TY - JOUR
T1 - Long-sarafotoxins
T2 - Characterization of a new family of endothelin-like peptides
AU - Hayashi, Mirian A.F.
AU - Ligny-Lemaire, Caroline
AU - Wollberg, Zvi
AU - Wery, Michaël
AU - Galat, Andrzej
AU - Ogawa, Tomohisa
AU - Muller, Bruno H.
AU - Lamthanh, Hung
AU - Doljansky, Yvon
AU - Bdolah, Avner
AU - Stöcklin, Reto
AU - Ducancel, Frédéric
N1 - Funding Information:
I would like to thank Pr. A. Ménez for his permanent support during that work, and also Pr. I. Ineich (Museum National d’Histoire Naturelle, Paris), Alexandra Savatier (bioMérieux), and Robert Thai (CEA/DIEP), for their contribution and collaboration in different aspects of this work. Thanks also to Ms. N. Paz for help in the preparation of the manuscript.
PY - 2004/8
Y1 - 2004/8
N2 - Sarafotoxins (SRTXs) constitute a family of vasoactive peptides that were initially isolated from the venom of Atractaspis engaddensis, and that are structurally and functionally related to endothelins (ETs). Analysis of the venom of Atractaspis microlepidota microlepidota revealed several new SRTX molecules manifesting some new structural and functional characteristics. These novel SRTXs are longer by three amino acids than the previously described SRTXs, and are designated here "long-SRTXs". Six isoforms, derived from new poly-cistronic precursors, have been identified so far in the venom of this snake. One of these isoforms, designated SRTX-m, was chemically synthesized and its biological properties were studied. Our results show that SRTX-m induces toxicity in mice, mostly due to vasoconstriction, and also that it has a lower toxicity and potency than the more potent SRTX described up to now: sarafotoxin-b (SRTX-b) from A. engaddensis.
AB - Sarafotoxins (SRTXs) constitute a family of vasoactive peptides that were initially isolated from the venom of Atractaspis engaddensis, and that are structurally and functionally related to endothelins (ETs). Analysis of the venom of Atractaspis microlepidota microlepidota revealed several new SRTX molecules manifesting some new structural and functional characteristics. These novel SRTXs are longer by three amino acids than the previously described SRTXs, and are designated here "long-SRTXs". Six isoforms, derived from new poly-cistronic precursors, have been identified so far in the venom of this snake. One of these isoforms, designated SRTX-m, was chemically synthesized and its biological properties were studied. Our results show that SRTX-m induces toxicity in mice, mostly due to vasoconstriction, and also that it has a lower toxicity and potency than the more potent SRTX described up to now: sarafotoxin-b (SRTX-b) from A. engaddensis.
KW - ET
KW - HPLC
KW - SDS-PAGE
KW - SRTX
KW - cDNA
KW - complementary deoxyribonucleic acid
KW - endothelin
KW - l-SRTX
KW - long-sarafotoxin
KW - messenger ribonucleic acid
KW - poly (A) RNA or mRNA
KW - sarafotoxin
KW - sodium dodecyl sulfate-polyacrylamide gel electrophoresis
UR - http://www.scopus.com/inward/record.url?scp=4444356635&partnerID=8YFLogxK
U2 - 10.1016/j.peptides.2004.05.010
DO - 10.1016/j.peptides.2004.05.010
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AN - SCOPUS:4444356635
SN - 0196-9781
VL - 25
SP - 1243
EP - 1251
JO - Peptides
JF - Peptides
IS - 8
ER -