Age-Dependent Modifications of the Human Salivary Secretory Protein Complex

Cabras, Tiziana; Pisano, Elisabetta; Boi, Roberto; Olianas, Alessandra; Manconi, Barbara; Inzitari, Rosanna; Fanali, Chiara; Giardina, Bruno; Castagnola, Massimo; Messana, Irene

doi:10.1021/pr900212u

Cited by 85 publications

(72 citation statements)

References 45 publications

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“…As previously shown, precipitation did not affect significantly the quali/quantitative profile of acid-soluble proteins (23). Levels of salivary proteins and naturally occurring peptides were determined by HPLC-ESI-MS analysis, and the typical chromatographic profile obtained under our experimental conditions in the two groups under study is shown in Figure 1.…”

Section: Resultssupporting

confidence: 53%

“…In a previous work devoted to the investigation of the influence of the age on salivary protein composition, we evidenced that the expression of basic PRPs is age-related and that these salivary proteins reach the concentration found in adults only after puberty (12-17 years of age) (23). Since the age of the subjects enrolled for this study was comprised between 7-18 years, basic PRPs (bPRPs) were not considered in the present investigation.…”

Section: Discussionmentioning

confidence: 95%

“…The XIC analysis selectively reveals a protein in the chromatographic profile by extracting the ion current associated with the multiply charged ions characteristic of the protein. The ions used to quantify the proteins/peptides were carefully selected to exclude values in common with other co-eluting proteins, and, with the exception of S100A8 and S100A9* isoforms and the new fragments characterized in this work, they were reported previously (16,19,23). The following ions were used to quantify S100A8 and S100A9* isoforms: S100A8, 985.9 (ϩ11), 1084.4 (ϩ10), 1204.8 (ϩ9), and 1355.3 m/z (ϩ8); S100A9* nonphosphorylated, 977.2 (ϩ13), 1058.5 (ϩ12), 1154.6 (ϩ11), 1270.0 (ϩ10), 1411.0 (ϩ9); S100A9* phosphorylated, 983.3(ϩ13), 1065.2 (ϩ12), 1161.9 (ϩ11), 1278.0 (ϩ10), 1419.9 (ϩ9); S100A9* nonphosphorylated oxidized, 978.4 (ϩ13), 1059.8 (ϩ12), 1156.1 (ϩ11), 1271.6 (ϩ10), 1412.8 (ϩ9); S100A9* phosphorylated oxidized, 984.5 (ϩ13), 1066.5 (ϩ12), 1163.4 (ϩ11), 1279.6 (ϩ10), 1421.7 (ϩ9).…”

Section: Hplc-esi-it-ms Analysis-mentioning

confidence: 99%

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Alterations of the Salivary Secretory Peptidome Profile in Children Affected by Type 1 Diabetes

Cabras

Pisano

Mastinu

et al. 2010

Molecular & Cellular Proteomics

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The acidic soluble fraction of whole saliva of type 1 diabetic children was analyzed by reversed phase (RP) 1 -HPLC-ESI-MS and compared with that of sex-and age-matched control subjects. Salivary acidic proline-rich phosphoproteins (aPRP), histatins, ␣-defensins, salivary cystatins, statherin, proline-rich peptide P-B (P-B), betathymosins, S100A8 and S100A9*(S100A9* corresponds to S100A9 vairant lacking the first four amino acids), as well some naturally occurring peptides derived from salivary acidic proline-rich phosphoproteins, histatins, statherin, and P-B peptide, were detected and quantified on the basis of the extracted ion current peak area. The level of phosphorylation of salivary acidic proline-rich phosphoproteins, histatin-1 (Hst-1), statherin and S100A9* and the percentage of truncated forms of salivary acidic proline-rich phosphoproteins was also determined in the two groups. The study revealed that statherin, proline-rich peptide P-B, P-C peptide, and histatins, were significantly less concentrated in saliva of diabetic subjects than in controls, while concentration of ␣-defensins 1, 2 and 4 and S100A9* was higher. The low concentration of P-C peptide was paralleled by high levels of some of its fragments. On the whole, the study highlighted the severe impairment of the repertoire of peptides involved in the safeguard of the oral cavity in children who have diabetes, as well as an higher concentration of the proinflammatory mediator S100A9* with respect to healthy children. Molecular & Cellular Proteomics 9:2099 -2108, 2010.Type 1 diabetes mellitus is a disease with universal distribution, affecting all populations (1) with an incidence increasing in Europe (2). Because type 1 diabetes involves many organs and tissues, signs and symptoms of diabetes can occur in the oral cavity. Indeed, several studies have shown that the prevalence, severity, and progression of periodontal diseases are significantly increased in diabetics, and the pathology is considered an important risk factor for periodontitis (3). The study of Lalla et al. (4) showed an association between diabetes and the increased risk for periodontal destruction even very early in life. Flow rate and composition of saliva are crucial for the maintenance of oral cavity health, and both have been found altered in diabetic subjects, although with contradictory findings. For instance, several studies reported a reduced resting salivary flow rate in adults and children who have type 1 diabetes with respect to healthy subjects (5-10), but it was also observed that stimulated saliva of diabetics and controls did not significantly differ (11,12). Total protein concentration of saliva was found either increased or not affected by the diabetic status. Lopez et al. (9) reported higher urea and total protein salivary content in diabetic children than in controls. Conversely, a study on 35 adult insulin-dependent diabetics demonstrated that they did not show a decreased saliva concentration of several innate antimicrobial factors (lysozyme, lactoferri...

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Section: Resultssupporting

confidence: 53%

Section: Discussionmentioning

confidence: 95%

Section: Hplc-esi-it-ms Analysis-mentioning

confidence: 99%

See 1 more Smart Citation

Alterations of the Salivary Secretory Peptidome Profile in Children Affected by Type 1 Diabetes

Cabras

Pisano

Mastinu

et al. 2010

Molecular & Cellular Proteomics

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“…In a previous study (6), we have established that some salivary proteins and peptides reach the levels typically observed in the adult around 18 years of age. Encouraged by the noninvasive specimen collection, we explored the salivary protein composition of at-term and preterm newborns, in order to establish the starting point of the secretion of the proteins and peptides specific of saliva.…”

mentioning

confidence: 77%

The Surprising Composition of the Salivary Proteome of Preterm Human Newborn

Castagnola

Inzitari²,

Fanali³

et al. 2011

Molecular & Cellular Proteomics

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Saliva is a body fluid of a unique composition devoted to protect the mouth cavity and the digestive tract. Our high performance liquid chromatography (HPLC)-electrospray ionization-MS analysis of the acidic soluble fraction of saliva from preterm human newborn surprisingly revealed more than 40 protein masses often undetected in adult saliva. We were able to identify the following proteins: stefin A and stefin B, S100A7 (two isoforms), S100A8, S100A9 (four isoforms), S100A11, S100A12, small proline-rich protein 3 (two isoforms), lysozyme C, thymosins ␤ 4 and ␤ 10 , antileukoproteinase, histone H1c, and ␣ and ␥ globins. The average mass value reported in international data banks was often incongruent with our experimental results mostly because of post-translational modifications of the proteins, e.g. acetylation of the N-terminal residue. A quantitative label-free MS analysis showed protein levels altered in relation to the postconceptional age and suggested coordinate and hierarchical functions for these proteins during development. In summary, this study shows for the first time that analysis of these proteins in saliva of preterm newborns might represent a noninvasive way to obtain precious information of the molecular mechanisms of development of human fetal oral structures. Molecular & Cellular Proteomics 10: 10.1074/mcp.M110.003467, 1-14, 2011.Saliva is a body fluid of a very complex and specific composition devoted to the protection and well-being of the oral cavity and, because it is swallowed, of the digestive tract (1). Protection is ensured by organic and inorganic solutes and specific peptides and proteins, such as acidic and basic proline-rich proteins, ␣-amylases, salivary cystatins, histatins, and statherin (2-5). In a previous study (6), we have established that some salivary proteins and peptides reach the levels typically observed in the adult around 18 years of age. Encouraged by the noninvasive specimen collection, we explored the salivary protein composition of at-term and preterm newborns, in order to establish the starting point of the secretion of the proteins and peptides specific of saliva. Our first study (7) showed that acidic proline-rich proteins secretion started, although at very low levels, at 7 months of postconceptional age. At this age the level of phosphorylation of these proteins was low and it increased reaching a value comparable with that of adults at about one year of age, in concomitance with the beginning of deciduous dentition. Other deep differences between human and preterm saliva were however evident. Highly abundant protein masses detected in preterm saliva were undetectable (at the sensitivity level of our MS apparatus) or at very low level in adult saliva. In a previous study (8) we identified, by different MS approaches, thymosin ␤ 4 (T␤ 4 ) and thymosin ␤ 10 (T␤ 10 ) in preterm newborn saliva and established by immunohistochemistry their presence in fetal salivary glands. This finding let us to suppose that in preterm newborns these peptides derived from glan...

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“…This process leads to great variation in the peptide profile and thus limits the reproducibility of peptidomic analyses. Other preanalytical variables, such as sex, age, diet, and circadian rhythms, can also play important roles in the peptide composition of saliva (29 ). Despite these shortcomings, peptidomic analyses of saliva have been used to assess a variety of pathologies, including Sjögren syndrome, xerostomia, and diabetes (30 ).…”

Section: Peptidomics Of Salivamentioning

confidence: 99%

Peptidomics of Urine and Other Biofluids for Cancer Diagnostics

2014

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BACKGROUND:Cancer is a leading cause of death worldwide. The low diagnostic sensitivity and specificity of most current cancer biomarkers make early cancer diagnosis a challenging task. The comprehensive study of peptides and small proteins in a living system, known as "peptidomics," represents an alternative technological approach to the discovery of potential biomarkers for the assessment of a wide variety of pathologies. This review examines the current status of peptidomics for several body fluids, with a focus on urine, for cancer diagnostics applications.CONTENT: Several studies have used high-throughput technologies to characterize the peptide content of different body fluids. Because of its noninvasive collection and high stability, urine is a valuable source of candidate cancer biomarkers. A wide variety of preanalytical issues concerning patient selection and sample handling need to be considered, because not doing so can affect the quality of the results by introducing bias and artifacts. Optimization of both the analytical strategies and the processing of bioinformatics data is also essential to minimize the false-discovery rate.

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Age-Dependent Modifications of the Human Salivary Secretory Protein Complex

Cited by 85 publications

References 45 publications

Alterations of the Salivary Secretory Peptidome Profile in Children Affected by Type 1 Diabetes

Alterations of the Salivary Secretory Peptidome Profile in Children Affected by Type 1 Diabetes

The Surprising Composition of the Salivary Proteome of Preterm Human Newborn

Peptidomics of Urine and Other Biofluids for Cancer Diagnostics

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