Posttranslational modification of indoleamine 2,3-dioxygenase

作者: Hidetsugu Fujigaki , Mitsuru Seishima , Kuniaki Saito

DOI: 10.1007/S00216-012-5946-2

关键词:

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

参考文章(60)
Stan A.B. Greenacre, Harry Ischiropoulos, Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radical Research. ,vol. 34, pp. 541- 581 ,(2001) , 10.1080/10715760100300471
Alain P. Gobert, Silla Semballa, Sylvie Daulouede, Sophie Lesthelle, Murielle Taxile, Bernard Veyret, Philippe Vincendeau, Murine Macrophages Use Oxygen- and Nitric Oxide-Dependent Mechanisms To Synthesize S-Nitroso-Albumin and To Kill Extracellular Trypanosomes Infection and Immunity. ,vol. 66, pp. 4068- 4072 ,(1998) , 10.1128/IAI.66.9.4068-4072.1998
Lynne Harrington, Chittur V. Srikanth, Reuben Antony, Sue J. Rhee, Andrew L. Mellor, Hai Ning Shi, Bobby J. Cherayil, Deficiency of Indoleamine 2,3-Dioxygenase Enhances Commensal-Induced Antibody Responses and Protects against Citrobacter rodentium-Induced Colitis Infection and Immunity. ,vol. 76, pp. 3045- 3053 ,(2008) , 10.1128/IAI.00193-08
Alessandra Castegna, Visith Thongboonkerd, Jon B. Klein, Bert Lynn, William R. Markesbery, D. Allan Butterfield, Proteomic identification of nitrated proteins in Alzheimer's disease brain. Journal of Neurochemistry. ,vol. 85, pp. 1394- 1401 ,(2003) , 10.1046/J.1471-4159.2003.01786.X
Stephen Jackson, INT CONGR SER 9th Symposium of the Esteve-Foundation. ,(2001)
Hannah Johnson, Claire E. Eyers, Analysis of post-translational modifications by LC-MS/MS. Methods of Molecular Biology. ,vol. 658, pp. 93- 108 ,(2010) , 10.1007/978-1-60761-780-8_5
Shozo Yamamoto, Osamu Hayaishi, Tryptophan Pyrrolase of Rabbit Intestine d- AND l-TRYPTOPHAN-CLEAVING ENZYME OR ENZYMES Journal of Biological Chemistry. ,vol. 242, pp. 5260- 5266 ,(1967) , 10.1016/S0021-9258(18)99420-2
Edward D. Hall, Megan R. Detloff, Kjell Johnson, Nancy C. Kupina, Peroxynitrite-mediated protein nitration and lipid peroxidation in a mouse model of traumatic brain injury. Journal of Neurotrauma. ,vol. 21, pp. 9- 20 ,(2004) , 10.1089/089771504772695904
Adam R. Farley, Andrew J. Link, Identification and quantification of protein posttranslational modifications. Methods in Enzymology. ,vol. 463, pp. 725- 763 ,(2009) , 10.1016/S0076-6879(09)63040-8
Hidetsugu Fujigaki, Kuniaki Saito, Felix Lin, Suwako Fujigaki, Kanako Takahashi, Brian M. Martin, Cai Y. Chen, Junichi Masuda, Jeffrey Kowalak, Osamu Takikawa, Mitsuru Seishima, Sanford P. Markey, Nitration and inactivation of IDO by peroxynitrite. Journal of Immunology. ,vol. 176, pp. 372- 379 ,(2006) , 10.4049/JIMMUNOL.176.1.372