title: Analysis of age and gender associated N-glycoproteome in human whole saliva.
abstract: BACKGROUND
  Glycoproteins comprise a large portion of the salivary proteome and have great potential for biomarker discovery and disease diagnosis. However, the rate of production and the concentration of whole saliva change with age, gender and physiological states of the human body. Therefore, a thorough understanding of the salivary glycoproteome of healthy individuals of different ages and genders is a prerequisite for saliva to have clinical utility.
  
  
  METHODS
  Formerly N-linked glycopeptides were isolated from the pooled whole saliva of six age and gender groups by hydrazide chemistry and hydrophilic affinity methods followed by mass spectrometry identification. Selected physiochemical characteristics of salivary glycoproteins were analyzed, and the salivary glycoproteomes of different age and gender groups were compared based on their glycoprotein components and gene ontology.
  
  
  CONCLUSIONS
  Among 85 N-glycoproteins identified in healthy human saliva, the majority were acidic proteins with low molecular weight. The numbers of salivary N-glycoproteins increased with age. Fifteen salivary glycoproteins were identified as potential age- or gender-associated glycoproteins, and many of them have functions related to innate immunity against microorganisms and oral cavity protection. Moreover, many salivary glycoproteins have been previously reported as disease related glycoproteins. This study reveals the important role of salivary glycoproteins in the maintenance of oral health and homeostasis and the great potential of saliva for biomarker discovery and disease diagnosis.
authors.affiliation: Laboratory of Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, P.R. China.
authors.forename: Shisheng
authors.initials: S
authors.lastname: Sun
authors.affiliation: Laboratory of Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, P.R. China.
authors.forename: Fei
authors.initials: F
authors.lastname: Zhao
authors.affiliation: Laboratory of Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, P.R. China.
authors.forename: Qinzhe
authors.initials: Q
authors.lastname: Wang
authors.affiliation: Laboratory of Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, P.R. China.
authors.forename: Yaogang
authors.initials: Y
authors.lastname: Zhong
authors.affiliation: Laborotary of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China.
authors.forename: Tanxi
authors.initials: T
authors.lastname: Cai
authors.affiliation: Laborotary of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China.
authors.forename: Peng
authors.initials: P
authors.lastname: Wu
authors.affiliation: Laborotary of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China.
authors.forename: Fuquan
authors.initials: F
authors.lastname: Yang
authors.affiliation: Laboratory of Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, P.R. China.
authors.forename: Zheng
authors.initials: Z
authors.lastname: Li
keywords: Age; Gender; Glycoproteins; Glycoproteome; Hydrazide chemistry; Hydrophilic affinity; Mass spectrometry; Saliva