|Titolo:||Top-down proteomics for the investigation of saliva during human development|
|Data di pubblicazione:||2014|
|Abstract:||Aim of this study was to evaluate by a label-free top-down proteomic platformsvariations during human development of the level of different proteins detectable in adult saliva and their post-translational modifications (PTMs). The relative amounts of different proteoforms of acidic-proline-rich proteins (aPRPs), basic proline-rich proteins, statherin, histatins 1, 3, 5 and 6, cystatin S, S1, S2, SA and SN and S100A9 were measured in 312 samples (111 serially collected from 17 preterm newborns at different post-conceptional age (PCA), 178 from subjects aged between 0 and 18 years, and 23 from adults). The different proteoforms of these protein families were expressed according to this order: aPRPs(PRH2 locus) and g-PRP(PRB3 locus)before 195 days of PCA; histatin 1 and statherin at 210-220 days of PCA; aPRPs (PRH1 locus)at normal term of delivery (270-280 days of PCA); cystatin S proteoforms after normal term of delivery;bPRPs (PRB1, PRB2 and PRB4 loci) later, reaching adult levels after puberty .All S100A9 proteoformswere highly abundant in pre-term newborn saliva, their concentration decreasing as a function of PCA . The PTMsevaluation of various proteoforms highlighted that the Golgi casein kinase (Fam20C ), responsible for the aPRPs, histatin 1, statherin and cystatin Sphosphorylation, is poorly active during fetal development. The p38 mitogen-activated protein kinase 14(MAPK14) responsible for S100A9 phosphorylation, the convertases, thecarboxy-peptidases, themethionine aminopeptidasesand N-terminal-acetyl-transferasesresponsible for the cleavage and processing of different proteins (aPRPs, bPRPs, histatins, S100A9) during secretionare fully active before 195 days of PCA.|
|Tipologia:||4.2 Abstract in Atti di convegno|
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