• 中国科学论文统计源期刊
  • 中国科技核心期刊
  • 美国化学文摘(CA)来源期刊
  • 日本科学技术振兴机构数据库(JST)

临床输血与检验 ›› 2026, Vol. 28 ›› Issue (3): 436-444.DOI: 10.3969/j.issn.1671-2587.2026.03.022

• 综述 • 上一篇    下一篇

人血白蛋白翻译后修饰、功能调控与疾病相关性研究进展*

孙盼1, 闫晨2, 陈永莹1, 蒋鹏1, 秦亮2, 杨波波2, 邓晋朝2, 李长清1, 王宗奎1, 马莉1   

  1. 1中国医学科学院输血研究所,四川成都 610052;
    2广东双林生物制药有限公司,广东湛江 524081
  • 收稿日期:2025-12-29 出版日期:2026-06-20 发布日期:2026-07-07
  • 通讯作者: 马莉,主要从事血浆蛋白质制品深度开发、血液制品有效性的评价体系建设及检测关键技术与标准化研究,(E-mail)mary@ibt.pumc.edu.cn。共同通信作者:王宗奎,主要从事血液制品研发、血浆蛋白质在疾病发生发展及治疗中的作用机制,(E-mail)zongkui.wang@ibt.pumc.edu.cn。
  • 作者简介:孙盼,主要从事血液制品质量控制及应用研究,(E-mail)pan.sun@ibt.pumc.edu.cn。并列第一作者:闫晨,主要从事血液制品等研究,(E-mail)yanchen@slbiop.com。
  • 基金资助:
    *本课题受四川省重大科技专项(No.2025ZDZX0043),中国医学科学院创新工程(No.2021-I2M-1-042)项目资助

Post-translational Modifications, Functional Regulation, and Disease Associations of Human Serum Albumin

SUN Pan1, YAN Chen2, CHEN Yongying1, JIANG Peng1, QIN Liang2, YANG Bobo2, DENG Jinchao2, LI Changqing1, WANG Zongkui1, MA Li1   

  1. 1Institue of Blood Transfusion, Chinese Academy of Medical Sciences, Chengdu 610052;
    2Guangdong Shuang Lin Bio-pharmacy Co., Ltd., Zhanjiang 524081
  • Received:2025-12-29 Online:2026-06-20 Published:2026-07-07

摘要: 人血白蛋白(human serum albumin, HSA)是人血浆中含量最丰富的蛋白质,由肝脏合成,HSA会发生多种酶促或非酶促的翻译后修饰,这些修饰可引起其结构的改变。HSA主要生理功能包括维持血浆胶体渗透压、结合与转运物质、抗氧化、抗炎等。HSA的生物学功能与结构密切相关。在多种疾病状态下,HSA的结构会发生改变,从而导致其功能受损,进而影响疾病进程及治疗效果。目前临床应用的人血浆来源白蛋白(plasma-derived HSA, pdHSA)由健康人血浆分离纯化制成,广泛用于各种危重患者的治疗。近年来,随着生物技术的发展,重组人血清白蛋白(recombinant HSA, rHSA)逐渐进入临床应用,其在结构、生物学功能及安全性等方面均与pdHSA存在一定差异。本文系统综述HSA主要的翻译后修饰和功能调控,阐述其在不同疾病状态下结构与功能的改变,并比较pdHSA和rHSA的异同,帮助我们更全面、系统地认识HSA,为HSA制品的创新应用和精准医学实践奠定理论基础。

关键词: 人血白蛋白, 翻译后修饰, 功能, 疾病, 血源人血白蛋白, 重组人白蛋白

Abstract: Human serum albumin (HSA), the most abundant circulating protein in human plasma, is exclusively synthesized by hepatic parenchymal cells. HSA undergoes a broad spectrum of enzymatic and non-enzymatic post-translational modifications (PTMs), which induce substantive conformational alterations to the protein backbone. The physiological functions of HSA include maintenance of plasma colloid osmotic pressure, ligand binding and transport, endogenous antioxidant activity, anti-inflammatory effects, etc. Critically, the biological functions of HSA are intrinsically coupled to its three-dimensional conformational state. Across a wide range of pathological conditions, disease-driven perturbations to HSA structure compromise its biological functionality, which in turn modifies disease trajectory and modulates the therapeutic efficacy of clinical interventions. Currently, plasma-derived HSA (pdHSA), purified from the plasma of healthy human donors, is ubiquitously administered in the clinical management of diverse critically ill patient populations. With recent transformative advances in biopharmaceutical technology, recombinant HSA (rHSA) has been successfully translated into clinical practice, with demonstrable differences in structural properties, biological functionality, and safety profiles relative to pdHSA. This review synthesizes the core PTMs and functional regulatory mechanisms of HSA, delineates disease-associated alterations in HSA structure and function across multiple pathological states, and directly compares the structural and functional similarities and differences between pdHSA and rHSA. Collectively, this article provides a comprehensive, integrated framework for understanding HSA biology, establishing a foundational theoretical basis for the innovative clinical application of HSA-based therapeutics and the advancement of precision medicine practice.

Key words: Human serum albumin, Post-translational modifications, Functional regulation, Disease associations, Plasma-derived human serum albumin, Recombinant human serum albumin

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