Human dynein and sperm pathology.
Human dynein and sperm pathology.
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人类动力蛋白和精子病理学。
DOI：
10.1083/jcb.88.1.102
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发表时间：
1981-01
影响因子：
7.8
通讯作者：
Renieri, T
中科院分区：
文献类型：
--
作者：
Baccetti, B;Burrini, A G;Pallini, V;Renieri, T
本文用电镜、SDS-聚丙烯酰胺凝胶电泳和ATP酶活性测定等方法对正常结构和轴丝缺陷（轴丝缺失、臂缺失或中央结构缺失）的人精子进行了研究。正常人精子具有高分子量多肽的补体，其电泳迁移类似于海胆和其他哺乳动物精子动力蛋白。人精子的高分子量条带按电泳迁移率增加的顺序排列为1 ~ 4条，在缺乏轴丝的精子中全部缺失。双峰臂的缺失与带2、3和4的缺失相一致;中心结构的缺失与带2的强度降低相一致。在后两种异常情况下，带1具有增加的强度。这些数据暂时解释归因于形成带3和4的臂结构的多肽，而带2应该包含位于臂和中心结构的多肽的混合物;这些异常精子包含聚集在带1中的修饰的多肽。组织化学ATP酶染色表明，这种酶主要定位于双臂，在较小程度上，在中央结构。
Human spermatozoa with normal structure and with different axonemal deficiencies (absence of axoneme, of arms, or of central structures) were studied by electron microscopy, SDS-polyacrylamide gel electrophoresis, and ATPase activity measurements. Normal human sperm possess a complement of high molecular weight polypeptides with an electrophoretic migration similar to that of sea urchin and other mammalian sperm dyneins. Human high molecular weight bands are numbered one to four in order of increasing of electrophoretic mobility; all of them are absent in spermatozoa that lack axoneme. The absence of doublet arms, coincides with the absence of bands 2, 3, and 4; the absence of central structures coincides with a reduction in intensity of band 2. In the latter two abnormal conditions, band 1 has an increased intensity. The data are tentatively interpreted by attributing the polypeptides forming bands 3 and 4 to the arm structure, whereas band 2 is supposed to contain a mixture of polypeptides localized in the arms and in the central structures; these abnormal sperm contain modified polypeptides which gather in band 1. Histochemical ATPase stainings indicate that this enzyme is localized mainly in the doublet arms and, to a minor extent, in the central structures.