Identification and characterization of histatin 1 salivary complexes by using mass spectrometry

Proteomics. 2012 Nov;12(22):3426-35. doi: 10.1002/pmic.201100665.

Abstract

With recent progress in the analysis of the salivary proteome, the number of salivary proteins identified has increased dramatically. However, the physiological functions of many of the newly discovered proteins remain unclear. Closely related to the study of a protein's function is the identification of its interaction partners. We investigated interactions among and functions of histatin 1 and the other proteins that are present in saliva by using high-throughput mass spectrometric techniques. This led to the identification of 43 proteins able to interact with histatin 1. In addition, we found that these protein-protein interactions protect complex partners from proteolysis and modulate their antifungal activity. Our data contribute significantly to characterization of the salivary interactome and to understanding the biology of salivary protein complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Amylases / metabolism
  • Analysis of Variance
  • Antifungal Agents / chemistry
  • Antifungal Agents / metabolism
  • Antifungal Agents / pharmacology
  • Candida / drug effects
  • Female
  • Histatins / chemistry
  • Histatins / metabolism*
  • Histatins / pharmacology
  • Humans
  • Hydrolysis
  • Male
  • Mass Spectrometry / methods*
  • Molecular Sequence Data
  • Peptide Fragments / analysis
  • Peptide Fragments / chemistry
  • Protein Interaction Mapping
  • Proteome / analysis
  • Proteome / chemistry
  • Proteome / metabolism
  • Saliva / chemistry*
  • Salivary Proteins and Peptides / analysis*
  • Salivary Proteins and Peptides / chemistry
  • Salivary Proteins and Peptides / classification
  • Salivary Proteins and Peptides / metabolism*
  • Starch / metabolism

Substances

  • Antifungal Agents
  • Histatins
  • Peptide Fragments
  • Proteome
  • Salivary Proteins and Peptides
  • HTN1 protein, human
  • Starch
  • Amylases