Posttranslational modification of indoleamine 2,3-dioxygenase

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Protein posttranslational modifications (PTMs) perform essential roles in the biological regulation of a cell. PTMs are extremely important because they can change a protein's physical or chemical properties, conformation, activity, cellular location, or stability. In fact, most proteins are altered by the addition or removal of a chemical moiety on either an amino acid or the protein's N- or C-terminus. Some PTMs can be added and removed dynamically as a mechanism for reversibly controlling protein function. Thus, identifying the PTM sites is critical to fully understand the biological roles of any given protein. Mass spectrometry (MS) is a widely used analytical strategy to identify PTMs. We have used an automated two-dimensional liquid chromatography (LC) system coupled with electrospray ionization quadrupole ion-trap MS to identify PTMs for indoleamine 2,3-dioxygenase 1 (IDO1), one of the tryptophan catabolic enzymes. IDO1 promotes immune tolerance by suppressing local T-cell responses under various physiological and pathophysiological conditions, such as pregnancy in mammals, tumor resistance, autoimmunity, and chronic inflammation. Although many studies have demonstrated the biological importance of IDO activity, the PTMs of IDO enzymes remain largely unknown. Only a few important PTMs of IDO1 have been found, such as nitration, N-terminal acetylation, and phosphorylation. In this review, we analyze the PTMs of IDO1 using our twodimensional LC-MS/MS system, and provide an overview of our current understanding.

Original languageEnglish
Pages (from-to)1777-1782
Number of pages6
JournalAnalytical and Bioanalytical Chemistry
Volume403
Issue number7
DOIs
Publication statusPublished - 01-06-2012

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Indoleamine-Pyrrole 2,3,-Dioxygenase
Post Translational Protein Processing
Mass spectrometry
Proteins
Liquid chromatography
Nitration
Liquid Chromatography
Acetylation
Electrospray ionization
Phosphorylation
Mammals
T-cells
Mass Spectrometry
Enzymes
Tryptophan
Chemical properties
Conformations
Tumors
Immune Tolerance
Thermodynamic properties

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Cite this

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abstract = "Protein posttranslational modifications (PTMs) perform essential roles in the biological regulation of a cell. PTMs are extremely important because they can change a protein's physical or chemical properties, conformation, activity, cellular location, or stability. In fact, most proteins are altered by the addition or removal of a chemical moiety on either an amino acid or the protein's N- or C-terminus. Some PTMs can be added and removed dynamically as a mechanism for reversibly controlling protein function. Thus, identifying the PTM sites is critical to fully understand the biological roles of any given protein. Mass spectrometry (MS) is a widely used analytical strategy to identify PTMs. We have used an automated two-dimensional liquid chromatography (LC) system coupled with electrospray ionization quadrupole ion-trap MS to identify PTMs for indoleamine 2,3-dioxygenase 1 (IDO1), one of the tryptophan catabolic enzymes. IDO1 promotes immune tolerance by suppressing local T-cell responses under various physiological and pathophysiological conditions, such as pregnancy in mammals, tumor resistance, autoimmunity, and chronic inflammation. Although many studies have demonstrated the biological importance of IDO activity, the PTMs of IDO enzymes remain largely unknown. Only a few important PTMs of IDO1 have been found, such as nitration, N-terminal acetylation, and phosphorylation. In this review, we analyze the PTMs of IDO1 using our twodimensional LC-MS/MS system, and provide an overview of our current understanding.",
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Posttranslational modification of indoleamine 2,3-dioxygenase. / Fujigaki, Hidetsugu; Seishima, Mitsuru; Saito, Kuniaki.

In: Analytical and Bioanalytical Chemistry, Vol. 403, No. 7, 01.06.2012, p. 1777-1782.

Research output: Contribution to journalArticle

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