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Our previous data showed that an apparent SR dimer resistant to sodium dodecyl sulfate and \u03b2\u2010mercaptoethanol was elevated in microglial cells after proinflammatory activation. Because the activation of microglia is typically associated with an oxidative burst, oxidative cross\u2010linking between SR subunits was speculated. In this study, an siRNA technique was employed to confirm the identity of this SR dimer band. The oxidative species potentially responsible for the cross\u2010linking was investigated with recombinant SR protein. The data indicate that nitric oxide, peroxynitrite, and hydroxyl radical were the likely candidates, whereas superoxide and hydrogen peroxide per se failed to contribute. Furthermore, the mechanism of formation of SR dimer by peroxynitrite oxidation was studied by mass spectrometry. A disulfide bond between Cys<jats:sub>6<\/jats:sub> and Cys<jats:sub>113<\/jats:sub> was identified in 3\u2010morpholinosydnonimine hydrochloride (SIN\u20101)\u2010treated SR monomer and dimer. Activity assays indicated that SIN\u20101 treatment decreased SR activity, confirming our previous conclusion that noncovalent dimer is the most active form of SR. These findings suggest a compensatory feedback in which the consequences of neuroinflammation might dampen D\u2010serine production to limit excitotoxic stimulation of NMDA receptors. \u00a9 2012 Wiley Priodicals, Inc.<\/jats:p>","DOI":"10.1002\/jnr.22832","type":"journal-article","created":{"date-parts":[[2012,2,22]],"date-time":"2012-02-22T05:37:48Z","timestamp":1329889068000},"page":"1218-1229","source":"Crossref","is-referenced-by-count":13,"title":["Cross\u2010linking of serine racemase dimer by reactive oxygen species and reactive nitrogen species"],"prefix":"10.1002","volume":"90","author":[{"given":"Wei","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven W.","family":"Barger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2012,2,22]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00726-003-0018-8"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0143-4160(03)00141-6"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1006\/niox.1999.0206"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.2741\/1481"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1471-4159.2001.00075.x"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.2007.04487.x"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neurobiolaging.2004.02.022"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111814200"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-4388(00)00215-4"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1119(00)00356-5"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1007\/s000180050357"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M405726200"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1093\/toxsci\/68.1.9"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(92)80911-Y"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1039\/j19680000450"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.5034-08.2008"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M512927200"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/ddp261"},{"key":"e_1_2_6_20_1","article-title":"Contributions of the D\u2010serine pathway to schizophrenia","author":"Labrie V","year":"2011","journal-title":"Neuropharmacology"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1124\/jpet.300.3.717"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1096\/fj.08-120568"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0611620104"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.2353\/ajpath.2008.080019"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00811a062"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7601840"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.9.3948"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.17-05-01604.1997"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.050062"},{"key":"e_1_2_6_30_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1749-6632.2001.tb05632.x"},{"key":"e_1_2_6_31_1","doi-asserted-by":"publisher","DOI":"10.1080\/10715760600918142"},{"key":"e_1_2_6_32_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(02)03855-3"},{"key":"e_1_2_6_33_1","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1113\/jphysiol.2003.049478","article-title":"Mitochondrial formation of reactive oxygen species","volume":"15","author":"Turrens JF","year":"2003","journal-title":"J Physiol"},{"key":"e_1_2_6_34_1","doi-asserted-by":"crossref","unstructured":"WangW BargerSW.2011.Roles of quaternary structure and cysteine residues in the activity of human serine racemase. 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