Proteomic Identification of S-Nitrosylated Golgi Proteins New Insights into Endothelial Cell Regulation by eNOS-Derived NO 英文参考文献.docVIP

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Proteomic Identification of S-Nitrosylated Golgi Proteins New Insights into Endothelial Cell Regulation by eNOS-Derived NO 英文参考文献.doc

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Proteomic Identification of S-Nitrosylated Golgi Proteins New Insights into Endothelial Cell Regulation by eNOS-Derived NO 英文参考文献

ProteomicIdentificationofS-NitrosylatedGolgiProteins: NewInsightsintoEndothelialCellRegulationbyeNOS- DerivedNO PanjamapornSangwung1.,ToddM.Greco2,3.,YanzhuangWang4,HarryIschiropoulos2,WilliamC. Sessa5,YasukoIwakiri1* 1SectionofDigestiveDiseases,DepartmentofInternalMedicine,YaleUniversitySchoolofMedicine,NewHaven,Connecticut,UnitedStatesofAmerica,2Departmentof PharmacologyandChildren’sHospitalofPhiladelphiaResearchInstitute,Children’sHospitalofPhiladelphiaandUniversityofPennsylvania,Philadelphia,Pennsylvania, UnitedStatesofAmerica,3DepartmentofMolecularBiology,PrincetonUniversity,Princeton,NewJersey,UnitedStatesofAmerica,4DepartmentofMolecular,Cellular andDevelopmentalBiology,UniversityofMichigan,AnnArbor,Michigan,UnitedStatesofAmerica,5DepartmentofPharmacology,YaleUniversitySchoolofMedicine, NewHaven,Connecticut,UnitedStatesofAmerica Abstract Background:Endothelialnitricoxidesynthase(eNOS)isprimarilylocalizedontheGolgiapparatusandplasmamembrane caveolaeinendothelialcells.Previously,wedemonstratedthatproteinS-nitrosylationoccurspreferentiallywhereeNOSis localized.Thus,inendothelialcells,GolgiproteinsarelikelytobetargetsforS-nitrosylation.Theaimofthisstudywasto identifyS-nitrosylatedGolgiproteinsandattributetheirS-nitrosylationtoeNOS-derivednitricoxideinendothelialcells. Methods: Golgi membranes were isolated from rat livers. S-nitrosylated Golgi proteins were determined by a modified biotin-switchassaycoupledwithmassspectrometrythatallowstheidentificationoftheS-nitrosylatedcysteineresidue.The biotin switch assay followed by Western blot or immunoprecipitation using an S-nitrosocysteine antibody was also employedtovalidateS-nitrosylatedproteinsinendothelialcelllysates. Results:Seventy-eightpotentialS-nitrosylatedproteinsandtheirtargetcysteineresiduesforS-nitrosylationwereidentified; 9 of them were Golgi-resident or Golgi/endoplasmic reticulum (ER)-associated proteins. Among these 9 proteins, S- nitrosylation of EMMPRIN and Golgi phosphoprotein 3 (GOLPH3) was verifi