The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function
Fibrinogen is one of the plasma proteins most susceptible to oxidative modification. It has been suggested that modification of fibrinogen may cause thrombotic/bleeding complications associated with many pathophysiological states of organism. We exposed fibrinogen molecules to three different modifi...
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1155/2013/359621 |
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| author | Jana Štikarová Roman Kotlín Tomáš Riedel Jiří Suttnar Kristýna Pimková Leona Chrastinová Jan E. Dyr |
| author_facet | Jana Štikarová Roman Kotlín Tomáš Riedel Jiří Suttnar Kristýna Pimková Leona Chrastinová Jan E. Dyr |
| author_sort | Jana Štikarová |
| collection | DOAJ |
| description | Fibrinogen is one of the plasma proteins most susceptible to oxidative modification. It has been suggested that modification of fibrinogen may cause thrombotic/bleeding complications associated with many pathophysiological states of organism. We exposed fibrinogen molecules to three different modification reagents—malondialdehyde, sodium hypochlorite, and peroxynitrite—that are presented to various degrees in different stages of oxidative stress. We studied the changes in fibrin network formation and platelet interactions with modified fibrinogens under flow conditions. The fastest modification of fibrinogen was caused by hypochlorite. Fibers from fibrinogen modified with either reagent were thinner in comparison with control fibers. We found that platelet dynamic adhesion was significantly lower on fibrinogen modified with malondialdehyde and significantly higher on fibrinogen modified either with hypochlorite or peroxynitrite reflecting different prothrombotic/antithrombotic properties of oxidatively modified fibrinogens. It seems that, in the complex reactions ongoing in living organisms at conditions of oxidation stress, hypochlorite modifies proteins (e.g., fibrinogen) faster and more preferentially than malondialdehyde. It suggests that the prothrombotic effects of prior fibrinogen modifications may outweigh the antithrombotic effect of malondialdehyde-modified fibrinogen in real living systems. |
| format | Article |
| id | doaj-art-9b984c4d9edf402c8538bbe4dd476d99 |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-9b984c4d9edf402c8538bbe4dd476d992025-02-03T01:12:50ZengWileyThe Scientific World Journal1537-744X2013-01-01201310.1155/2013/359621359621The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen FunctionJana Štikarová0Roman Kotlín1Tomáš Riedel2Jiří Suttnar3Kristýna Pimková4Leona Chrastinová5Jan E. Dyr6Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicInstitute of Hematology and Blood Transfusion, U Nemocnice 1, 128 00 Prague 2, Czech RepublicFibrinogen is one of the plasma proteins most susceptible to oxidative modification. It has been suggested that modification of fibrinogen may cause thrombotic/bleeding complications associated with many pathophysiological states of organism. We exposed fibrinogen molecules to three different modification reagents—malondialdehyde, sodium hypochlorite, and peroxynitrite—that are presented to various degrees in different stages of oxidative stress. We studied the changes in fibrin network formation and platelet interactions with modified fibrinogens under flow conditions. The fastest modification of fibrinogen was caused by hypochlorite. Fibers from fibrinogen modified with either reagent were thinner in comparison with control fibers. We found that platelet dynamic adhesion was significantly lower on fibrinogen modified with malondialdehyde and significantly higher on fibrinogen modified either with hypochlorite or peroxynitrite reflecting different prothrombotic/antithrombotic properties of oxidatively modified fibrinogens. It seems that, in the complex reactions ongoing in living organisms at conditions of oxidation stress, hypochlorite modifies proteins (e.g., fibrinogen) faster and more preferentially than malondialdehyde. It suggests that the prothrombotic effects of prior fibrinogen modifications may outweigh the antithrombotic effect of malondialdehyde-modified fibrinogen in real living systems.http://dx.doi.org/10.1155/2013/359621 |
| spellingShingle | Jana Štikarová Roman Kotlín Tomáš Riedel Jiří Suttnar Kristýna Pimková Leona Chrastinová Jan E. Dyr The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function The Scientific World Journal |
| title | The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function |
| title_full | The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function |
| title_fullStr | The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function |
| title_full_unstemmed | The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function |
| title_short | The Effect of Reagents Mimicking Oxidative Stress on Fibrinogen Function |
| title_sort | effect of reagents mimicking oxidative stress on fibrinogen function |
| url | http://dx.doi.org/10.1155/2013/359621 |
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