Albumin is one of the most abundant proteins in the body of mammals: about 40% of its pool is located in the intravascular space and the remainder is found in the interstitial space. The content of this multifunctional protein in blood is about 60-65% of total plasma proteins. A decrease in its synthesis or changes of functional activity can destabilize oncotic blood pressure, cause a violation of transporting hormones, fatty acids, metals, and drugs. Albumin properties change under ischemic attacks associated with oxidative stress, production of reactive oxygen species, and acidosis. Under these conditions, ischemia-modified albumin (IMA) is generated that has a reduced metal-binding capacity, especially for transition metals, such as copper, nickel, and cobalt. The method of determining the cobalt-binding capability of HSA was initially proposed to evaluate IMA level and then licensed as an ACB test for routine clinical analysis for myocardial ischemia. Subsequent studies have shown the viability of the ACB test in diagnosing other diseases associated with the development of oxidative stress. This review examines recent data on IMA generation mechanisms, describes principles, advantages, and limitations of methods for evaluation of IMA levels, and provides detailed analysis of its use in diagnostic and monitoring therapeutic efficacy in different diseases.

中文翻译：

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缺血修饰白蛋白：起源和临床意义

白蛋白是哺乳动物体内最丰富的蛋白质之一：其库中约 40% 位于血管内空间，其余位于间质空间。这种多功能蛋白在血液中的含量约为血浆总蛋白的 60-65%。其合成的减少或功能活性的变化会破坏渗透压，导致运输激素、脂肪酸、金属和药物的障碍。白蛋白性质在与氧化应激、活性氧产生和酸中毒相关的缺血发作下发生变化。在这些条件下，会产生具有降低的金属结合能力的缺血修饰白蛋白 (IMA)，尤其是对铜、镍和钴等过渡金属。确定 HSA 钴结合能力的方法最初是为了评估 IMA 水平而提出的，然后被许可作为 ACB 测试用于心肌缺血的常规临床分析。随后的研究表明 ACB 测试在诊断与氧化应激发展相关的其他疾病方面的可行性。本综述检查了有关 IMA 生成机制的最新数据，描述了 IMA 水平评估方法的原则、优势和局限性，并详细分析了其在诊断和监测不同疾病治疗效果中的用途。