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单克隆抗体可诱导海胆精子表面抗原发生易位、成斑和脱落。

Monoclonal antibodies induce the translocation, patching, and shedding of surface antigens of sea urchin spermatozoa.

作者信息

Trimmer J S, Vacquier V D

机构信息

Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego 92093.

出版信息

Exp Cell Res. 1988 Mar;175(1):37-51. doi: 10.1016/0014-4827(88)90253-4.

DOI:10.1016/0014-4827(88)90253-4
PMID:3278914
Abstract

Monoclonal antibodies reacting with external domains of plasma membrane proteins of sea urchin spermatozoa cause the reversible aggregation of sperm. The rate of disaggregation is temperature dependent indicating the involvement of membrane fluidity. Immunofluorescence shows that disaggregation is temporally correlated with the movement of surface-bound antibody into large aggregates which are then shed from the cell surface. Electrophoretic analysis of the shed antigens shows that they resemble the total complement of proteins of isolated sperm membranes. The translocation and shedding of surface-bound ligands may be a common property of eukaryotic flagellar membranes.

摘要

与海胆精子质膜蛋白外部结构域发生反应的单克隆抗体可导致精子可逆性聚集。解聚速率取决于温度,这表明膜流动性参与其中。免疫荧光显示,解聚在时间上与表面结合抗体向大聚集体的移动相关,随后这些聚集体从细胞表面脱落。对脱落抗原的电泳分析表明,它们类似于分离出的精子膜蛋白的总补体。表面结合配体的易位和脱落可能是真核生物鞭毛膜的共同特性。

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Monoclonal antibodies induce the translocation, patching, and shedding of surface antigens of sea urchin spermatozoa.单克隆抗体可诱导海胆精子表面抗原发生易位、成斑和脱落。
Exp Cell Res. 1988 Mar;175(1):37-51. doi: 10.1016/0014-4827(88)90253-4.
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Monoclonal antibodies to a membrane glycoprotein induce the phosphorylation of histone H1 in sea urchin spermatozoa.针对一种膜糖蛋白的单克隆抗体可诱导海胆精子中组蛋白H1的磷酸化。
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引用本文的文献

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3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography.冷冻电子断层扫描揭示静止状态下真核生物鞭毛的三维结构
Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15889-94. doi: 10.1073/pnas.0508274102. Epub 2005 Oct 24.
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Monoclonal antibodies to a membrane glycoprotein induce the phosphorylation of histone H1 in sea urchin spermatozoa.针对一种膜糖蛋白的单克隆抗体可诱导海胆精子中组蛋白H1的磷酸化。
J Cell Biol. 1988 Dec;107(6 Pt 1):2021-7. doi: 10.1083/jcb.107.6.2021.