Revealing the Amylase Interactome in Whole Saliva Using Proteomic Approaches.

Understanding proteins present in saliva and their function when isolated is not enough to describe their real role in the mouth. Due to protein-protein interactions, structural changes may occur in macromolecules leading to functional modulation or modification. Besides amylase’s function in carboh...

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Publicado en:BioMed Research International Vol. 2018; pp. 1 - 16
Autores principales: Crosara, Karla Tonelli Bicalho, Zuanazzi, David, Moffa, Eduardo Buozi, Xiao, Yizhi, Machado, Maria Aparecida de Andrade Moreira, Siqueira, Walter Luiz
Formato: research tables/charts Journal Article
Publicado: Wiley-Blackwell 1/31/2018
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 1/31/2018
      vid: 2018
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        10.1155/2018/6346954
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        atl: Revealing the Amylase Interactome in Whole Saliva Using Proteomic Approaches.
      aug:
        au:
          Crosara, Karla Tonelli Bicalho
          Zuanazzi, David
          Moffa, Eduardo Buozi
          Xiao, Yizhi
          Machado, Maria Aparecida de Andrade Moreira
          Siqueira, Walter Luiz
        affil: Schulich Dentistry and Department of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, ON, Canada
      sug:
        subj:
          Proteomics
          Amylases Physiology
          Saliva
          Human
          Molecular Biology
          Cell Physiology
          Carrier Proteins Physiology
          Chromatography
          Electrophoresis, Gel, Pulsed-Field
          Sodium Compounds
          Mass Spectrometry
          Interaction (Research)
          Data Analysis Software
      ab: Understanding proteins present in saliva and their function when isolated is not enough to describe their real role in the mouth. Due to protein-protein interactions, structural changes may occur in macromolecules leading to functional modulation or modification. Besides amylase’s function in carbohydrate breakdown, amylase can delay proteolytic degradation of protein partners (e.g., histatin 1) when complexed. Due to its biochemical characteristics and high abundance in saliva, amylase probably interacts with several proteins acting as a biological carrier. This study focused on identifying interactions between amylase and other proteins found in whole saliva (WS) using proteomic approaches. Affinity chromatography was used, followed by gel electrophoresis methods, sodium dodecyl sulfate and native, tryptic in-solution and in-gel digestion, and mass spectrometry. We identified 66 proteins that interact with amylase in WS. Characterization of the identified proteins suggests that acidic (pI < 6.8) and low molecular weight (MW < 56 kDa) proteins have preference during amylase complex formation. Most of the identified proteins present biological functions related to host protection. A new protein-amylase network was constructed using the STRING database. Further studies are necessary to investigate individualities of the identified amylase interactors. These observations open avenues for more comprehensive studies on not yet fully characterized biological function of amylase.
      pubtype: Academic Journal
      doctype:
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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