Terentiev A A, Moldogazieva N T
Russian State Medical University, Department of Biochemistry, Moscow 117997, Russia.
Biochemistry (Mosc). 2007 Sep;72(9):920-35. doi: 10.1134/s0006297907090027.
This review summarizes and analyzes data on structural and functional relationships between cell adhesion proteins and alpha-fetoprotein (AFP), which play an important role in embryo- and carcinogenesis and act in synergism with growth factors. These two groups of proteins are mosaic, multimodular, and polyfunctional, and each of their modules can function independently through binding with its specific membrane receptor. Most cell adhesion proteins contain modules similar to epidermal growth factor (EGF) and also their repeats, which determine the involvement of these proteins in regulation of cell proliferation, differentiation, and apoptosis. These EGF-like modules are found to include short motifs similar to the fragment LDSYQCT of human AFP. Both direct and inverted AFP-like motifs are linked through a consensus octapeptide motif CXXGY/FXGX. Such AFP-like motifs of cell adhesion proteins and the tripeptide RGD found in AFP may be structural prerequisites for common functions of these groups of nonhomologous and unrelated proteins.
本综述总结并分析了细胞粘附蛋白与甲胎蛋白（AFP）之间结构和功能关系的数据，它们在胚胎发育和致癌过程中发挥重要作用，并与生长因子协同作用。这两类蛋白质是镶嵌的、多模块的和多功能的，它们的每个模块都可以通过与其特定的膜受体结合而独立发挥功能。大多数细胞粘附蛋白含有类似于表皮生长因子（EGF）的模块及其重复序列，这些决定了这些蛋白质参与细胞增殖、分化和凋亡的调控。发现这些类EGF模块包含类似于人AFP片段LDSYQCT的短基序。直接和反向的类AFP基序都通过共有八肽基序CXXGY/FXGX相连。细胞粘附蛋白的此类类AFP基序以及AFP中发现的三肽RGD可能是这些非同源且不相关蛋白质组共同功能的结构先决条件。
