TY - JOUR
T1 - Screening for fibrinolytic activity in eight Viperid venoms
AU - Ramírez, María Susana
AU - Sánchez, Elda E.
AU - García-Prieto, Celia
AU - Pérez, John C.
AU - Rodríguez Chapa, Gloria
AU - McKeller, Morgan R.
AU - Ramírez, Rosemary
AU - De Anda, Yvonne
N1 - Funding Information:
This research was supported by NIH/MBRS No. GM08107-23, NIH/RIMI No. 2P20RR11594-03, and the Ronald E. McNair Scholars Program. Special thanks to Lucy Arispe, Curator of live collection, and Nora Diaz DeLeon for her technical support.
PY - 1999/9
Y1 - 1999/9
N2 - Snake venoms contain direct-acting fibrinolytic metalloproteinases (MMP) that could have important applications in medicine. Fibrinolytic enzymes isolated from venom can induce in vitro clot lysis by directly acting on a fibrin clot. The most ideal fibrinolytic enzyme would have high affinity for clots, dissolve clots directly without causing hemorrhage, and would not be neutralized in vivo by endogenous metalloproteinase inhibitors. The purpose of this study was to compare DEAE/HPLC venom profiles from Viperid snakes and identify fractions that contain fibrinolytic activity with no hemorrhagic activity and are not neutralized by animal sera. The sera selected were from four (Virginia opossum, Gray woodrat, Mexican ground squirrel, and Hispid cottonrat) animals known to neutralize hemorrhagic activity in snake venoms. Nineteen fractions from the Viperid venoms had fibrinolytic activity. Agkistrodon venom fractions contained the highest specific fibrinolytic activities. A. piscivorus leucostoma fraction 4 contained a high specific fibrinolytic activity, no hemorrhagic activity, and the fibrinolytic activity was not neutralized by the proteinase inhibitors of the four animal sera. A. contortrix laticinctus fraction 1 also had a high specific fibrinolytic activity and no hemorrhagic activity. However, the fibrinolytic activity was neutralized by Didelphis virginiana (Virginia opossum) serum. Copyright (C) 1999 Elsevier Science Inc.
AB - Snake venoms contain direct-acting fibrinolytic metalloproteinases (MMP) that could have important applications in medicine. Fibrinolytic enzymes isolated from venom can induce in vitro clot lysis by directly acting on a fibrin clot. The most ideal fibrinolytic enzyme would have high affinity for clots, dissolve clots directly without causing hemorrhage, and would not be neutralized in vivo by endogenous metalloproteinase inhibitors. The purpose of this study was to compare DEAE/HPLC venom profiles from Viperid snakes and identify fractions that contain fibrinolytic activity with no hemorrhagic activity and are not neutralized by animal sera. The sera selected were from four (Virginia opossum, Gray woodrat, Mexican ground squirrel, and Hispid cottonrat) animals known to neutralize hemorrhagic activity in snake venoms. Nineteen fractions from the Viperid venoms had fibrinolytic activity. Agkistrodon venom fractions contained the highest specific fibrinolytic activities. A. piscivorus leucostoma fraction 4 contained a high specific fibrinolytic activity, no hemorrhagic activity, and the fibrinolytic activity was not neutralized by the proteinase inhibitors of the four animal sera. A. contortrix laticinctus fraction 1 also had a high specific fibrinolytic activity and no hemorrhagic activity. However, the fibrinolytic activity was neutralized by Didelphis virginiana (Virginia opossum) serum. Copyright (C) 1999 Elsevier Science Inc.
KW - Agkistrodon
KW - Crotalinae
KW - Fibrin clot
KW - Fibrinolytic enzymes
KW - Metalloproteinases
KW - Proteinase inhibitors
KW - Thrombolytic therapy
KW - Venom
KW - Viperid
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U2 - 10.1016/S0742-8413(99)00056-0
DO - 10.1016/S0742-8413(99)00056-0
M3 - Article
C2 - 10579653
AN - SCOPUS:0345035486
SN - 0742-8413
VL - 124
SP - 91
EP - 98
JO - Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology
JF - Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology
IS - 1
ER -