对补充因子H的自身抗体和治疗性抗体
Saskia Nugteren1, Haiyu Wang1, Cees van Kooten2
1Department of Immunology, Leiden University Medical Center, Leiden, the Netherlands.
Immunology letters
|March 21, 2025
概括
H因子调节免疫系统的作用.
科学领域:
- 免疫学 免疫学 免疫学
- 补充系统生物学 补充系统生物学
背景情况:
- 补体系统对免疫防御至关重要,但需要严格监管,以防止宿主组织受损.
- H因子是替代补充路径的关键调节者,控制细胞表面和流体相中的激活.
- 由于遗传因素,竞争性蛋白质或自身抗体导致H因子功能受损,可能会破坏补充体的调节.
研究的目的:
- 审查各种疾病中抗H因子自身抗体的存在和影响.
- 探索这些自身抗体如何影响H因子功能和补体激活.
- 讨论理解抗H因子自身抗体的潜在治疗影响.
主要方法:
- 对不同疾病中报告抗H因子自身抗体的研究的文献综述.
- 对自抗体对H因子调节功能的报告影响的分析.
- 综合当前对自身抗体结合部位和功能后果的理解.
主要成果:
- 抗H因子自身抗体在各种疾病中发现,包括自身免疫性疾病和癌症,超出了以前已知的联系,如非典型的血溶性尿素性综合征.
- 这些自身抗体可以抑制或增强H因子的活性,这取决于针对的特定表位体.
- 反H因子自身抗体在某些疾病中的确切的致病作用尚未完全阐明.
结论:
- 抗H因子自身抗体与以前认为的更广泛的疾病谱系有关.
- 了解这些自身抗体的表位特异性影响对于评估它们的致病性至关重要.
- 针对病理性抗H因子自身抗体的向干预可以提供治疗效益,而抗H因子自身的抗体也可以作为治疗剂进行探索.
更多相关视频
07:25In Vitro Methods for Comparing Target Binding and CDC Induction Between Therapeutic Antibodies: Applications in Biosimilarity Analysis
Published on: May 4, 2017
17.7K
08:49Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals
Published on: February 14, 2019
6.8K
相关概念视频
Antibody Actions
1.0K
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
1.0K
Humoral Immune Responses
71.1K
Overview
71.1K
Hybridoma Technology
13.9K
Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation,...
Hybridoma Selection
Commonly used fusion techniques — electroporation,...
13.9K
Antibody Structure
58.7K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
58.7K
Cross-reactivity
30.9K
Overview
30.9K
Antibody Structure and Classes
723
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
723
