.png){kind=icon}
.png){kind=icon}
Return
Functional characterization of a novel antithrombotic and thrombolytic metalloproteinase from Cerastes cerastes venom: a promising thromboprotective agent
.png){kind=icon}
PRE
AI
N
H
F
F
DOI：10.1080/15569543.2026.2636025.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
Snake venom metalloproteinases (SVMPs) are abundant multidomain enzymes with diverse biological functions. This study aimed to purify and characterize a novel SVMP, CcVMP-III, from Cerastes cerastes venom and assess its protective effects in pulmonary embolism murine model.
CcVMP-III (110 kDa) was purified by chromatographic techniques and partially sequenced using N-terminal and LC-MS/MS analyses. Biological activities were evaluated using coagulation parameters (aPTT, TT, PT), clot degradation, and fibrin plate lysis. Thromboprotective efficacy was assessed using a thrombin-induced pulmonary embolism model.
CcVMP-III was identified as a class-III SVMP containing metalloproteinase, disintegrin-like, and cysteine-rich domains. It selectively prolonged aPTT and TT without affecting PT and exhibited strong fibrinolytic and thrombolytic activities. In vivo, it significantly prevented pulmonary thrombus formation, demonstrating marked thromboprotective efficacy.
These findings emphasize the potential of CcVMP-III as a promising thromboprotective agent that may mitigate morbidity and mortality associated with thromboembolic events.
Keywords:
Cerastes cerastes
snake venom metalloproteinases
anticoagulant
thrombolytic
pulmonary embolism
cardiovascular diseases
Journal
IF:
2.4
Papers:
837
Citations:
1.8K
Organization
Cited Papers