Endothelin-like peptides.
Mammalian endothelins (ETs) and snake venom sarafotoxins (SRTXs) comprise structurally and functionally related potent vasoconstrictor isopeptides that act on the vascular system via identical receptors. This similarity is remarkable, since SRTXs are highly toxic components isolated from the venoms of snakes of the genus Atractaspis of the Atractaspididae family, while ETs are endogenous hormones of the mammalian vascular system. Since the first functional and structural description of SRTXs in 1988, the full extent of their natural diversity has become increasingly apparent, and this has led to the characterization of new families of endothelin-like peptides. Based on a combination of conventional biochemical approaches and the latest molecular biology and mass spectrometry techniques, this review describes the more recent panel of SRTX isopeptides isolated from various snake species within the Atractaspididae family, but also the similarities and differences that exist between sarafotoxins and endothelins in terms of their metabolism, genetic origin, structure and functional sites.
Ducancel
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Département d'ingénierie et d'études des protéines, Bâtiment 152, CEA de Saclay, 91191, Gif sur Yvette Cedex, France. frederic.ducancel@cea.fr
D000595:Amino Acid Sequence; D000818:Animals; D016232:Endothelins / Q000737:chemistry / Q000494:pharmacology / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013329:Structure-Activity Relationship; D014757:Viper Venoms / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology
D016232:Endothelins; D010455:Peptides; D014757:Viper Venoms; C057354:sarafotoxins s6