Cebo Christelle, Vergoten Gérard, Zanetta Jean-Pierre
CNRS Unité Mixte de Recherche 8576, Glycobiologie Structurale et Fonctionnelle, Lab. de Chimie Biologique, Université des Sciences et Technologie de Lille Bâtiment C9, 59655 Cedex, Villeneuve d'Ascq, France.
Biochim Biophys Acta. 2002 Sep 19;1572(2-3):422-34. doi: 10.1016/s0304-4165(02)00323-9.
The discovery that some cytokines have carbohydrate-binding (lectin) properties opens new concepts in the understanding of their mechanism of action. The carbohydrate-recognition domain (CRD), which is localized at the opposite of the receptor-binding domain, makes these molecules bi-functional. The expression of the biological activity of the cytokine relies on its carbohydrate-binding activity, which allows the association of the cytokine receptor with molecular complexes comprising the specific kinase/phosphatase involved in receptor phosphorylation/dephosphorylation and in specific signal transduction. As a correlate, a cytokine can act only on cells possessing both the receptor and the ligand. Two cytokines using the same receptor can have different target cells and functions because of their different lectin activities. Based on a few examples, the CRD can be predicted based on the 3-D structures of the molecules.
一些细胞因子具有碳水化合物结合(凝集素)特性这一发现,为理解其作用机制开启了新的概念。位于受体结合域相对位置的碳水化合物识别域(CRD),使这些分子具有双功能性。细胞因子生物活性的表达依赖于其碳水化合物结合活性,这使得细胞因子受体能够与包含参与受体磷酸化/去磷酸化及特定信号转导的特定激酶/磷酸酶的分子复合物相结合。相应地,一种细胞因子只能作用于同时拥有受体和配体的细胞。由于具有不同的凝集素活性,两种使用相同受体的细胞因子可能具有不同的靶细胞和功能。基于一些实例,可以根据分子的三维结构预测CRD。