{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,6,17]],"date-time":"2025-06-17T23:23:52Z","timestamp":1750202632482},"reference-count":21,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2017,8,6]],"date-time":"2017-08-06T00:00:00Z","timestamp":1501977600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100007899","name":"University of Arizona","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007899","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Basic Clin Pharma Tox"],"published-print":{"date-parts":[[2018,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Envenomation by haemotoxic enzymes remains a significant source of human morbidity and mortality worldwide, with administration of long\u2010acting or multiple doses of antivenom first\u2010line therapy. However, coagulopathy can still occur and recur. Of interest, it has been recently demonstrated that direct, isolated exposure of snake venom enzymes with fibrinogenolytic activity to carbon monoxide (CO) abrogates venom\u2010mediated loss of coagulation in human plasma. These observations of CO inhibition of venom fibrinogenolytic activity were subsequently repeated in rabbit whole blood. This study sought to translate these findings in an <jats:italic>in vivo<\/jats:italic> rabbit model of envenomation with fibrinogenolytic <jats:italic>Crotalus atrox<\/jats:italic> venom. Sedated rabbits were intravenously administered <jats:italic>C. atrox<\/jats:italic> venom (400 \u03bcg\/kg) pre\u2010exposed to 0 or 1000 \u03bcM carbon monoxide\u2010releasing molecule\u20102 (CORM\u20102) <jats:italic>in vitro<\/jats:italic>. Arterial whole\u2010blood samples demonstrated that compared to pre\u2010envenomation values, the CORM\u20102\u2010na\u00efve venom significantly prolonged the onset of coagulation, decreased the velocity of clot growth and decreased clot strength as determined by thromboelastography an hour after venom injection. In contrast, CORM\u20102 pre\u2010exposure prevented or attenuated <jats:italic>C. atrox<\/jats:italic> venom effects on coagulation kinetics. Future studies to determine whether rabbits injected with such venom subcutaneously\/intramuscularly can have consequent coagulopathy abrogated by injection of carbon monoxide\u2010releasing molecules into the \u2018bite site\u2019 are justified.<\/jats:p>","DOI":"10.1111\/bcpt.12846","type":"journal-article","created":{"date-parts":[[2017,7,10]],"date-time":"2017-07-10T08:12:46Z","timestamp":1499674366000},"page":"82-86","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["<i>Crotalus atrox<\/i> Venom Exposed to Carbon Monoxide Has Decreased Fibrinogenolytic Activity <i>In Vivo<\/i> in Rabbits"],"prefix":"10.1111","volume":"122","author":[{"given":"Vance G.","family":"Nielsen","sequence":"first","affiliation":[{"name":"Department of Anesthesiology University of Arizona College of Medicine Tucson AZ USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2017,8,6]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tmrv.2014.09.005"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.3109\/15563650.2014.974263"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10534-016-9963-z"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1039\/C6MD00336B"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11239-016-1442-4"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1111\/bcpt.12654"},{"key":"e_1_2_7_8_1","article-title":"Characterization of the rabbit as an in vitro and in vivo model to assess the effects of fibrinogenolytic activity of snake venom on coagulation","author":"Nielsen VG","journal-title":"Basic Clin Pharmacol Toxicol"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1097\/00000539-200007000-00007"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2143(97)90040-8"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.thromres.2013.12.004"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0165-1838(81)90085-0"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1249\/01.mss.0000210205.17823.74"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuroscience.2007.12.002"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(91)80615-A"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1161\/01.ATV.20.4.1162"},{"key":"e_1_2_7_17_1","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1042\/bj1970661","article-title":"Characterization of the inhibition of fibrin assembly by fibrinogen fragment D","volume":"197","author":"Williams JE","year":"1981","journal-title":"Biochem J"},{"key":"e_1_2_7_18_1","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0049-3848(82)90073-1","article-title":"Quantitation of the inhibitory effect of fibrinogen and its degradation products on fibrin polymerization","volume":"27","author":"Belitser VA","year":"1982","journal-title":"Thromb Res"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00311a021"},{"key":"e_1_2_7_20_1","doi-asserted-by":"crossref","first-page":"35988","DOI":"10.1038\/srep35988","article-title":"The effect of physiological levels of South African puff adder (Bitis arietans) snake venom on blood cells: an in vitro model","volume":"6","author":"Strydom MA","year":"2016","journal-title":"Sci Rep"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1159\/000447895"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2012.04.019"}],"container-title":["Basic &amp; 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