Dataset Information

Salivary proteomics of sP and sNP rats

ABSTRACT: Sardinian alcohol-preferring (sP) and Sardinina alcohol-non preferring (sNP) rats have been selectively bred for opposite alcohol preference and consumption. The project proposed to identify salivary markers distinguishing the two rat lines possibly correlated to alcohol preference, by a proteomic approach.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Saliva

DISEASE(S): Disease Free

SUBMITTER: Tiziana Cabras

LAB HEAD: Tiziana Cabras

PROVIDER: PXD006997 | Pride | 2017-11-03

REPOSITORIES: Pride

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Publications

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.

Cabras Tiziana T D'Alessandro Alfredo A Serrao Simone S Isola Raffaella R Iavarone Federica F Vincenzoni Federica F Colombo Giancarlo G Ekström Jörgen J Messana Irene I Castagnola Massimo M

Journal of proteome research 20171116 1

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 ...[more]

PMID: 29083190

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Project description:Due to the distinctive features of oral mucosa, determination of the proteins involved in the formation of “oral protein pellicle” is demanding. The present study investigated the susceptibility of several human basic proline-rich peptides (bPRPs) named P-H, P-D, P-F, P-J, and II-2 as substrates of transglutaminase-2. The reactivity of P-C peptide and statherin was also investigated. Peptides purified from human whole saliva were incubated at diverse temperatures with two different transglutaminases (type 2; guinea pig and human), in the presence or in the absence of monodansyl-cadaverine. High resolution HPLC-ESI-MS and MS/MS analyses of the reaction products highlighted that P-H, and P-D were active substrates of transglutaminase-2, II-2 was less reactive and the reactivity of P-F and P-J was negligible. All the peptides formed cyclo-derivatives, and only specific glutamine residues were involved in the cycle formation and reacted with monodansyl-cadaverine. Q29 for P-H, Q37 for P-D, and Q21 for II-2 were the principal reactive residues. One or two secondary glutamine residues were hierarchically susceptible to reaction with dansyl-cadaverine. The main consensus sequence recognized by transglutaminase-2 in basic proline-rich peptides was GNPQ, and, despite the great similarity of P-F and P-J with the other salivary peptides, their reactivity was negligible, probably because the GNPQ consensus sequence was missing in their sequence. The reactivity of P-D A32 variant was lower than that of P-D P32 peptide suggesting that the more rigid peptide structure was a better substrates for transglutaminase-2. The reactivity of P-C was high, but followed rules different from the other basic peptides under study, Q41 being the principal reactive residue, confirming that P-C is not strictly related to the basic proline-rich proteins. The reactivity of statherin was very high too, and the manual inspection of the MS/MS fragmentation patterns of the reaction products confirmed, as determined in previous studies, that Q37 is the pivotal residue, Q39 and Q40 the secondary residues recognized by transglutaminase-2. Moreover, Q39 and Q40 residues were more reactive in cyclo-statherin Q37 than in statherin, suggesting that cycle formation increases the reactivity of the secondary glutamine residues. Finally, the physiological temperature (37°C) was the best for the reaction and no significant qualitative differences were observed using human or guinea pig transglutaminase-2.

Dataset Information

Salivary proteomics of sP and sNP rats

Publications

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.

Similar Datasets

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