{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,3,22]],"date-time":"2025-03-22T10:16:10Z","timestamp":1742638570071},"reference-count":26,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2016,9,16]],"date-time":"2016-09-16T00:00:00Z","timestamp":1473984000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Department of Anesthesiology"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Basic Clin Pharma Tox"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Since the introduction of antivenom administration over a century ago to treat venomous snake bite, it has been the most effective therapy for saving life and limb. However, this treatment is not always effective and not without potential life\u2010threatening side effects. We tested a new paradigm to abrogate the plasmatic anticoagulant effects of fibrinogenolytic snake venom metalloproteinases (SVMP) by inhibiting these Zn<jats:sup>+2<\/jats:sup>\u2010dependent enzymes directly with carbon monoxide (CO) exposure. Assessment of the fibrinogenolytic effects of venoms collected from the Arizona black rattlesnake, Northern Pacific rattlesnake, Western cottonmouth, Eastern cottonmouth, Broad\u2010banded copperhead and Southern copperhead on human plasmatic coagulation kinetics was performed with thrombelastography <jats:italic>in vitro<\/jats:italic>. Isolated exposure of all but one venom (Southern copperhead) to CO significantly decreased the ability of the venoms to compromise coagulation. These results demonstrated that direct inhibition of transition metal\u2010containing venom enzymes by yet to be elucidated mechanisms (e.g. <jats:styled-content style=\"fixed-case\">CO<\/jats:styled-content>, binding to Zn<jats:sup>+2<\/jats:sup> or displacing Zn<jats:sup>+2<\/jats:sup> from the catalytic site, <jats:styled-content style=\"fixed-case\">CO<\/jats:styled-content> binding to histidine residues) can in many instances significantly decrease fibrinogenolytic activity. This new paradigm of CO\u2010based inhibition of the anticoagulant effects of SVMP could potentially diminish haemostatic compromise in envenomed patients until antivenom can be administered.<\/jats:p>","DOI":"10.1111\/bcpt.12654","type":"journal-article","created":{"date-parts":[[2016,8,22]],"date-time":"2016-08-22T08:04:48Z","timestamp":1471853088000},"page":"207-212","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Direct Inhibitory Effects of Carbon Monoxide on Six Venoms Containing Fibrinogenolytic Metalloproteinases"],"prefix":"10.1111","volume":"120","author":[{"given":"Vance G.","family":"Nielsen","sequence":"first","affiliation":[{"name":"The Department of Anesthesiology University of Arizona College of Medicine Tucson AZ USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philip A.","family":"Losada","sequence":"additional","affiliation":[{"name":"The Department of Anesthesiology University of Arizona College of Medicine Tucson AZ USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2016,9,16]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1136\/bmj.2.1859.399"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1067\/mem.2001.113372"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2010.09.014"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.wem.2014.11.019"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1097\/MBC.0b013e32834aa7b0"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1097\/MBC.0000000000000128"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10534-016-9909-5"},{"key":"e_1_2_7_9_1","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1097\/MBC.0000000000000440","article-title":"Iron and carbon monoxide attenuate degradation of plasmatic coagulation by Crotalus atrox venom","volume":"27","author":"Nielsen VG","year":"2016","journal-title":"Blood Coagul Fibrinolysis"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1111\/bcpt.12504"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1097\/MBC.0000000000000529"},{"key":"e_1_2_7_12_1","first-page":"403","article-title":"Carbon monoxide reduces the expression and activity of matrix metalloproteinases 1 and 2 in alveolar epithelial cells","volume":"51","author":"Desmard M","year":"2005","journal-title":"Cell Mol Biol"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2010.02.028"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0305-0491(93)90025-Z"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2009.04.008"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/0020-711X(93)90016-8"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.2174\/1568006043335754"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(89)90183-9"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1097\/MBC.0000000000000146"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00289a009"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1103\/PhysRevB.82.165401"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja505318p"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1177\/15353702-0322805-09"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00424-011-0924-7"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1165\/rcmb.2008-0458OC"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.198010"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1152\/japplphysiol.00726.2015"}],"container-title":["Basic &amp; 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