Different vulnerability of fibrinogen subunits to oxidative/nitrative modifications induced by peroxynitrite: Functional consequences

Nowak, Paweł; Żbikowska, Halina Małgorzata; Ponczek, Michał B.; Kołodziejczyk, Joanna; Wachowicz, Barbara

doi:10.1016/j.thromres.2007.03.017

Cited by 88 publications

(57 citation statements)

References 60 publications

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“…Animals were housed 5 per polycarbonate cage under controlled temperature (20)(21)(22)(23)(24)(25) o C) and humidity (40-45%) under a 12：12 hour light/dark cycle, and a normal rodent pellet diet and water were supplied during acclimatization ad libitum. All animals were treated in accordance with the Guidelines for Care and Use of Laboratory Animals issued by Kyungpook National University.…”

Section: Animals and Husbandrymentioning

confidence: 99%

“…Control plasma and plasma incubated with OA were trebly diluted TBS (50 mM Tris-buffered physiological saline solution pH 7.4) and clotted with thrombin (final concentration -0.5 U/ml). The maximal velocity of polymerization (Vmax, ΔmOD/min) was recorded for each absorbance curve (22). All experiments were performed 3 times.…”

Section: Thrombin-catalyzed Fibrin Polymerizationmentioning

confidence: 99%

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Anticoagulant activities of oleanolic acid via inhibition of tissue factor expressions

Lee

Yang²,

Ku³

et al. 2012

BMB Reports

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Section: Animals and Husbandrymentioning

confidence: 99%

Section: Thrombin-catalyzed Fibrin Polymerizationmentioning

confidence: 99%

Anticoagulant activities of oleanolic acid via inhibition of tissue factor expressions

Lee

Yang²,

Ku³

et al. 2012

BMB Reports

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“…Since fibrinogen (Fg) injury induced by ONOOǦ is closely associated with cardiovascular diseases [18], the nitration sites and extents of fibrinogen were identified using LC-MS/MS. As suggested from the SDS-PAGE gel, fibrinogen polypeptide chains were damaged in the order of Ȗ, Bȕ, and AĮ as the ONOOǦ amount increased.…”

Section: Discussionmentioning

confidence: 99%

“…Nitrotyrosine is recognized as an indicator of oxidative injury and inflammation in proteins [4]. As a result of this post-translational modification induced by ONOOǦ, protein spatial conformation and associated functions are usually altered [5]. In several cases, the identification of specific nitrated proteins has assisted in illuminating the molecular mechanisms of diseases, thus inducing atherosclerosis disorders [6] and coronary artery disease [7].…”

Section: Introductionmentioning

confidence: 99%

Peroxynitrite induced fibrinogen site identification

Luo

Shi

2015

BME

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Abstract. An increasing number of peroxynitrite-mediated fibrinogen nitrifications have been associated with thrombotic diseases. However, few reports related to priority nitrified fibrinogen injury sites exist. In this paper, an improved method, which simulated the environment in vivo, was used to inspect the structural changes of fibrinogen treated with peroxynitrite and LC-MS/MS in order to investigate the fibrinogen injury sites. The SDS-PAGE results indicated that Ȗ subunits of Fg were vulnerable to oxidative/nitrative modifications induced by peroxynitrite. An in-depth analysis of fibrinogen Ȗ chain (Fg I) nitration site identification and susceptibility to peroxynitrite-utilizing LC-MS/MS strategy was performed. Based on a large dataset, the results indicated the priority injury sites during database searching were Y96, Y262, Y274, Y348, and Y363; these results could be applied to biomedical studies.

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“…Human fibrinogen seems to be highly susceptible to nitration [41,42]. Peroxynitrite induces changes in the function and the structure of human fibrinogen in vitro, generating nitrotyrosine, mostly in Aa-chain, acting on aC subunits [43], which in most vertebrates are natively unfolded regions of molecule with no stable structure [29]. Fibrinogen nitration in vivo results in increased velocity of fibrin clot formation, altered fibrin clot architecture, increased fibrin clot stiffness and reduced rate of fibrin clot lysis by plasmin [44].…”

Section: Discussionmentioning

confidence: 99%

The comparison of peroxynitrite action on bovine, porcine and human fibrinogens

et al. 2013

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Subjects of bovine and porcine flocks are sometimes susceptible to death before time of slaughter, and some of those deaths may be due to cardiovascular problems connected with stress. The role of oxidative stress in farm animals is yet unexplored. Human fibrinogen seems to be highly susceptible to nitration. Peroxynitrite produced from superoxide and nitric oxide initiates noticeable changes in the structure of human fibrinogen molecule. The objective of this work is to compare the in vitro interactions of peroxynitrite with human fibrinogen and with fibrinogen from mammals of great economic importance, namely cows and pigs. Using western blots and ELISA we show that porcine fibrinogen is susceptible to tyrosine nitration induced by peroxynitrite whereas, bovine fibrinogen is more resistant. Moreover, porcine fibrinogen polymerization is susceptible to peroxynitrite action, whereas bovine fibrinogen is the least susceptible to inhibition of polymerization caused by peroxynitrite. These observed differences may result from differences in amino acid sequence of fibrinogen chains, mostly including tyrosine content and location in the Aα chain. Protection against toxic effects of peroxynitrite activity in the circulatory system seems to be important in avoiding cardiovascular diseases and may prevent production loss in pig breeding herds.

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Different vulnerability of fibrinogen subunits to oxidative/nitrative modifications induced by peroxynitrite: Functional consequences

Cited by 88 publications

References 60 publications

Anticoagulant activities of oleanolic acid via inhibition of tissue factor expressions

Anticoagulant activities of oleanolic acid via inhibition of tissue factor expressions

Peroxynitrite induced fibrinogen site identification

The comparison of peroxynitrite action on bovine, porcine and human fibrinogens

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