scholarly journals Gas phase oxidants of cigarette smoke induce lipid peroxidation and changes in lipoprotein properties in human blood plasma. Protective effects of ascorbic acid

1991 ◽  
Vol 277 (1) ◽  
pp. 133-138 ◽  
Author(s):  
B Frei ◽  
T M Forte ◽  
B N Ames ◽  
C E Cross
Keyword(s):  
Lipid Peroxidation ◽  
Ascorbic Acid ◽  
Blood Plasma ◽  
Gas Phase ◽  
Cigarette Smoke ◽  
Human Blood ◽  
Biological Fluids ◽  
Human Blood Plasma ◽  
Lipid Hydroperoxides ◽  
Protein Thiols

Cigarette smoke (CS) is known to contain a large number of oxidants. In order to assess the oxidative effects of CS on biological fluids, we exposed human blood plasma to filtered (gas phase) and unfiltered (whole) CS, and determined the rate of utilization of endogenous antioxidants in relation to the appearance of lipid hydroperoxides. Lipid peroxidation was measured with a specific and sensitive assay that can detect lipid hydroperoxides at plasma levels as low as 10 nM. We found that exposure of plasma to the gas phase of CS, but not to whole CS, induces lipid peroxidation once endogenous ascorbic acid has been oxidized completely. In addition, CS exposure caused oxidation of plasma protein thiols and albumin-bound bilirubin, whereas uric acid and alpha-tocopherol were not consumed at significant rates. In plasma exposed to the gas phase of CS, low-density lipoprotein exhibited slightly increased electrophoretic mobility, but there was no apparent degradation of apolipoprotein B. Our results support the concept of an increased vitamin C utilization in smokers, and suggest that lipid peroxidation induced by oxidants present in the gas phase of CS leads to potentially atherogenic changes in lipoproteins.

scholarly journals One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centred radicals

1997 ◽  
Vol 321 (3) ◽  
pp. 743-750 ◽  
Author(s):  
Donatella PIETRAFORTE ◽  
Maurizio MINETTI
Keyword(s):  
Blood Plasma ◽  
Human Blood ◽  
Structural Information ◽  
Biological Fluids ◽  
Nitroxide Radical ◽  
Amide Bond ◽  
Human Blood Plasma ◽  
Oxidation Pathway ◽  
Protein Adduct ◽  
Radical Adduct

Exposure of human blood plasma to peroxynitrite in the presence of 3,5-dibromo-4-nitrosobenzenesulphonic acid (DBNBS) resulted in the trapping of a strongly immobilized nitroxide radical adduct. The adduct was due to protein-centred radicals derived not only from serum albumin but also from other major plasma proteins (fibrinogen, IgG, α1-antitrypsin and transferrin). Urate significantly protected plasma from the peroxynitrite-induced DBNBSŐplasma protein adduct, whereas ascorbate and glutathione were protective at concentrations exceeding those usually found in plasma. Alkylation of plasma ŐSH groups did not affect the intensity of DBNBSŐplasma protein adduct, whereas bicarbonate increased its formation, thus showing a pro-oxidant effect. The DBNBSŐplasma protein adduct provided little structural information, but subsequent non-specific-protease treatment resulted in the detection of an isotropic three-line spectrum, indicating the trapping of radicals centred on a tertiary carbon. The nitrogen hyperfine coupling constant of this adduct and its superhyperfine structure were similar to those of DBNBSŐtryptophan peptides with the α-amino group of tryptophan linked in the amide bond, consistent with a radical adduct formed at C-3 of the indole ring of tryptophan-containing peptides. DBNBS was unable to trap radicals derived from peroxynitrite-treated tyrosine or tyrosine-containing peptides. Methionine treated with peroxynitrite resulted in the trapping of at least two DBNBSŐmethionine adducts with hyperfine structures different from that of protease-treated DBNBSŐplasma proteins. These results demonstrate that peroxynitrite induced in blood plasma the formation of protein radicals centred on tryptophan residues and underline the relevance of the one-electron oxidation pathway of peroxynitrite decomposition in biological fluids.

Mechanisms of lipid peroxidation in human blood plasma: a kinetic approach

1997 ◽  
Vol 88 (2) ◽  
pp. 83-96 ◽  
Author(s):  
Barbara Karten ◽  
Ulrike Beisiegel ◽  
Günther Gercken ◽  
Anatol Kontush
Keyword(s):  
Lipid Peroxidation ◽  
Blood Plasma ◽  
Human Blood ◽  
Kinetic Approach ◽  
Human Blood Plasma

The Chemiluminescence Assay of Lipid Peroxidation Products in Human Blood Plasma Lipoproteins

1994 ◽  
Vol 20 (5) ◽  
pp. 279-288 ◽  
Author(s):  
Elena Driomina ◽  
Igor Polnikov ◽  
Victor Sharov ◽  
Ofelia Azizova ◽  
Yury Vladimirov
Keyword(s):  
Lipid Peroxidation ◽  
Blood Plasma ◽  
Human Blood ◽  
Plasma Lipoproteins ◽  
Human Blood Plasma ◽  
Lipid Peroxidation Products ◽  
Chemiluminescence Assay ◽  
Blood Plasma Lipoproteins

scholarly journals Glucose Concentration Measurement in Human Blood Plasma Solutions with Microwave Sensors

Sensors ◽  
2019 ◽  
Vol 19 (17) ◽  
pp. 3779 ◽  
Author(s):  
Carlos G. Juan ◽  
Enrique Bronchalo ◽  
Benjamin Potelon ◽  
Cédric Quendo ◽  
José M. Sabater-Navarro
Keyword(s):  
Ascorbic Acid ◽  
Blood Plasma ◽  
Glucose Level ◽  
Human Blood ◽  
Human Blood Plasma ◽  
Dielectric Losses ◽  
Human Blood Sample ◽  
Glucose Concentration Measurement ◽  
Electromagnetic Signature ◽  
Microwave Sensors

Three microwave sensors are used to track the glucose level of different human blood plasma solutions. In this paper, the sensors are evaluated as glucose trackers in a context close to real human blood. Different plasma solutions sets were prepared from a human blood sample at several added glucose concentrations up to 10 wt%, adding also ascorbic acid and lactic acid at different concentrations. The experimental results for the different sensors/solutions combinations are presented in this work. The sensors show good performance and linearity as glucose level retrievers, although the sensitivities change as the rest of components vary. Different sensor behaviors depending upon the concentrations of glucose and other components are identified and characterized. The results obtained in terms of sensitivity are coherent with previous works, highlighting the contribution of glucose to the dielectric losses of the solution. The results are also consistent with the frequency evolution of the electromagnetic signature of glucose found in the literature, and are helpful for selecting frequency bands for sensing purposes and envisioning future approaches to the challenging measurement in real biological contexts. Discussion of the implications of the results and guidelines for further research and development of more accurate sensors is offered.

scholarly journals One-electron oxidation pathway of thiols by peroxynitrite in biological fluids: bicarbonate and ascorbate promote the formation of albumin disulphide dimers in human blood plasma

1998 ◽  
Vol 329 (2) ◽  
pp. 405-413 ◽  
Author(s):  
Giuseppe SCORZA ◽  
Maurizio MINETTI
Keyword(s):  
Blood Plasma ◽  
Peptide Mapping ◽  
Biological Fluids ◽  
Protein S ◽  
Human Blood Plasma ◽  
Thiol Groups ◽  
Chain Reactions ◽  
Thiyl Radicals ◽  
Protein Thiols ◽  
The One

Recent studies have shown that peroxynitrite oxidizes thiol groups through competing one- and two-electron pathways. The two-electron pathway is mediated by the peroxynitrite anion and prevails quantitatively over the one-electron pathway, which is mediated by peroxynitrous acid or a reactive species derived from it. In CO2-containing fluids the oxidation of thiols might follow a different mechanism owing to the rapid formation of a different oxidant, the nitrosoperoxycarbonate anion (ONOOCO2-). Here we present evidence that in blood plasma peroxynitrite induces the formation of a disulphide cross-linked protein identified by immunological (anti-albumin antibodies) and biochemical criteria (peptide mapping) as a dimer of serum albumin. The albumin dimer did not form in plasma devoid of CO2 and its formation was enhanced by ascorbate. However, analysis of thiol groups showed that reconstituting dialysed plasma with NaHCO3 protected protein thiols against the oxidation mediated by peroxynitrite and that the simultaneouspresence of ascorbate provided further protection. Ascorbate alone did not protect thiol groups from peroxynitrite-mediated oxidation. ESR spin-trapping studies with N-t-butyl-α-phenylnitrone (PBN) revealed that peroxynitrite induced the formation of protein thiyl radicals and their intensity was markedly decreased by plasma dialysis and restored by reconstitution with NaHCO3. PBN completely inhibited the formation of albumin dimer. Moreover, the addition of iron-diethyldithiocarbamate to plasma demonstrated that peroxynitrite induced the formation of protein S-nitrosothiols and/or S-nitrothiols. Our results are consistent with the hypothesis that NaHCO3 favours the one-electron oxidation of thiols by peroxynitrite with formation of thiyl radicals, •NO2, and RSNOx. Thiyl radicals, in turn, are involved in chain reactions by which thiols are oxidized to disulphides.

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