| 1. |
- Cabras, T., et al.
(författare)
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Proteomics of the acid-soluble fraction of whole and major gland saliva in burning mouth syndrome patients
- 2019
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Ingår i: Archives of Oral Biology. - : Elsevier BV. - 0003-9969. ; 98, s. 148-155
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Tidskriftsartikel (refereegranskat)abstract
- Objective: In the present study the salivary proteome of burning mouth syndrome patients and healthy subjects was characterized by a top-down proteomic approach and compared to highlight possible qualitative and quantitative differences that may give suggestions about the causes of this pathology which are still unknown. Materials and methods: Resting and stimulated whole saliva, stimulated parotid and submandibular/sublingual saliva samples were collected from burning mouth syndrome patients (n = 16) and age- and gender-matched healthy subjects (n = 14). An equal volume of 0.2% trifluoroacetic acid was added to each sample immediately after collection and the supernatants were analysed by liquid chromatography coupled to electrospray-ionisation mass spectrometry. Proteins and peptides were quantified using a label-free approach measuring the extracted ion current peak areas of the main salivary proteins and peptides. Results: The quantitation of the main salivary proteins and peptides revealed a higher concentration of cystatin SN in resting saliva of burning mouth syndrome patients with respect to healthy controls and no other conspicuous changes. Conclusions: The reported data showed that the salivary protein profile was not affected, in composition and relative abundance, by the burning mouth syndrome, except for the cystatin SN, a protein up-regulated in several pathological conditions, that might be considered potentially indicative of the disease. © 2018
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| 2. |
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| 3. |
- Cabras, T., et al.
(författare)
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Marked Differences in the Submandibular Salivary Proteome between Sardinian Alcohol-Preferring and Sardinian Alcohol-Non Preferring Rats Revealed by an Integrated Top-Down-Bottom-Up Proteomic Platform
- 2018
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Ingår i: Journal of Proteome Research. - : American Chemical Society (ACS). - 1535-3893 .- 1535-3907. ; 17:1, s. 455-469
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Tidskriftsartikel (refereegranskat)abstract
- Sardinian alcohol-preferring (sP) and Sardinian alcohol-non preferring (sNP) rats have been selectively bred for opposite alcohol preference and consumption. Aiming to verify possible differences at the proteomics level between sP and sNP rats, we investigated the salivary proteome by a a liquid chromatography-mass spectrometry top-down-bottom-up integrated approach. For this purpose, submandibular saliva was collected from alcohol-naive sP and sNP rats under isoprenaline stimulation. A total of 200 peptides and proteins were detected and quantified in the two rat lines, 149 of which were characterized in their naturally occurring structure. The data are available via ProteomeXchange with identifier PXD006997. Surprisingly, sP rats exhibited marked quantitative and qualitative differences with respect to sNP rats, namely higher levels of proteoforms originating from submandibular gland protein C, and from submandibular rat protein 2, as well as those of several unidentified peptides and proteins. sP rats expressed some proteins not detectable in sNP rats such as the glutamine and glutamic acid-rich protein (GRP)-CB. The isoform GRP-B, detectable in both rat lines, was more abundant in sNP rats. The submandibular saliva of sNP rats was also characterized by very high levels of GRP-B proteolytic peptides and rat salivary protein 1. Whether these differences could contribute to the opposite alcohol preference and consumption of sP and sNP rats is currently unknown and requires further investigation. © 2017 American Chemical Society.
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| 4. |
- Cabras, T., et al.
(författare)
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Top-down HPLC-ESI-MS characterization of rat gliadoralin A, a new member of the family of rat submandibular gland glutamine-rich proteins and potential substrate of transglutaminase
- 2013
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Ingår i: Journal of Separation Science. - : Wiley. - 1615-9306. ; 36:17, s. 2848-2861
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Tidskriftsartikel (refereegranskat)abstract
- During HPLC-ESI-MS/MS analysis of rat submandibular saliva secreted under isoprenaline stimulation, a protein with an experimental [M+H](1+) = 10544.24 m/z was detected (17.5 +/- 0.7 min). The MS/MS fragmentation pattern, manually investigated, allowed establishing an internal sequence in agreement with a DNA-derived sequence of an unknown rat protein coded D3Z9M3 (Swiss-Prot). To match the experimental MS/MS fragmentation pattern and protein mass with theoretical data, the removal from the N terminus of the signal peptide and from the C terminus of three amino acid (a.a.) residues (Arg-Ala-Val) and the cyclization of the N-terminal glutamine in pyroglutamic had to be supposed, resulting in a mature protein of 90 a.a. HPLC-ESI-MS/MS of the trypsin digest ensured 100% sequence coverage. For the high glutamine content (34/90 = 37.8%) we propose to name this protein rat gliadoralin A 1-90. Low amounts of five different isoforms were sporadically detected, which did not significantly change their relative amounts after stimulation. Gliadoralin A is substrate for transglutaminase-2, having Lys 60 and different Gln residues as major determinants for enzyme recognition. In silico investigation of superior structures evidenced that a small part of the protein adopts an -helical fold, whereas large segments are unfolded, suggesting an unordered conformation.
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| 5. |
- Nemolato, S., et al.
(författare)
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Immunoreactivity for thymosin beta 4 and thymosin beta 10 in the adult rat oro-gastrointestinal tract
- 2013
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Ingår i: European Journal of Histochemistry. - : PAGEPress Publications. - 1121-760X .- 2038-8306. ; 57:2, s. 106-111
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Tidskriftsartikel (refereegranskat)abstract
- Thymosin beta 4 (T beta 4) and thymosin beta 10 (T beta 10) are two members of the beta-thymosin family, involved in multiple cellular activities in different organs in multiple animal species. Here we report the expression pattern of T beta 4 and T beta 10 in rat tissues, in the gut and in annexed glands. The two peptide were differently expressed: T beta 4 was absent in salivary glands whereas T beta 10 was expressed in parotid and in submandibular glands. T beta 4 was mildly expressed in the tongue and in the oesophagus, where T beta 10 was absent. A similar expression was found in the stomach, ileum and colon mucosa. In pancreas T beta 4 reactivity was restricted to the Langerhans islet cells; T beta 4 was also detected in the exocrine cells. Both peptide were not expressed in liver cells. When the rat expression pattern in rat organs was compared to reactivity for T beta 4 and T beta 10 in humans, marked differences were found. Our data clearly indicate a species-specific expression of T beta 4 and T beta 10, characterized by the actual unpredictability of the expression of these peptides in different cells and tissues. The common high expression of T beta 4 in mast cells, both in humans and in rats, represents one of the few similarities between these two species.
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