Pubmed-entry ::= {
  pmid 10769188,
  medent {
    em std {
      year 2000,
      month 6,
      day 15
    },
    cit {
      title {
        name "Inactivation of creatine kinase by S-glutathionylation of the
 active-site cysteine residue."
      },
      authors {
        names ml {
          "Reddy S",
          "Jones AD",
          "Cross CE",
          "Wong PS",
          "Van Der Vliet A"
        },
        affil str "Department of Internal Medicine and Center for Comparative
 Lung Biology and Medicine, University of California, Davis, CA 95616, USA.
 sreddy@ucdavis.edu"
      },
      from journal {
        title {
          iso-jta "Biochem. J.",
          ml-jta "Biochem J",
          issn "0264-6021",
          name "The Biochemical journal"
        },
        imp {
          date std {
            year 2000,
            month 5,
            day 1
          },
          volume "347",
          pages "821-827",
          part-sup "PT 3",
          language "eng",
          pubstatus ppublish,
          history {
            {
              pubstatus pubmed,
              date std {
                year 2000,
                month 4,
                day 19,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus medline,
              date std {
                year 2000,
                month 6,
                day 17,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus other,
              date std {
                year 2000,
                month 4,
                day 19,
                hour 9,
                minute 0
              }
            }
          }
        }
      },
      ids {
        pubmed 10769188,
        other {
          db "pmc",
          tag str "PMC1221021"
        }
      }
    },
    abstract "Protein S-thiolation, the formation of mixed disulphides of
 cysteine residues in proteins with low-molecular-mass thiols, occurs under
 conditions associated with oxidative stress and can lead to modification of
 protein function. In the present study, we examined the site of S-thiolation
 of the enzyme creatine kinase (CK), an important source of ATP in myocytes.
 Inactivation of this enzyme is thought to play a critical role in cardiac
 injury during oxidative stress, such as during reperfusion injury. Reaction
 of rabbit CK M isoenzyme with GSSG, used to model protein S-thiolation, was
 found to result in enzyme inactivation that could be reversed by GSH or
 dithiothreitol. Measurement of GSH that is released during the thiolation
 reaction indicated that the maximum extent of CK thiolation was approx. 1 mol
 of GSH/mol of protein, suggesting thiolation on one reactive cysteine
 residue. Accordingly, matrix-assisted laser-desorption ionization MS
 confirmed that the molecular mass of CK was increased, consistent with
 addition of one GSH molecule/molecule of CK. Using trypsin digestion, HPLC
 and MS analysis, the active-site cysteine residue (Cys(283)) was identified
 as the site of thiolation. Reversal of thiolation was shown to be rapid when
 GSH is abundant, rendering dethiolation of CK thermodynamically favoured
 within the cell. We conclude that S-glutathionylation of CK could be one
 mechanism to explain temporary reversible loss in activity of CK during
 ischaemic injury. The maintainance of GSH levels represents an important
 mechanism for regeneration of active CK from S-glutathionylated CK.",
    mesh {
      {
        term "Amino Acid Sequence"
      },
      {
        term "Animals"
      },
      {
        term "Binding Sites"
      },
      {
        term "Chromatography, High Pressure Liquid"
      },
      {
        term "Creatine Kinase",
        qual {
          {
            mp TRUE,
            subh "antagonists & inhibitors"
          },
          {
            subh "chemistry"
          },
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Cysteine",
        qual {
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Dithiothreitol",
        qual {
          {
            subh "metabolism"
          }
        }
      },
      {
        term "Glutathione",
        qual {
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Glutathione Disulfide",
        qual {
          {
            subh "metabolism"
          }
        }
      },
      {
        term "Isoenzymes"
      },
      {
        term "Kinetics"
      },
      {
        term "Molecular Sequence Data"
      },
      {
        term "Molecular Weight"
      },
      {
        term "Muscle, Skeletal",
        qual {
          {
            subh "enzymology"
          }
        }
      },
      {
        term "Oxidative Stress"
      },
      {
        term "Peptide Fragments",
        qual {
          {
            subh "metabolism"
          }
        }
      },
      {
        term "Rabbits"
      },
      {
        term "Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization"
      },
      {
        term "Sulfhydryl Compounds",
        qual {
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Thermodynamics"
      },
      {
        term "Trypsin",
        qual {
          {
            subh "metabolism"
          }
        }
      }
    },
    substance {
      {
        type nameonly,
        name "Isoenzymes"
      },
      {
        type nameonly,
        name "Peptide Fragments"
      },
      {
        type nameonly,
        name "Sulfhydryl Compounds"
      },
      {
        type cas,
        cit "27025-41-8",
        name "Glutathione Disulfide"
      },
      {
        type cas,
        cit "3483-12-3",
        name "Dithiothreitol"
      },
      {
        type cas,
        cit "52-90-4",
        name "Cysteine"
      },
      {
        type cas,
        cit "70-18-8",
        name "Glutathione"
      },
      {
        type ec,
        cit "2.7.3.2",
        name "Creatine Kinase"
      },
      {
        type ec,
        cit "3.4.21.4",
        name "Trypsin"
      }
    },
    idnum {
      "P30 ES05707/ES/NIEHS NIH HHS",
      "P42 ES04699/ES/NIEHS NIH HHS",
      "R01HL/ES47628/HL/NHLBI NIH HHS"
    },
    pmid 10769188,
    pub-type {
      "Journal Article",
      "Research Support, U.S. Gov't, P.H.S."
    },
    status medline
  }
}

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