectrometry (MS and MS/MS) analysis. Undigested samples were analysed by LC-MS (both linear and reflector modes) and LC-MS/MS analysis, and samples were subjected to nano-HPLC followed by on-plate digestion and mass spectrometry (MS and MS/MS) analysis. The majority of the identifications corresponded to peptide/protein fragments of salivary protein, belonging to the classes: acidic PRPs, basic PRPs, statherin, cystatins S and SN and histatin 1 (all also identified in intact form). Overall, more than 90 peptides/proteins were identified. Results clearly show that peptides with acidic groups are enriched in the TFA fraction while peptides with no acidic or phosphate groups are prevalent on the guanidine extract. Also, phosphorylated peptides were observed mainly on the TFA fraction. Fragments present in the AEP show a predominance of cleavage points located at Arg, Tyr and Lys residues. Obtained data suggest that proteolytic activity could influence AEP formation and composition.

show abstract

Section: Discussionmentioning

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

Vitorino

Calheiros-Lobo²,

Duarte

et al. 2008

J of Separation Science

View full text Add to dashboard Cite

show abstract

“…These results suggested that proteins originating from non-glandular sources may contribute more significantly to WS and EP than previously recognized or that proteins may have undergone extensive proteolysis, cross-linking, and other modifications (54,55). Some interesting contributors to EP are members of the cytokeratin family, cytokeratin 13 and 15 (56), pointing to oral epithelium as one of the sources of proteins deposited on the tooth surface.…”

Section: Fig 2 Two-dimensional Gel Electrophoresis Of Salivary Glanmentioning

confidence: 88%

Identification of Protein Components in Human Acquired Enamel Pellicle and Whole Saliva Using Novel Proteomics Approaches

Yao¹,

Berg²,

Costello³

et al. 2003

Journal of Biological Chemistry

207

183

View full text Add to dashboard Cite

Precursor proteins of the acquired enamel pellicle derive from glandular and non-glandular secretions, which are components of whole saliva. The purpose of this investigation was to gain further insights into the characteristics of proteins in whole saliva and in vivo formed pellicle components. To maximize separation and resolution using only micro-amounts of protein, a two-dimensional gel electrophoresis system was employed. Protein samples from parotid secretion, submandibular/sublingual secretion, whole saliva, and pellicle were subjected to isoelectric focusing followed by SDS-PAGE. Selected protein spots were excised, subjected to "in-gel" trypsin digestion, and examined by mass spectrometry (MS). The data generated, including peptide maps and tandem MS spectra, were analyzed using protein data base searches. Components identified in whole saliva include cystatins (SA-III, SA, and SN), statherin, albumin, amylase, and calgranulin A. Components identified in pellicle included histatins, lysozyme, statherin, cytokeratins, and calgranulin B. The results showed that whole saliva and pellicle have more complex protein patterns than those of glandular secretions. There are some similarities and also distinct differences between the patterns of proteins present in whole saliva and pellicle. MS approaches allowed identification of not only well characterized salivary proteins but also novel proteins not previously identified in pellicle.Human teeth are exposed to whole saliva (WS), 1 consisting mainly of secretions derived from three pairs of major salivary glands, which comprise parotid, submandibular, and sublingual glands. Protein components that have been identified in all of the major glandular secretions are proline-rich proteins (acidic, basic, and glycosylated families), amylase, statherin, histatins, lysozyme, lactoferrin, lactoperoxidase, and secretory IgA (1-10), whereas cystatins and mucins have been identified in submandibular/sublingual secretions (9, 11-13). However, detailed understanding of the protein composition in WS is still limited because of the lack of knowledge about proteins in other contributors to whole saliva such as secretions from minor salivary glands and gingival crevicular fluid. In addition, little is known about modifications that occur on proteins during or after secretion into the oral cavity.The acquired enamel pellicle (EP) is a protein film thought to result from the selective adsorption of precursor proteins present in WS onto tooth surfaces. Because of its intimate contact with enamel surfaces, the EP plays an important role in maintaining tooth integrity by controlling the mineral solution dynamics of enamel. At its interface with the oral environment, the EP exerts selectivity on bacterial attachment and is involved in the initial stages of plaque formation (14). Because of the limiting amount of proteins that can be harvested from EP formed in vivo, previous investigations have utilized sensitive but indirect approaches such as enzymatic assays and immunologic detectio...

show abstract

“…Tissue samples used for ISH and IHC were thawed on ice, fixed in 4% paraformaldehyde at 4C overnight, embedded in paraffin, sectioned, and mounted on microscope slides. Buccal epithelial cells were obtained from whole saliva sediment as described (Yao et al 2000). These studies were approved by the Institutional Review Board at Boston University Medical Center.…”

Section: Tissue Samplesmentioning

confidence: 99%

Expression of Membrane-associated Mucins MUC1 and MUC4 in Major Human Salivary Glands

Liu

Lague

Nunes

et al. 2002

J Histochem Cytochem.

View full text Add to dashboard Cite

Mucins are high molecular weight glycoproteins secreted by salivary glands and epithelial cells lining the digestive, respiratory, and reproductive tracts. These glycoproteins, encoded in at least 13 distinct human genes, can be subdivided into gel-forming and membrane-associated forms. The gel-forming mucin MUC5B is secreted by mucous acinar cells in major and minor salivary glands, but little is known about the expression pattern of membrane-associated mucins. In this study, RT-PCR and Northern blotting demonstrated the presence of transcripts for MUC1 and MUC4 in both parotid and submandibular glands, and in situ hybridization localized these transcripts to epithelial cells lining striated and excretory ducts and in some serous acinar cells. The same cellular distribution was observed by immunohistochemistry. Soluble forms of both mucins were detected in parotid secretion after immunoprecipitation with mucin-specific antibodies. These studies have shown that membrane-associated mucins are produced in both parotid and submandibular glands and that they are expressed in different cell types than gel-forming mucins. Although the function of these mucins in the oral cavity remains to be elucidated, it is possible that they both contribute to the epithelial protective mucin layer and act as receptors initiating one or more intracellular signal transduction pathways.

show abstract

Pellicle Precursor Protein Crosslinking: Characterization of an Adduct between Acidic Proline-rich Protein (PRP-1) and Statherin Generated by Transglutaminase

Cited by 43 publications

References 30 publications

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

Peptide profile of human acquired enamel pellicle using MALDI tandem MS

Identification of Protein Components in Human Acquired Enamel Pellicle and Whole Saliva Using Novel Proteomics Approaches

Expression of Membrane-associated Mucins MUC1 and MUC4 in Major Human Salivary Glands

Contact Info

Product

Resources

About