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首页> 外文期刊>Chinese science bulletin >A new scorpion polypeptide enhances the binding of radiolabeled-ryanodine on ryanodine receptor in sarcoplasmic reticulum of rabbit skeletal muscle
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A new scorpion polypeptide enhances the binding of radiolabeled-ryanodine on ryanodine receptor in sarcoplasmic reticulum of rabbit skeletal muscle

机译：一种新的蝎多肽增强了兔骨骼肌肌浆网中放射性标记的ryanodine与ryanodine受体的结合

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摘要

RYANODINE is a toxic alkaloid from the plant Ryania speciosa Vahl. It selectively binds to the Ca~(2+) release channel on skeletal and cardiac heavy sarcoplasmic reticulum (HSR) and has been Vised as a tool to study the channels on the membrane of intracellular Ca~(2+) stores. However, ryanodine used as a probe for the function of ryanodine receptor (RyR) seems to be limited. For instance, ryanodine has extremely slow association and dissociation kinetics to its receptors. In addition, the effects ofryanodine to mediate the Ca~(2+) permeability of the HSR was shown to be in a non-linearly dose-dependent manner. Recently, Valdivia et al. have indicated that only the venom of Buthotus hottentota, out of eight genera of scorpion venoms tested, and high affinity peptide component(s) with a molecular size of 5 000--8 000 u in the venom selectively increased the binding of [~3H]-ryanodine to the receptor and opened the Ca~(2+) release channel on HSR of rabbit skeletal muscle and bovine ventricle and ratbrain micro-somes. Here we report the purification and partial amino acid sequence of a novel active pep-tide from Chinese scorpion Buthus martensi Karsch that enhances selectively the binding of radiolabeled-ryanodine on ryanodine receptor in HSR of rabbit skeletal muscle.
机译：RYANODINE是来自植物Ryania speciosa Vahl的有毒生物碱。它选择性地与骨骼和心脏重质浆网（HSR）上的Ca〜（2+）释放通道结合，已被视作研究细胞内Ca〜（2+）膜上通道的工具。然而，用作雷诺定受体（RyR）功能的探针的雷诺定似乎受到限制。例如，ryanodine与受体的缔合和解离动力学极其缓慢。此外，研究显示，ryanodine介导高铁的Ca〜（2+）渗透性具有非线性的剂量依赖性。最近，瓦尔迪维亚等。已经表明，在所测试的蝎子毒液的八属中，只有Buthotus hottentota的毒液和该毒液中分子大小为5 000--8 000 u的高亲和力肽组分选择性地增加了[〜3H ] -ryanodine进入受体，并在兔骨骼肌和牛脑室和大鼠脑微体的HSR上打开Ca〜（2+）释放通道。在这里，我们报道了来自中国蝎子Buthus martensi Karsch的一种新型活性肽的纯化和部分氨基酸序列，该肽选择性增强了放射性标记的ryanodine对兔骨骼肌HSR中ryanodine受体的结合。

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