Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
Mass spectrometry characterization of circulating human serum albumin microheterogeneity in patients with alcoholic hepatitis. / Naldi, Marina; Baldassarre, Maurizio; Domenicali, Marco et al.
In: Journal of Pharmaceutical and Biomedical Analysis, Vol. 122, 15.04.2016, p. 141-7.Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
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TY - JOUR
T1 - Mass spectrometry characterization of circulating human serum albumin microheterogeneity in patients with alcoholic hepatitis
AU - Naldi, Marina
AU - Baldassarre, Maurizio
AU - Domenicali, Marco
AU - Giannone, Ferdinando Antonino
AU - Bossi, Matteo
AU - Montomoli, Jonathan
AU - Sandahl, Thomas Damgaard
AU - Glavind, Emilie
AU - Vilstrup, Hendrik
AU - Caraceni, Paolo
AU - Bertucci, Carlo
N1 - Copyright © 2016 Elsevier B.V. All rights reserved.
PY - 2016/4/15
Y1 - 2016/4/15
N2 - Human serum albumin (HSA) is the most abundant plasma protein, endowed with several biological properties unrelated to its oncotic power, such as antioxidant and free-radicals scavenging activities, binding and transport of many endogenous and exogenous substances, and regulation of endothelial function and inflammatory response. These non-oncotic activities are closely connected to the peculiarly dynamic structure of the albumin molecule. HSA undergoes spontaneous structural modifications, mainly by reaction with oxidants and saccharides; however, patients with cirrhosis show extensive post-transcriptional changes at several molecular sites of HSA, the degree of which parallels the severity of the disease. The present work reports the development and application of an innovative LC-MS analytical method for a rapid and reproducible determination of the relative abundance of HSA isoforms in plasma samples from alcoholic hepatitis (AH) patients. A condition of severe oxidative stress, similar to that observed in AH patients, is associated with profound changes in circulating HSA microheterogeneity. More interestingly, the high resolution provided by the analytical platform allowed the monitoring of novel oxidative products of HSA never reported before.
AB - Human serum albumin (HSA) is the most abundant plasma protein, endowed with several biological properties unrelated to its oncotic power, such as antioxidant and free-radicals scavenging activities, binding and transport of many endogenous and exogenous substances, and regulation of endothelial function and inflammatory response. These non-oncotic activities are closely connected to the peculiarly dynamic structure of the albumin molecule. HSA undergoes spontaneous structural modifications, mainly by reaction with oxidants and saccharides; however, patients with cirrhosis show extensive post-transcriptional changes at several molecular sites of HSA, the degree of which parallels the severity of the disease. The present work reports the development and application of an innovative LC-MS analytical method for a rapid and reproducible determination of the relative abundance of HSA isoforms in plasma samples from alcoholic hepatitis (AH) patients. A condition of severe oxidative stress, similar to that observed in AH patients, is associated with profound changes in circulating HSA microheterogeneity. More interestingly, the high resolution provided by the analytical platform allowed the monitoring of novel oxidative products of HSA never reported before.
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1016/j.jpba.2016.01.048
DO - 10.1016/j.jpba.2016.01.048
M3 - Journal article
C2 - 26852162
VL - 122
SP - 141
EP - 147
JO - Journal of Pharmaceutical and Biomedical Analysis
JF - Journal of Pharmaceutical and Biomedical Analysis
SN - 0731-7085
ER -