Dataset Information

Human salivary basic proline-rich proteins

ABSTRACT: Human basic proline-rich proteins and basic glycosylated proline-rich proteins are the most complex family of human adult salivary proteins, secreted only by the parotid gland, expressed by the polymorphic PRB1-4 genes. This study reports the results obtained for their characterization in our laboratory utilizing integrated top-down and bottom-up HPLC-ESI-MS and MS/MS platform. The family include 11 parent peptides/proteins and more than 6 parent glycosylated proteins. Despite the complexity, on the basis of their primary structure they result the product of the duplication of three repeats and we propose that they can be classified in two main groups, the first including the peptides called P-E, P-Ko, IB-6, Ps-1, Ps-2, P-H, P-F, P-J, and P-D, the second including the peptides called IB-1, II-2 and the glycosylated basic proline-rich proteins codified by PRB3 and PRB4 genes. A third minor hybrid group includes the proteins called IB-8a Con1- and Con1+. Some of the proteins of the family (IB-1, II-2 and P-J) are almost always detectable in adult human saliva, while the others are expressed with different frequencies according to the phenotype. Various isoforms are detectable in the adult saliva and three of them, until now not reported (P-H S1→A, P-Ko P36→S, P-Ko A41→S), were characterized by MS/MS fragmentation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Saliva

SUBMITTER: Barbara Manconi

LAB HEAD: Tiziana Cabras

PROVIDER: PXD009813 | Pride | 2018-08-08

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	CSM001_Roma_HCD_250915.raw	Raw
	CSM002_Roma_HCD_250915.raw	Raw
	CSM003_Roma_HCD_250915.raw	Raw
	CSM004_Roma_HCD_250915.raw	Raw
	CSM005_Roma_HCD_250915.raw	Raw

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Publications

Extensive Characterization of the Human Salivary Basic Proline-Rich Protein Family by Top-Down Mass Spectrometry.

Padiglia Alessandra A Orrù Roberto R Boroumand Mozhgan M Olianas Alessandra A Manconi Barbara B Sanna Maria Teresa MT Desiderio Claudia C Iavarone Federica F Liori Barbara B Messana Irene I Castagnola Massimo M Cabras Tiziana T

Journal of proteome research 20180820 9

Human basic proline-rich proteins and basic glycosylated proline-rich proteins, encoded by the polymorphic PRB1-4 genes and expressed only in parotid glands, are the most complex family of adult salivary proteins. The family includes 11 parent peptides/proteins and more than 6 parent glycosylated proteins, but a high number of proteoforms with rather similar structures derive from polymorphisms and post-translational modifications. 55 new components of the family were characterized by top-down l ...[more]

PMID: 30064219

Similar Datasets

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.