Protein glutathionylation and oxidative stress.

Abstract

Liquid chromatography/electrospray ionization-mass spectrometry (LC/ESI-MS) demonstrated that glutathionyl hemoglobin (Hb) levels are increased in patients with diabetes, hyperlipidemia, uremia and Friedreich's ataxia. Glutathionylation of Hb is enhanced by oxidative stress. High performance liquid chromatography (HPLC) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) have also been developed for the quantification of glutathionyl Hb. Glutathionyl-lens proteins were detected in uremic patients and cataractous aged subjects. Glutathionylation of numerous enzymes is induced by oxidative stress, reduces their catalytic activities and may be involved in protection from the damaging effects of oxidative agents. Thioredoxin, glutaredoxin (thioltransferase) and protein disulfide isomerase are the key enzymes in controlling cellular oxidative stress that catalyze reduction of glutathionyl protein disulfide bonds. Thus, protein glutathionylation is closely associated with oxidative stress.

• Authors: Toshimitsu Niwa
• Journal: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences (J Chromatogr B Analyt Technol Biomed Life Sci) Vol. 855 Issue 1 Pg. 59-65 (Aug 2007) ISSN: 1570-0232 [Print] Netherlands
• PMID: 17222592 (Publication Type: Journal Article, Review)

Chemical References

• Crystallins
• Hemoglobins
• glutathionyl hemoglobin
• Protein Disulfide Reductase (Glutathione)
• Glutathione

Topics

• Crystallins (analysis)
• Glutathione (analysis, chemistry, metabolism)
• Hemoglobins (analysis, metabolism)
• Oxidation-Reduction
• Oxidative Stress
• Protein Disulfide Reductase (Glutathione) (chemistry, metabolism)
• Spectrometry, Mass, Electrospray Ionization
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization