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The putative chaperone calmegin is required for sperm fertility

机译：假定的伴侣伴侣卡介蛋白是精子受精所必需的

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摘要

The proper folding of newly synthesized membrane proteins in the endoplasmic reticulum (ER) is required for the formation of functional mature proteins. Calnexin is a ubiquitous ER chaperone that plays a major role in quality control by retaining incompletely folded or misfolded proteins. In contrast to other known chaperones such as heat-shock proteins, BiP and calreticulin, calnexin is an integral membrane protein. Calmegin is a testis-specific ER protein that is homologous to calnexin. Here we show that calmegin binds to nascent polypeptides during spermatogenesis, and have analysed its physiological function by targeted disruption of its gene. Homozygous-null male mice are nearly sterile even though spermatogenesis is morphologically normal and mating is normal. In vitro, sperm from homozygous-null males do not adhere to the egg extracellular matrix (zona pellucida), and this defect may explain the observed infertility. These results suggest that calmegin functions as a chaperone for one or more sperm surface proteins that mediate the interactions between sperm and egg. The defective zona pellucida-adhesion phenotype of sperm from calmegin-deficient mice is reminiscent of certain cases of unexplained infertility in human males.
机译：新合成的膜蛋白在内质网（ER）中的正确折叠是形成功能成熟蛋白所必需的。 Calnexin是一种普遍存在的ER分子伴侣，通过保留不完全折叠或错误折叠的蛋白质在质量控制中起主要作用。与其他已知的伴侣蛋白（例如热激蛋白，BiP和钙网蛋白）相反，钙粘蛋白是必不可少的膜蛋白。 Calmegin是睾丸特异性的ER蛋白，与Calnexin同源。在这里，我们显示Calegin在生精过程中与新生多肽结合，并通过有针对性地破坏其基因来分析其生理功能。即使精子发生在形态上是正常的并且交配是正常的，纯合子无效的雄性小鼠也几乎是不育的。在体外，纯合无效男性的精子不粘附于卵细胞外基质（透明带），这种缺陷可能解释了观察到的不育。这些结果表明，钙镁蛋白作为一种或多种精子表面蛋白的伴侣，介导精子和卵之间的相互作用。 Calegegin缺陷小鼠精子的透明带透明带粘附表型缺陷，使人想起某些无法解释的男性雄性不育病例。

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