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• W2129461444 abstract "HomeArteriosclerosis, Thrombosis, and Vascular BiologyVol. 30, No. 1Smoking Out the Cause of Thrombosis Free AccessEditorialPDF/EPUBAboutView PDFView EPUBSections ToolsAdd to favoritesDownload citationsTrack citationsPermissions ShareShare onFacebookTwitterLinked InMendeleyReddit Jump toFree AccessEditorialPDF/EPUBSmoking Out the Cause of Thrombosis Robert A. Campbell, PhD, Kellie R. Machlus, BS and Alisa S. Wolberg, PhD Robert A. CampbellRobert A. Campbell From Department of Human Molecular Biology and Genetics (R.A.C.), University of Utah, Salt Lake City, Utah; Department of Pathology and Laboratory Medicine (K.R.M., A.S.W.), University of North Carolina, Chapel Hill, NC. Search for more papers by this author , Kellie R. MachlusKellie R. Machlus From Department of Human Molecular Biology and Genetics (R.A.C.), University of Utah, Salt Lake City, Utah; Department of Pathology and Laboratory Medicine (K.R.M., A.S.W.), University of North Carolina, Chapel Hill, NC. Search for more papers by this author and Alisa S. WolbergAlisa S. Wolberg From Department of Human Molecular Biology and Genetics (R.A.C.), University of Utah, Salt Lake City, Utah; Department of Pathology and Laboratory Medicine (K.R.M., A.S.W.), University of North Carolina, Chapel Hill, NC. Search for more papers by this author Originally published1 Jan 2010https://doi.org/10.1161/ATVBAHA.109.198051Arteriosclerosis, Thrombosis, and Vascular Biology. 2010;30:7–8Cigarette smoke exposure (CSE) is known to increase the risk of arterial thrombosis; almost 40% of smoking-related deaths are associated with cardiovascular disease.1 Most research has focused on the direct cellular effects of CSE, demonstrating that increased risk of thrombosis is linked to oxidative damage to cardiomyocyte mitochondria,2 increased smooth muscle cell proliferation,3 and increased platelet aggregation.4 Studies examining the effects of CSE on hemostasis have documented decreased expression of tissue factor pathway inhibitor on endothelial cells exposed to serum from chronic smokers5 and increased plasma fibrinogen levels in smokers compared to nonsmokers.6 Few studies have examined the effects of acute CSE on clotting, but increased levels of circulating tissue factor activity7 have been demonstrated after short-term exposure to cigarette smoke. Thus, CSE appears to increase prothrombotic biomarkers and may directly promote thrombosis.See accompanying article on page 75In this issue of Arteriosclerosis, Thrombosis, and Vascular Biology, Barua et al8 strengthen the argument for a direct functional effect of CSE in thrombosis by demonstrating abnormal fibrin clot dynamics and structure in plasma from individuals exposed to acute CSE. Whereas baseline fibrin clot dynamics and structure in platelet-rich and platelet-poor plasma in nonsmokers and smokers is similar, acute CSE exposure shortens the onset and increases the rate of fibrin formation and development of fibrin clot strength as measured by thrombelastography. The authors suggest the increase in clot strength is attributable to changes in platelet function as well as changes in fibrin structure. Acute CSE effects are observed in platelet-rich plasma in the presence and absence of the platelet antagonist, Abciximab. Visual evidence using scanning electron microscopy shows decreased fibrin diameter and increased fibrin fiber density in clots formed from platelet-poor plasma isolated after acute CSE. Whereas the authors did not explicitly examine fibrinolysis in this study, previous studies have demonstrated dense fibrin networks composed of thin fibers are associated with abnormally high resistance to fibrinolysis.9 These findings suggest alteration in fibrin clot structure attributable to acute CSE plays a central role in the etiology of smoking-associated thrombosis.Although these data suggest a novel, independent means by which acute CSE contributes to the pathology of thrombosis, the findings are currently limited because they lack a specific, biochemical mechanism explaining the effects of acute CSE on clotting. Because high thrombin concentrations were added to platelet-poor plasma to induce fibrin formation in the microscopy studies, the fibrin structural abnormalities seen in this assay likely reflect fibrin(ogen) abnormalities and not contributions of endogenous thrombin generation. Thus, these data support the idea of a direct functional modification to fibrinogen. The authors suggest oxidative stress from CSE directly modifies fibrinogen and, therefore, fibrin formation and structure. Cigarette smoke contains free radicals (reactive oxygen species) and may downregulate endogenous antioxidants. Moreover, fibrinogen is susceptible to oxidation in vitro,10 and oxidative stress has been implicated in abnormal fibrin structure and stability in acute coronary syndrome.11 However, further studies are necessary to determine whether acute CSE modifies fibrinogen through oxidation or another mechanism in vivo, and whether this modification affects fibrin formation and structure. Although these data suggest direct functional effects on fibrinogen, the data do not rule out additional effects of acute CSE on plasma proteins or endogenous procoagulant activity. Because Abciximab not only inhibits platelet integrin/fibrin interactions but also reduces platelet procoagulant activity, the relative contributions of fibrinogen abnormality and effects of altered thrombin generation are difficult to ascertain from these experiments. Moreover, the authors initiate fibrin formation in the thrombelastography experiments through contact activation rather than tissue factor. Given previous reports of increased tissue factor expression in atherosclerotic plaques and its role in arterial thrombosis,12 additional studies are necessary to determine whether and how acute CSE affects tissue factor-induced fibrin formation.Although abnormal fibrin structure and stability were first reported for dysfibrinogenemia-associated coagulopathies, abnormal fibrin quality (formation, structure, or stability) can be detected in plasmas from patients with a variety of disorders (Figure). The present study complements an increasing number of reports correlating abnormal fibrin quality with hemostatic and thrombotic pathologies, including hemophilia,13,14 idiopathic venous thromboembolism,15 chronic thromboembolic pulmonary hypertension,16 cryptogenic ischemic stroke,17 myocardial infarction,18,19 and diabetes.20 Findings that acute CSE modulates fibrinogen/fibrin quality suggest a similar situation occurs in thrombosis associated with environmental toxins, as well. For example, studies showing the incidence of acute thrombotic events peaks on days after increased air pollution21,22 provide an intriguing parallel to the effects of acute CSE observed by Barua et al. Overall, these studies suggest abnormal fibrin quality is a pathological mechanism common to a number of coagulopathic disorders. Further studies are warranted to fully elucidate the contributions of altered fibrin quality to hemostatic and thrombotic diatheses, and to identify novel therapeutic targets to reverse or prevent abnormal fibrin formation. Download figureDownload PowerPointFigure. Abnormal fibrin quality has been detected in plasmas from patients with hemostatic and thrombotic disorders, and it may be a biomarker or mechanism for coagulopathy.Received October 8, 2009; revision accepted October 16, 2009. FootnotesCorrespondence to Alisa S. Wolberg, PhD, Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, 815 Brinkhous-Bullitt Building, CB #7525, Chapel Hill, NC 27599-7525. E-mail [email protected] References 1 Armour BS, Woollery T, Malarcher A, Pechacek TF, Husten C. Annual smoking-attributable mortality, years of potential life lost, and productivity losses—United States, 1997–2001. Morb Mortal Wkly Rep. 2005; 54: 625–628.MedlineGoogle Scholar2 Armani C, Landini L Jr, Leone A. Molecular and biochemical changes of the cardiovascular system due to smoking exposure. Curr Pharm Des. 2009; 15: 1038–1053.CrossrefMedlineGoogle Scholar3 Schroeter MR, Sawalich M, Humboldt T, Leifheit M, Meurrens K, Berges A, Xu H, Lebrun S, Wallerath T, Konstantinides S, Schleef R, Schaefer K. Cigarette smoke exposure promotes arterial thrombosis and vessel remodeling after vascular injury in apolipoprotein E-deficient mice. J Vasc Res. 2008; 45: 480–492.CrossrefMedlineGoogle Scholar4 Fusegawa Y, Goto S, Handa S, Kawada T, Ando Y. Platelet spontaneous aggregation in platelet-rich plasma is increased in habitual smokers. Thromb Res. 1999; 93: 271–278.CrossrefMedlineGoogle Scholar5 Barua RS, Ambrose JA, Saha DC, Eales-Reynolds LJ. Smoking is associated with altered endothelial–derived fibrinolytic and antithrombotic factors: an in vitro demonstration. Circulation. 2002; 106: 905–908.LinkGoogle Scholar6 Grines CL, Topol EJ, O'Neill WW, George BS, Kereiakes D, Phillips HR, Leimberger JD, Woodlief LH, Califf RM. Effect of cigarette smoking on outcome after thrombolytic therapy for myocardial infarction. Circulation. 1995; 91: 298–303.CrossrefMedlineGoogle Scholar7 Sambola A, Osende J, Hathcock J, Degen M, Nemerson Y, Fuster V, Crandall J, Badimon JJ. Role of risk factors in the modulation of tissue factor activity and blood thrombogenicity. Circulation. 2003; 107: 973–977.LinkGoogle Scholar8 Barua RS, Sy F, Srikanth S, Huang G, Javed U, Buhari C, Margosan D, Ambrose JA. Effects of cigarette smoking exposure on cbt dynamics and fibrin structure: an ex vivo investigation. Arterioscler Thromb Vasc Biol. 2010; 30: 75–79.LinkGoogle Scholar9 Collet JP, Park D, Lesty C, Soria J, Soria C, Montalescot G, Weisel JW. Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy. Arterio Thromb Vasc Biol. 2000; 20: 1354–1361.CrossrefMedlineGoogle Scholar10 Shacter E, Williams JA, Lim M, Levine RL. Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay. Free Radic Biol Med. 1994; 17: 429–437.CrossrefMedlineGoogle Scholar11 Undas A, Szuldrzynski K, Stepien E, Zalewski J, Godlewski J, Tracz W, Pasowicz M, Zmudka K. Reduced clot permeability and susceptibility to lysis in patients with acute coronary syndrome: effects of inflammation and oxidative stress. Atherosclerosis. 2008; 196: 551–557.CrossrefMedlineGoogle Scholar12 Matetzky S, Tani S, Kangavari S, Dimayuga P, Yano J, Xu H, Chyu KY, Fishbein MC, Shah PK, Cercek B. Smoking increases tissue factor expression in atherosclerotic plaques: implications for plaque thrombogenicity. Circulation. 2000; 102: 602–604.CrossrefMedlineGoogle Scholar13 He S, Blomback M, Jacobsson Ekman G, Hedner U. The role of recombinant factor VIIa (FVIIa) in fibrin structure in the absence of FVIII/FIX. J Thromb Haemost. 2003; 1: 1215–1219.CrossrefMedlineGoogle Scholar14 Wolberg AS, Allen GA, Monroe DM, Hedner U, Roberts HR, Hoffman M. High dose factor VIIa enhances clot stability in a model of hemophilia B. Br J Haematol. 2005; 131: 645–655.CrossrefMedlineGoogle Scholar15 Undas A, Zawilska K, Ciesla-Dul M, Lehmann-Kopydlowska A, Skubiszak A, Ciepluch K, Tracz W Altered fibrin clot structure/function in patients with idiopathic venous thromboembolism and in their relatives. Blood. 2009.Google Scholar16 Morris TA, Marsh JJ, Chiles PG, Magana MM, Liang NC, Soler X, Desantis DJ, Ngo D, Woods VL Jr. High prevalence of dysfibrinogenemia among patients with chronic thromboembolic pulmonary hypertension. Blood. 2009; 114: 1929–1936.CrossrefMedlineGoogle Scholar17 Undas A, Podolec P, Zawilska K, Pieculewicz M, Jedlinski I, Stepien E, Konarska-Kuszewska E, Weglarz P, Duszynska M, Hanschke E, Przewlocki T, Tracz W. Altered fibrin clot structure/function in patients with cryptogenic ischemic stroke. Stroke. 2009; 40: 1499–1501.LinkGoogle Scholar18 Fatah K, Silveira A, Tornvall P, Karpe F, Blomback M, Hamsten A. Proneness to formation of tight and rigid fibrin gel structures in men with myocardial infarction at a young age. Thromb Haemost. 1996; 76: 535–540.CrossrefMedlineGoogle Scholar19 Collet JP, Allali Y, Lesty C, Tanguy ML, Silvain J, Ankri A, Blanchet B, Dumaine R, Gianetti J, Payot L, Weisel JW, Montalescot G. Altered fibrin architecture is associated with hypofibrinolysis and premature coronary atherothrombosis. Arterioscler Thromb Vasc Biol. 2006; 26: 2567–2573.LinkGoogle Scholar20 Dunn EJ, Ariens RA, Grant PJ. The influence of type 2 diabetes on fibrin structure and function. Diabetologia. 2005; 48: 1198–1206.CrossrefMedlineGoogle Scholar21 Vermylen J, Nemmar A, Nemery B, Hoylaerts MF. Ambient air pollution and acute myocardial infarction. J Thromb Haemost. 2005; 3: 1955–1961.CrossrefMedlineGoogle Scholar22 Mills NL, Donaldson K, Hadoke PW, Boon NA, MacNee W, Cassee FR, Sandstrom T, Blomberg A, Newby DE. Adverse cardiovascular effects of air pollution. Nat Clin Pract Cardiovasc Med. 2009; 6: 36–44.CrossrefMedlineGoogle Scholar Previous Back to top Next FiguresReferencesRelatedDetailsCited By Jeon S, Hong J, Lee H, Kim E, Lee H, Kim Y, Ri H and Lee J (2021) Acute lower extremity arterial thrombosis after intraocular foreign body removal under general anesthesia: A case report and review of literature, World Journal of Clinical Cases, 10.12998/wjcc.v9.i27.8232, 9:27, (8232-8241), Online publication date: 26-Sep-2021. Wang J and Wang X (2011) The Process of Cigarette Smoking Cigarette Smoke Toxicity, 10.1002/9783527635320.ch3, (37-53), Online publication date: 23-Feb-2011. January 2010Vol 30, Issue 1 Advertisement Article InformationMetrics https://doi.org/10.1161/ATVBAHA.109.198051PMID: 20018940 Originally publishedJanuary 1, 2010 PDF download Advertisement" @default.
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