Thrombolytic protein from cobra venom with anti-adhesive properties
A metalloproteinase anticoagulant toxin of molecular weight 66 kDa has been purified from the venom of Indian monocled cobra (Naja kaouthia). This toxin named as NKV 66 cleaved fibrinogen in a dose and time dependent manner. The digestion process was specific to Aα chain and cleaved fibrinogen to pe...
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Published in | Archives of biochemistry and biophysics Vol. 590; pp. 20 - 26 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
15.01.2016
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Subjects | |
Online Access | Get full text |
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Summary: | A metalloproteinase anticoagulant toxin of molecular weight 66 kDa has been purified from the venom of Indian monocled cobra (Naja kaouthia). This toxin named as NKV 66 cleaved fibrinogen in a dose and time dependent manner. The digestion process was specific to Aα chain and cleaved fibrinogen to peptide fragments. NKV 66 completely liquefied the fibrin clots developed in vitro in 18 h. Plasma recalcification time and thrombin time were significantly prolonged following treatment of plasma with NKV 66. NKV 66 significantly inhibited ADP and collagen induced platelet aggregation in a dose dependent manner. It showed disintegrin like activity on A549 cells cultured in vitro. About 40% inhibition of adherence of A549 cells to matrix was observed following NKV 66 treatment also NKV 66 treated A549 cells were drastically inhibited from passing through the matrix in cell invasion assays in vitro, suggesting anti-adhesive properties of NKV 66.
•A novel 66 kDa protein toxin isolated from Indian monocled cobra (Naja kaouthia) venom by a combination of ion-exchange chromatography and RP-HPLC.•The toxin was named NKV 66.•NKV 66 showed thrombolytic and fibrinogenolytic activities in vitro.•NKV 66 inhibits collagen and ADP induced platelet aggregation.•NKV 66 showed disintegrin like activity and affected migration of A549 cells. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/j.abb.2015.11.006 |