Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modulation of several physiological functions but can also be potentially destructive if produced in excessive amounts. Protein cysteinyl thiols appear especially sensitive to ROS/RNS attack. Experimental evidence started to accumulate recently, documenting that S-glutathionylation occurs in a number of physiologically relevant situations, where it can produce discrete modulatory effects on protein function. The increasing evidence of functional changes resulting from this modification, and the growing number of proteins shown to be S-glutathionylated both in vitro and in vivo support this contention, and confirm this as an attractive area of research. S-glutathionylated proteins are now actively investigated with reference to problems of biological interest and as possible biomarkers of human diseases associated with oxidative/nitrosative stress.

Giustarini, D., Rossi, R., Milzani, A., Colombo, R., & Dalle Donne, I. (2004). S-Glutathionylation: from redox regulation of protein functions to human diseases. JOURNAL OF CELLULAR AND MOLECULAR MEDICINE, 8(2), 201-212 [10.1111/j.1582-4934.2004.tb00275.x].

S-Glutathionylation: from redox regulation of protein functions to human diseases

Giustarini, D.
;
Rossi, Ranieri;
2004

Abstract

Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modulation of several physiological functions but can also be potentially destructive if produced in excessive amounts. Protein cysteinyl thiols appear especially sensitive to ROS/RNS attack. Experimental evidence started to accumulate recently, documenting that S-glutathionylation occurs in a number of physiologically relevant situations, where it can produce discrete modulatory effects on protein function. The increasing evidence of functional changes resulting from this modification, and the growing number of proteins shown to be S-glutathionylated both in vitro and in vivo support this contention, and confirm this as an attractive area of research. S-glutathionylated proteins are now actively investigated with reference to problems of biological interest and as possible biomarkers of human diseases associated with oxidative/nitrosative stress.
Giustarini, D., Rossi, R., Milzani, A., Colombo, R., & Dalle Donne, I. (2004). S-Glutathionylation: from redox regulation of protein functions to human diseases. JOURNAL OF CELLULAR AND MOLECULAR MEDICINE, 8(2), 201-212 [10.1111/j.1582-4934.2004.tb00275.x].
File in questo prodotto:
File Dimensione Formato  
2004 Giustarini JCMM.pdf

non disponibili

Tipologia: PDF editoriale
Licenza: PUBBLICO - Pubblico con Copyright
Dimensione 1.12 MB
Formato Adobe PDF
1.12 MB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/411607