95kd精子蛋白与ZP3结合,并作为响应区域结合的氨酸激酶基质
1Department of Obstetrics and Gynecology, Duke University Medical Center, Durham, North Carolina 27710.
Cell
|June 30, 1989
概括
鼠标精子利用95kd蛋白质来结合透明区 (ZP) 并触发体反应. 这种ZP结合蛋白还充当氨酸激酶基质,启动精子-卵相互作用信号.
科学领域:
- 生殖生物学 生殖生物学
- 分子细胞生物学 分子细胞生物学
- 生物化学 生物化学
背景情况:
- 透明区 (ZP) 对于精子结合和启动体反应至关重要.
- 参与ZP3诱导的宏体反应的精确信号通路尚不清楚.
- 类似Gi的蛋白质以前已经涉及到精子信号传导.
研究的目的:
- 调查小鼠精子中的抗色胺抗体反应性,作为信号转导的潜在指标.
- 为了识别参与ZP结合和体反应的精子蛋白.
- 阐明铁酸酸化在精子和卵子相互作用中的作用.
主要方法:
- 使用免疫光学检查小鼠精子中的抗色胺抗体活性.
- 通过探测带有放射标记的ZP和ZP3.3的精子蛋白斑点,确定了ZP结合蛋白.
- 与精子电容状态和ZP相互作用相关的光蛋白检测.
主要成果:
- 抗氨酸抗体在精子体区域识别了52,75和95kd蛋白.
- 一种95 kd蛋白被确定为ZP3结合蛋白和氨酸激酶基质.
- ZP3 结合到 95 kd 蛋白增强的氨酸激酶活性,与宏体反应诱导相关.
结论:
- 95kd的精子血蛋白作为ZP3.3的受体起作用.
- 这95kd受体的ZP3诱导的聚合刺激了氨酸激酶活性.
- 这种信号级联被认为是触发体外细胞形成的机制.
相关概念视频
Protein Kinases and Phosphatases
15.2K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.2K
Ligand Binding and Linkage
5.6K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.6K
The Equilibrium Binding Constant and Binding Strength
15.2K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.2K
The Equilibrium Binding Constant and Binding Strength
10.1K
No description available
10.1K
Receptor Tyrosine Kinases
19.0K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
19.0K
Ligand Binding Sites
15.2K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.2K


