{"database":"MassIVE","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://massive-ftp.ucsd.edu/v06/MSV000093040/"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"submitter":["Steven Lonergan"],"full_dataset_link":["https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=83c04c84038c45b29dc6f340bd5e1089"],"submitter_email":["slonerga@iastate.edu"],"sample_protocol":[""],"repository":["MassIVE"],"file_size":["52"],"ptm_modification":["[C,N] [80.06260] hexenal","MOD:01253 - \"modification from UniMod Chemical derivative - Malondialdehyde (MDA) adduct\"","UNIMOD:53 - \"4-hydroxynonenal (HNE).\"","MOD:01060 - \"A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.\"","UNIMOD:35 - \"Oxidation or Hydroxylation.\""],"data_protocol":[""],"omics_type":["Proteomics"],"instrument_platform":["Orbitrap Eclipse","ultrafleXtreme"],"species":["Sus Scrofa (ncbitaxon:9823)"],"submitter_affiliation":["Iowa State University"],"name_synonyms":["Ca2+ Activated Protease, Proteinase, Calcium Activated Neutral Protease, Ca2+-Activated, Calcium Dependent Neutral Protease, Protease, Calcium Activated Neutral Proteinase, Calcium-Activated Neutral, Desminase., Calpain II, metastatic, Calcium-Dependent, Neutral Protease, Calcium-Dependent Neutral Protease, Calcium-Activated Neutral Protease, Ca2+-Activated Protease, Calcium-Activated Protease, Calcium-Dependent Neutral Proteinase, Calcium Dependent Neutral Proteinase, Calpain I, Calcium-Dependent Neutral, Calcium-Activated, Calcium-Activated Neutral Proteinase, Calcium Activated Protease, Neutral Proteinase"],"description_synonyms":["liquid chromatography tandem mass spectroscopy, 4-Hydroxynonenal, Plantaris, E 920, Laser Desorption-Ionization Mass Spectrometry, Anterior, Activity, 4-Hydroxy-2, Calcium 40, Skeletal, Anterior Tibial Muscle, Matrix Assisted Laser Desorption Ionization Mass Spectrometry, 4-HNE, protein, sci, Malonaldehyde, protein polypeptide chains, HOW, How, 2, 4, 2-amino-3-mercaptopropanoic acid, Cystein, protein aggregate, Calcium-Activated Neutral Proteinase, l(3)j5D5, Surface Enhanced Laser Desorption Ionization Mass Spectrometry, Desminase, imprinted and ancient gene protein, 24B, calcio, C, E, LCMSMS, Calcium Activated Neutral Protease, cisteina, stru, MS-MALD, proteins, Mass Spectrometry, MALDI MS, l(3)S053606, CG10293, (E)-isomer, autolysis, Matrix Assisted Laser Desorption Ionization, l(3)j5B5, Sodium Malondialdehyde, hex-2-en-1-al, Muscles, 6(1H, Autolyses, 3H, Half Cystine, Gastrocnemius, Blood Coagulation Factor IV, Ca, LC-MS2, close to, Ca2+ Activated Protease, 0904/17, Proteinase, Coagulation, Hexobarbitone, Zinc Cysteinate, LC-MS/MS, Calcium Dependent Neutral Protease, Calcium Activated Neutral Proteinase, Laser Desorption Ionization Mass Spectrometry, Cys, Sodium Hexobarbital, Spectroscopy, Voluntary Muscle, SZ1, Voluntary, Calpain I, Voluntary Muscles, Malonylaldehyde, Calcium-Dependent Neutral, Calcium-Activated, (2R)-2-amino-3-sulfanylpropanoic acid, trans-2-hexenal, 4-hydroxynonen-2-al, Ca2+-Activated, L-Cysteine, L-Cystein, Calcium-Activated Neutral, calcium, metastatic, Ca2+-Activated Protease, Calcium-Activated Protease, liquid chromatography-tandem mass spectroscopy, 4-hydroxynonenal, anon-EST:Liang-2.39, E430016J11Rik, Gastrocnemius Muscle, Cysteine Hydrochloride, MALDI-MS, conformation, 2-hexenal, P62, 5H)-Pyrimidinetrione, number, L-Zystein, Gene, Protease, protein-containing complex, Ximpact, skeletal muscle, LC-MS-MS, Desminase., Calcium-Dependent Neutral Protease, Calcium-Activated Neutral Protease, polypeptide chain, 20Ca, Factor IV, Malondialdehyde, LC-MSMS, Gene Products, Mass, Half-Cystine, Mass Spectroscopy, Ca(0), Hexobarbital, Calcium-40, l(3)s2612, Tibial Muscle, L Cysteine, E-920, 5-(1-cyclohexen-1-yl)-1, Hcys, Matrix Assisted, Skeletal Muscles, 4-hydroxy-2-nonenal, Z-isomer, SELDI-TOF-MS, Calpain II, Skeletal Muscle, Plantaris Muscle, CYSTEINE, Calcium-Dependent Neutral Proteinase, Propanedial, DmelCG10293, 4-HNE cpd, FREE CYSTEINE, (2R)-2-amino-3-mercaptopropanoic acid, relational structural quality, Anterior Tibial, 5-dimethyl-, Calcium Activated Protease, MALD-MS, Neutral Proteinase, striated muscle, 3-nonenal, Evipan, clone 2.39, protein complex, Proteins, Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry, function, qkr, Kalzium, 4-hydroxy-2, Muscle, l(3)S090417, impact-a, near to, Soleus, somatic muscle, Neutral Protease, LC/MS/MS, native protein, natural protein, KH93F, Calcium Dependent Neutral Proteinase, Protein, Can, IMPACT, imprinted and ancient gene protein homolog, Sodium, Zystein, who, Calcium, Soleus Muscle, 2-amino-3-sulfanylpropanoic acid, Matrix-Assisted, L-2-Amino-3-mercaptopropionic acid, (R)-2-amino-3-mercaptopropanoic acid, Who/How, Matrix-Assisted Laser Desorption-Ionization, Malonyldialdehyde, 2-Amino-3-mercaptopropionic acid, Protein Gene Products, 4-Hydroxy-2-nonenal, Gene Proteins, Calcium-Dependent, Coagulation Factor IV, MALDI, approaches, Hexenal, vicinity of, cardinality, qkr[93F], E920, liquid chromatography tandem mass spectrometry, General activity, RWDD5, HNE, skeletal muscle system"],"additional_accession":["PXD045905"]},"is_claimable":false,"name":"Secondary Lipid Oxidation Products as Modulators of Calpain-2 Functionality In Vitro","description":"Secondary lipid oxidation products modify and impact the function of proteins. Identifying where and how these products modify a protein's structure would allow for targeted approaches to mitigate or prevent this modification. Here, we purified calpain-2, a neutral calcium dependent cysteine protease, from porcine skeletal muscle and conducted in-vitro experiments using various concentrations of malondialdehyde, 2-hexenal, and 4-hydroxynonenal. We determined these secondary lipid oxidation products differentially impact calpain-2 proteolytic activity and autolysis. We identified modifications of malondialdehyde and hexenal on calpain-2 with LC-MS/MS approaches. We further evaluated the number of adduction sites on the catalytic and regulatory subunits of calpain-2 through MALDI-MS approaches. These data demonstrate that secondary lipid oxidation products can modify and differentially impact calpain-2.","dates":{"publication":"Wed Oct 04 15:10:00 BST 2023"},"accession":"MSV000093040","cross_references":{}}