title: Complexity of the human whole saliva proteome.
abstract: Recent characterization of the whole saliva proteome led to contradictory pictures concerning the complexity of its proteome. In this work, 110 proteins were analysed by mass spectrometry allowing the identification of 10 accessions previously not detected on protein two-dimensional maps, including myosin heavy chain (fast skeletal muscle, IIA and IIB), phosphatidylethanolamine binding protein, secretory actin-binding protein precursor and triosephosphate isomerase. Further comparison with available data demonstrated simultaneously a low diversity in terms of variety of accessions and a high complexity in terms of number of protein spots identifying the same accession, the two thirds of identified spots corresponding to amylases, cystatins and immunoglobulins. This diversity may be of interest in the development of non invasive diagnostic tool for several disease.
authors.affiliation: Laboratory of Physiology, UFR d'Odontologie, Université Montpellier 1, France. christophe.hirtz@univ-montp1.fr
authors.forename: C
authors.initials: C
authors.lastname: Hirtz
authors.forename: F
authors.initials: F
authors.lastname: Chevalier
authors.forename: D
authors.initials: D
authors.lastname: Centeno
authors.forename: J C
authors.initials: JC
authors.lastname: Egea
authors.forename: M
authors.initials: M
authors.lastname: Rossignol
authors.forename: N
authors.initials: N
authors.lastname: Sommerer
authors.forename: Deville
authors.initials: D
authors.lastname: de Périère
mesh_terms: D030562:Databases, Protein; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D020543:Proteome; D012463:Saliva / Q000737:chemistry*; D012471:Salivary Proteins and Peptides / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D020543:Proteome; D012471:Salivary Proteins and Peptides