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Keywords: nitrotyrosine
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Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2003) 31 (6): 1417–1422.
Published: 01 December 2003
... were detected free in physiological fluids and in enzymatic hydrolysates of cellular and extracellular proteins. Hydroimidazolones were the most important glycation biomarkers, and methionine sulphoxide was the most important oxidative biomarker quantitatively; 3-nitrotyrosine was the biomarker of...
Abstract
Glycation of proteins forms fructosamines and AGEs (advanced glycation end products). Oxidative and nitrosative stress leads to the formation of oxidative and nitrosative modifications. The modified amino acid residues formed in these processes are biomarkers of protein damage: some are risk markers and some may be risk factors for disease development. We developed a method for the concurrent quantitative measurement of 16 biomarkers indicative of protein glycation, oxidation and nitrosation damage using LC-MS/MS (LC with tandem MS detection). Underivatized analytes were detected free in physiological fluids and in enzymatic hydrolysates of cellular and extracellular proteins. Hydroimidazolones were the most important glycation biomarkers, and methionine sulphoxide was the most important oxidative biomarker quantitatively; 3-nitrotyrosine was the biomarker of nitrosation. Quantitative screening showed high levels of AGEs in cellular protein and moderate levels in protein of blood plasma. Levels of 3-nitrotyrosine were typically 100-fold lower than this. The major glycation adducts in blood plasma had high renal clearances in normal healthy human subjects, whereas methionine sulphoxide and 3-nitrotyrosine had low renal clearances due to further metabolism. Physiological AGEs in blood plasma were eliminated from the circulation in the kidney and not in the liver. LC-MS/MS peptide mapping was also used to locate the protein biomarkers. These studies reveal that advanced glycation is a significant modification of cellular and extracellular protein. The enzymatic defences against glycation, antioxidants and proteasomal protein degradation inside cells are probable factors regulating biomarker levels of cellular protein.
Articles
Journal:
Biochemical Society Transactions
Biochem Soc Trans (2003) 31 (6): 1133–1136.
Published: 01 December 2003
... ischaemia/reperfusion nitrotyrosine peroxynitrite sepsis Abbreviations used: CPT I, outer membrane carnitine palmitoyltransferase I; M-CPT I and L-CPT I, muscle and liver isoforms of CPT I, respectively. The Glucose/Fatty Acid Cycle 1963 2003 1133 Myocardial carnitine palmitoyltransferase I...
Abstract
CPT I (outer membrane carnitine palmitoyltransferase I) is a crucial enzyme in myocardial substrate selection. Two isoforms exist in the heart, the liver (L-) and muscle (M-) isoforms, which have different kinetic characteristics and alter in relative amounts during the neonatal/weaning/adult transition. CPT I is a point for control and regulation of fatty acid oxidation via modulation of its activity by malonyl-CoA, the concentration of which is set by acetyl-CoA carboxylase, AMP-activated protein kinase and malonyl-CoA decarboxylase in response to, for example, alterations in glucose supply. Systemic inflammatory responses and sepsis lead to myocardial dysfunction as part of multiple system organ failure. We have shown that: (i) myocardial CPT I activity is inhibited during neonatal sepsis; (ii) on the basis of inhibitor studies this inhibition appears to be of M-CPT I rather than L-CPT I; (iii) nitration of M-CPT I occurs, probably by peroxynitrite, and this may be responsible for the decrease in CPT I activity; (iv) myocardial CPT I activity is also inhibited in another model of systemic inflammatory response, namely intestinal ischaemia/reperfusion injury, but this can prevented by whole-body moderate hypothermia. Inhibition of M-CPT I would be predicted to alter myocardial substrate selection but there are several questions that remain to be answered.