Schweitz H, Vigne P, Moinier D, Frelin C, Lazdunski M
Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
J Biol Chem. 1992 Jul 15;267(20):13928-32.
This paper describes the purification, sequence, and biological properties of a 38-amino acid residue peptide from the venom of Dendroaspis angusticeps which shared important sequence homologies with natriuretic peptides. Dendroaspis natriuretic peptide (DNP) relaxed aortic strips that had been contracted by 40 mM KCl with a potency (K0.5 = 20 nM) similar to that of atrial natriuretic peptide (ANP) and larger than that of C type natriuretic peptide (CNP). The relaxing actions of ANP and DNP (both at 100 nM) were mutually exclusive. Bovine aortic endothelial cells responded to ANP (K0.5 = 3 nM) and DNP (K0.5 = 3 nM) but not to CNP by a large activation of guanylate cyclase. Rat aortic myocytes showed larger cGMP responses to CNP (K0.5 = 10 nM) than to ANP or DNP (K0.5 = 100 nM). Finally, DNP completely prevented the specific 125I-ANP binding to clearance receptors in cultured aortic myocytes with a potency (Kd = 10 nM) that was less than that of ANP (Kd = 0.3 nM). It is concluded that DNP is a new member of the family of natriuretic peptides and that it recognizes ANPA receptors and clearance, ANPc receptors, but not CNP-specific ANPB receptors.
本文描述了从绿曼巴蛇毒液中提取的一种含38个氨基酸残基的肽的纯化、序列及生物学特性，该肽与利钠肽具有重要的序列同源性。绿曼巴蛇利钠肽（DNP）可舒张由40 mM氯化钾收缩的主动脉条，其效力（半数效应浓度K0.5 = 20 nM）与心房利钠肽（ANP）相似，且大于C型利钠肽（CNP）。ANP和DNP（均为100 nM）的舒张作用相互排斥。牛主动脉内皮细胞对ANP（K0.5 = 3 nM）和DNP（K0.5 = 3 nM）有反应，但对CNP无反应，可大量激活鸟苷酸环化酶。大鼠主动脉肌细胞对CNP（K0.5 = 10 nM）的环磷酸鸟苷（cGMP）反应大于对ANP或DNP（K0.5 = 100 nM）的反应。最后，DNP可完全阻止125I-ANP与培养的主动脉肌细胞中的清除受体特异性结合，其效力（解离常数Kd = 10 nM）小于ANP（Kd = 0.3 nM）。结论是，DNP是利钠肽家族的新成员，它识别ANPA受体和清除受体、ANPc受体，但不识别CNP特异性的ANPB受体。
