Kaltner H, Stierstorfer B
Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, München, Deutschland.
Acta Anat (Basel). 1998;161(1-4):162-79. doi: 10.1159/000046456.
Protein-carbohydrate interaction is exploited in cell adhesion mechanisms besides the recognition of peptide motifs. The sugar code thus significantly contributes to the intriguing specificity of cellular selection of binding partners. Focusing on two classes of lectins (selectins and galectins), it is evident that their functionality for mediation of adhesive contacts is becoming increasingly appreciated, as is the integration of this type of interaction with other recognition modes to yield the noted specificity. The initial contact formation between leukocytes and activated endothelium makes use of selectins to guide lymphocyte trafficking. In addition to the three selectins which bind a distinct array of ligands, galectin-1 and galectin-3 and possibly other members of this family are involved in cell-cell or cell-matrix interactions. This review summarizes structural and functional aspects of these two classes of endogenous lectins relevant for cell adhesion.
除了对肽基序的识别外，蛋白质 - 碳水化合物相互作用还被用于细胞黏附机制。因此，糖代码显著促成了细胞对结合伴侣选择的有趣特异性。聚焦于两类凝集素（选择素和半乳糖凝集素），很明显它们介导黏附接触的功能越来越受到重视，这类相互作用与其他识别模式的整合以产生所述特异性也是如此。白细胞与活化内皮之间的初始接触形成利用选择素来引导淋巴细胞运输。除了三种能结合不同配体阵列的选择素外，半乳糖凝集素 -1 和半乳糖凝集素 -3 以及该家族的其他成员可能也参与细胞 - 细胞或细胞 - 基质相互作用。本综述总结了这两类与细胞黏附相关的内源性凝集素的结构和功能方面。
