Potent histamine-releasing activity of atrahagin, a novel snake venom metalloproteinase
| Autor: | Hua Xie, Xiao-Long Wei, Ji-Fu Wei, Wan-Yu Wang, Shao-Heng He, Yu-Liang Xiong, Yi-Ling Fu, Li-Ya Qiao, Ya-Zhen Mo, Han-Qiu Chen |
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| Rok vydání: | 2006 |
| Předmět: |
Time Factors
Reptilian Proteins Pharmacology Biology Pertussis toxin Histamine Release Biochemistry Pathogenesis Mice chemistry.chemical_compound medicine Animals Humans Mast Cells Cells Cultured Elapid Venoms chemistry.chemical_classification Mice Inbred BALB C Metalloproteinase Fibrinogen Cell Biology Mast cell Enzyme medicine.anatomical_structure chemistry Snake venom Tonsil Immunology Metalloproteases Histamine |
| Zdroj: | The International Journal of Biochemistry & Cell Biology. 38:510-520 |
| ISSN: | 1357-2725 |
| DOI: | 10.1016/j.biocel.2005.10.011 |
| Popis: | Poisonous snakebite wound is a popular disease worldwide. However, the pathogenesis remains unclear. In the present study, a novel metalloproteinase atrahagin in Chinese cobra (Naja atra) snake venom was purified, using heparin–sepharose followed by Superdex 75 gel filtration chromatography. Apart from its α-fibrinogenase activity, atrahagin potently activated human colon, lung and tonsil mast cells with the net histamine release being 25.9 ± 4.4, 17.0 ± 1.9, 13.2 ± 3.6%, respectively. Time course studies revealed that the peak histamine release induced by atrahagin occurred at 12, 12 and 8 min following incubation of the enzyme with colon, lung and tonsil mast cells, respectively. The response of mast cells to atrahagin was abolished by preincubation of the cells with metabolic inhibitors or pertussis toxin, and by removal of Ca2+ and Mg2+ from the challenge buffer. In conclusion, activation of human mast cells by atrahagin indicated that the enzyme might contribute to the pathogenesis of snakebite wound. |
| Databáze: | OpenAIRE |
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