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首页> 外文期刊>Archives of Andrology: An International Journal >Expression and phosphorylation of mitogen-activated protein kinases during spermatogenesis and epididymal sperm maturation in mice.
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Expression and phosphorylation of mitogen-activated protein kinases during spermatogenesis and epididymal sperm maturation in mice.

机译：小鼠精子发生和附睾精子成熟过程中促分裂原活化蛋白激酶的表达和磷酸化。

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摘要

The expression and phosphorylation/dephosphorylation of mitogen-activated protein (MAP) kinases during mouse spermatogenesis and epididymal sperm maturation have been investigated by immunoblotting and immunohistochemical staining with commercially available anti-ERK2 and anti-Active MAPK antibodies. Two forms of MAP kinases, p42ERK2 and p44ERK1, were expressed in a similar amount in spermatogenic cells at different stages. ERK1 and ERK2 were phosphorylated (activated) in early spermatogenic cells from primitive spermatogonia to zygotene primary spermatocytes, while only a small quantity of phosphorylated MAP kinases could be detected in pachytene primary spermatocytes and spermatids. MAP kinase activity in primative spermatogonia and preleptotene primary spermatocytes was the highest among spermatogenic cells. ERK1 and ERK2 were also present in epididymal spermatozoa, and their phosphorylation was increased while spermatozoa pass through epididymis and vas deferens for maturation. It would appear that MAP kinase activation may contribute to the mitotic proliferation of primative spermatogonia, an early phase of spermatogenic meiosis, and, later, sperm motility acquirement.
机译：已通过免疫印迹和免疫组化染色，用市售抗ERK2和抗Active MAPK抗体研究了小鼠精子发生和附睾精子成熟过程中有丝分裂原活化蛋白（MAP）激酶的表达和磷酸化/去磷酸化。两种形式的MAP激酶p42ERK2和p44ERK1在不同阶段的生精细胞中的表达量相似。 ERK1和ERK2在从原始精原细胞到合子原初生精细胞的早期生精细胞中被磷酸化（激活），而在上层初生精原细胞和精细胞中只能检测到少量的磷酸化MAP激酶。在生精细胞中，原始精原细胞和前瘦素初级精细胞中的MAP激酶活性最高。 ERK1和ERK2也存在于附睾精子中，当精子穿过附睾和输精管成熟时，它们的磷酸化增加。似乎MAP激酶的活化可能有助于原始的精原细胞的有丝分裂增殖，生精减数分裂的早期，以及随后的精子活动能力的获得。

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