Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us?

Messana, Irene; Inzitari, Rosanna; Fanali, Chiara; Cabras, Tiziana; Castagnola, Massimo

doi:10.1002/jssc.200800100

Cited by 131 publications

(142 citation statements)

References 79 publications

(88 reference statements)

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“…In addition, mucin-5B was abundant in exosome I. Whereas alpha-amylase (about 20% in weight of salivary proteins) and proline-rich proteins (about 40% in weight of salivary proteins), both abundant protein components in whole saliva, 32) only a small amount or none of these proteins were detected in exosome I and exosome II. In contrast, carbonic anhydrase 6 and cystatin family proteins are also extracellularly secreted proteins that are minor components in whole salivary proteins, but distinct amounts of these proteins were detected in exosome II.…”

Section: Discussionmentioning

confidence: 96%

Proteomic Analysis of Two Types of Exosomes in Human Whole Saliva

Ogawa

Miura

Harazono³

et al. 2011

Biological & Pharmaceutical Bulletin

217

174

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Section: Discussionmentioning

confidence: 96%

Proteomic Analysis of Two Types of Exosomes in Human Whole Saliva

Ogawa

Miura

Harazono³

et al. 2011

Biological & Pharmaceutical Bulletin

217

174

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“…The more acidic spots would therefore correspond to more phosphorylated isoforms. Although post-translational modifications are extremely frequent in salivary proteins (Helmerhorst and Oppenheim 2007;Messana et al 2008), regulation or functionality of more or less phosphorylated PIPs is still unknown (Vitorino et al 2004). It is therefore unclear why urea would favor phosphorylation of PIPs.…”

Section: Discussionmentioning

confidence: 98%

Short-Term Modification of Human Salivary Proteome Induced by Two Bitter Tastants, Urea and Quinine

Quintana

Palicki

Lucchi³

et al. 2009

Chem. Percept.

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Salivary proteome patterns of healthy volunteers (n=12) were compared before and after they tasted bitter solutions made of either urea (0.36M) or quininehydrochloride (40 µM). Relative abundance of 22 and 18 spots was modified 15 min after stimulation by urea and quinine, respectively. Only two spots were common to both tastants, indicating a molecule-specific response. Proteins, relative quantity of which was altered, were agents of the oral cavity defense (e.g., thioredoxin, cystatin, parotid secretory proteins, etc.) and markers of inflammation (transthyretin and transferrin) or enzymes. In particular, the relative abundance of carbonic anhydrase VI, a protein previously described as crucial to taste function, declined after tasting the urea solution.

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“…Under constant analytical conditions, the area of the XIC peaks is proportional to the peptide/ protein concentration (21,22). 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.…”

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

confidence: 99%

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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Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us?

Cited by 131 publications

References 79 publications

Proteomic Analysis of Two Types of Exosomes in Human Whole Saliva

Proteomic Analysis of Two Types of Exosomes in Human Whole Saliva

Short-Term Modification of Human Salivary Proteome Induced by Two Bitter Tastants, Urea and Quinine

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

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