Cysteine rich secretory proteins in reproduction and venom.

Cysteine rich secretory proteins in reproduction and venom.
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生殖和毒液中富含半胱氨酸的分泌蛋白。

DOI:
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发表时间:
2007
期刊:
Society of Reproduction and Fertility supplement
影响因子:
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通讯作者:
M. O’Bryan
M. O’Bryan
中科院分区:
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文献类型:
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作者:
G. Gibbs;M. O’Bryan

文献摘要

被引文献

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富含半胱氨酸的分泌蛋白(Crisp)主要存在于哺乳动物雄性生殖道和爬行动物的毒液中。Crisps是两种结构域蛋白,它们具有结构相似但进化上不同的n端结构域和具有特征的富含半胱氨酸的c端结构域,我们称之为Crisp结构域。自从它们在30年前被发现以来,Crisp对哺乳动物的研究一直集中在它们的表达定位特征上,以推断其功能。虽然这些观察无疑是重要的,但它们并没有从本质上导致对薯片的生化活性及其在精子功能或受精中的作用的理解。最近,我们证明了Crisp-2 Crisp结构域具有类似于离子通道毒素ShK和BgK的结构,并且本身能够通过ryanodine受体调节Ca2+通量。这些数据建立在爬行动物毒液薯片作为几种离子通道调节剂的先前特征的基础上,并允许首次解剖哺乳动物薯片的生化活性。
The cysteine rich secretory proteins (Crisp) are predominantly found in the mammalian male reproductive tract and in the venom of reptiles. Crisps are two domain proteins with a structurally similar yet evolutionarily diverse N-terminal domain and a characteristic cysteine rich C-terminal domain which we refer to as the Crisp domain. Since their identification 30 years ago Crisp research in mammals has focused on the characterisation of their expression localization to infer function. While no doubt important observations, these have not substantially led to an understanding of the biochemical activity of the Crisps and their role in sperm function or fertilisation. Recently, we demonstrated that the Crisp-2 Crisp domain has a structure similar to ion channel toxins ShK and BgK and was itself able to regulate Ca2+ flux through ryanodine receptors. These data build upon the previous characterizations of reptile venom Crisps as regulators of several types of ion channels and permits for the first time a dissection of the biochemical activity of mammalian Crisps.