TY - JOUR
T1 - Resistance of the Eegyptian mongoose to sarafotoxins
AU - Bdolah, Avner
AU - Kochva, Elazar
AU - Ovadia, Michael
AU - Kinamon, Sara
AU - Wollberg, Zvi
N1 - Funding Information:
.4l ~l,rlo,l~ll~l~,~Tchle,r aou,tth.so rs wish to thank Mr D. Gonen for technical assistance and Ms N. Paz for critical reading of the manuscript. This work was partially supported by the Rose and Norman Lederer chair in Experimental Biology (EK).
PY - 1997/8
Y1 - 1997/8
N2 - The Egyptian mongoose (Herpestes ichneumon) is known for its resistance to viperid and elapid venoms. The current work demonstrates that it is also resistant to the venom of Atractaspis and its most toxic component, sarafotoxin-b. Intravenous administration of this toxin, at a dose of about 13 times LD100 for mice, resulted in disturbance in electrocardiograms in the mongoose, which returned to normal after several hours. Sarafotoxin-b failed to induce contraction of mongoose aortal preparations. Endothelin-1, which was demonstrated in tissue extracts of the mongoose by immunological methods, induced contraction of the isolated mongoose aorta. This contraction, however, was greatly reduced when endothelin-I was applied on top of sarafotoxin-b. Binding studies revealed endothelin/sarafotoxin-specific binding sites in brain and cardiovascular preparations of the mongoose. It is suggested that some structural features of endothelin/sarafotoxin receptors in the mongoose enable them to differentiate between the two peptides.
AB - The Egyptian mongoose (Herpestes ichneumon) is known for its resistance to viperid and elapid venoms. The current work demonstrates that it is also resistant to the venom of Atractaspis and its most toxic component, sarafotoxin-b. Intravenous administration of this toxin, at a dose of about 13 times LD100 for mice, resulted in disturbance in electrocardiograms in the mongoose, which returned to normal after several hours. Sarafotoxin-b failed to induce contraction of mongoose aortal preparations. Endothelin-1, which was demonstrated in tissue extracts of the mongoose by immunological methods, induced contraction of the isolated mongoose aorta. This contraction, however, was greatly reduced when endothelin-I was applied on top of sarafotoxin-b. Binding studies revealed endothelin/sarafotoxin-specific binding sites in brain and cardiovascular preparations of the mongoose. It is suggested that some structural features of endothelin/sarafotoxin receptors in the mongoose enable them to differentiate between the two peptides.
UR - http://www.scopus.com/inward/record.url?scp=0030610956&partnerID=8YFLogxK
U2 - 10.1016/S0041-0101(97)00019-6
DO - 10.1016/S0041-0101(97)00019-6
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AN - SCOPUS:0030610956
SN - 0041-0101
VL - 35
SP - 1251
EP - 1261
JO - Toxicon
JF - Toxicon
IS - 8
ER -