Laboratorio de Inmunopatologı́a, Instituto de Biologı́a y Medicina Experimental, CONICET, Ciudad de Buenos Aires, Argentina.
Biochemistry. 2011 Sep 20;50(37):7842-57. doi: 10.1021/bi201121m. Epub 2011 Aug 26.
In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings.
在过去的十年中，人们越来越关注半乳糖凝集素的研究，这是一类进化上保守的糖结合蛋白，具有多功能特性。半乳糖凝集素在细胞内或细胞外发挥作用，作为关键的生物介质，能够监测细胞表面在细胞通讯、炎症、发育和分化等基本生物学过程中发生的变化。它们高度保守的结构、精细的碳水化合物特异性以及调节广泛生物学过程的能力吸引了来自生物化学、生物物理学、细胞生物学和生理学等多个学科的广泛科学家的关注。然而，尽管人们付出了巨大的努力来剖析这些糖结合蛋白的功能和特性，但关于这些蛋白质的结构和生化方面如何影响生物学功能的信息仍然有限。在这篇综述中，我们旨在整合这个令人困惑和古老的糖结合蛋白家族的结构、生化和功能方面，并讨论它们在生理和病理环境中的意义。
