FUNCTION OF MACAQUE SPERM PROTEINS IN FERTILIZATION

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 目的：我们实验室长期以来一直致力于鉴定和鉴定精子表面蛋白，这些蛋白在精子与女性生殖道的液体和细胞的相互作用中发挥作用。我们在非人类灵长类动物身上的发现与人类生殖方面的问题相关，为不孕不育的原因提供了见解，并确定了可能的避孕目标。我们之前报道过DEFB126(以前的ESP13.2)覆盖在猕猴精子的整个表面，并一直保持到精子获得能力。在精子获能过程中，DEFB126的释放是精子识别和结合透明带所必需的，这表明DEFB126掩盖了精子表面的透明带配体。此外，DEFB126似乎可以掩盖所有精子表面成分，保护精子免受免疫识别。免疫保护似乎源于高度糖化的羧基结构域，该结构域由以唾液酸终止的寡糖组成。DEFB126在精子表面提供均匀的负电荷，在获能过程中，随着精子释放DEFB126，负电荷显著减少。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Objective: Our lab has had a long standing interest in identifying and characterizing sperm surface proteins that play a role in the interaction of sperm with the fluids and cells of the female reproductive tract. Our findings in non-human primates are relevant to issues in human reproduction, providing insights into causes of infertility as well as identifying possible targets for contraception. We previously reported that DEFB126 (formerly ESP13.2) coats the entire surface of macaque sperm and remains until sperm become capacitated. The release of DEFB126 from sperm during capacitation is required for sperm recognition and binding of the zona pellucida, suggesting that DEFB126 masks zona pellucida ligands on the sperm surface. Furthermore, DEFB126 appears to masks all sperm surface components and protects sperm from immune recognition. Immunoprotection appears to stem from the highly glycosylated carboxyl domain which is comprised of oligosaccharides that terminate in sialic acid. DEFB126 provides uniform negative charge over the surface of sperm that is significantly reduced as sperm release DEFB126 during capacitation.