Krenacs Laszlo, Krenacs Tibor, Stelkovics Eva, Raffeld Mark
Laboratory of Tumor Pathology, Bay Zoltan Foundation for Applied Research, Szeged, Hungary.
Methods Mol Biol. 2010;588:103-19. doi: 10.1007/978-1-59745-324-0_14.
The development of heat-induced antigen (epitope) retrieval (HIER) technologies has led to dramatic improvements in our ability to detect antigens in formalin fixed, archival tissues. Paradoxically, wet heat treatment at temperatures greater than 95 degrees C in appropriate buffer solutions can reconstitute the antigenicity of many proteins that have been rendered nonreactive during the fixation and paraffin embedding process, which heretofore could only be identified in fresh or frozen tissues. The reason for this effect is unclear, but it has been suggested that the vigorous heat treatment partially reverses or disrupts the aldehyde cross-links occurring in proteins during formalin fixation and restores the original conformation of antigenic epitopes. The great success of antigen/epitope retrieval technologies further emphasizes the importance of preanalytical steps in immunohistochemistry. Over the past several years, since this technology was first reported, there have been numerous modifications to the original formulation. It is the purpose of this chapter to discuss the critical issues required for optimal HIER and to provide guidelines for the use of popular HIER buffers and heating devices used for routine immunohistochemical detection.
热诱导抗原(表位)修复(HIER)技术的发展极大地提高了我们在福尔马林固定的存档组织中检测抗原的能力。矛盾的是,在适当的缓冲溶液中于高于95摄氏度的温度下进行湿热处理,可以恢复许多在固定和石蜡包埋过程中失去反应性的蛋白质的抗原性,而这些蛋白质此前只能在新鲜或冷冻组织中被识别。这种效应的原因尚不清楚,但有人认为,剧烈的热处理部分逆转或破坏了福尔马林固定过程中蛋白质中发生的醛交联,并恢复了抗原表位的原始构象。抗原/表位修复技术的巨大成功进一步强调了免疫组织化学分析前步骤的重要性。在过去几年中,自该技术首次报道以来,对原始配方进行了许多修改。本章的目的是讨论最佳HIER所需的关键问题,并为常规免疫组织化学检测中使用的常用HIER缓冲液和加热设备的使用提供指导。