Protein carbonylation has attracted the interest of a great number of
laboratories since the pioneering studies at the Earl Stadtman's lab at
NIH started in early 1980s. Since then, detecting protein carbonyls in
oxidative stress situations became a highly efficient tool to uncover
biomarkers of oxidative damage in normal and altered cell physiology.
In this book, research groups from several areas of interest have
contributed to update the knowledge regarding detection, analyses and
identification of carbonylated proteins and the sites where these
modifications occur.
The scientific community will benefit from these reviews since they deal
with specific, detailed technical approaches to study formation and
detection of protein carbonyls. Moreover, the biological impact of such
modifications in metabolic, physiologic and structural functions and,
how these alterations can help understanding the downstream effects on
cell function are discussed.
- Oxidative stress occurs in all living organisms and affects proteins
and other macromolecules: Protein carbonylation is a measure of
oxidative stress in biological systems
- Mass spectrometry, fluorescent labelling, antibody based detection,
biotinylated protein selection and other methods for detecting protein
carbonyls and modification sites in proteins are described
- Aging, neurodegenerative diseases, obstructive pulmonary diseases,
malaria, cigarette smoke, adipose tissue and its relationship with
protein carbonylation
- Direct oxidation, glycoxidation and modifications by lipid
peroxidation products as protein carbonylation pathways
- Emerging methods for characterizing carbonylated protein networks and
affected metabolic pathways
