The structure of helokinestatin-5 and its biosynthetic precursor from Gila monster (Heloderma suspectum) venom: Evidence for helokinestatin antagonism of bradykinin-induced relaxation of rat tail artery smooth muscle

详细信息    查看全文

• 作者：Yao Zhang ; Lei Wang ; Mei Zhou ; Zhihao Zhou ; Xiaole Chen ; Tianbao Chen ; HangFai Kwok ; Craig Ivanyi ; Chris Shaw
• 关键词：Lizard ; Venom ; Bradykinin ; Antagonist ; Mass spectrometry ; Molecular cloning
• 刊名：Peptides
• 出版年：2010
• 出版时间：August 2010
• 年：2010
• 卷：31
• 期：8
• 页码：1555-1561
• 全文大小：1113 K

文摘

Here we report the primary structure of a novel peptide, named helokinestatin-5 (VPPPLQMPLIPR), from the venom of the Gila monster (Heloderma suspectum). Helokinestatin-5 differs in structure from helokinestatin-3 by deletion of a single prolyl residue in the N-terminally located polyproline region. Two different biosynthetic precursors were consistently cloned from a venom-derived cDNA library. The first encoded helokinestatins 1–4 and a single copy of C-type natriuretic peptide, as previously described, whereas the second was virtually identical, lacking only a single prolyl codon as found in the mature attenuated helokinestatin-5 peptide. Helokinestatins 1–3 and 5 were synthesized by solid-phase fmoc chemistry and each synthetic replicate was found to antagonize the relaxation effect induced by bradykinin on rat tail artery smooth muscle. Helokinestatins thus represent a novel family of vasoactive peptides from the venom of helodermatid lizards.