Galasso Alessia, Zollo Massimo
Centro di Ingegneria Genetica e Biotecnologia Avanzate (CEINGE), Via Comunale Margherita 482, 80145 Naples, Italy.
Mol Cell Biochem. 2009 Sep;329(1-2):149-59. doi: 10.1007/s11010-009-0115-4. Epub 2009 Apr 24.
Nm23-H1 (also known as NDPKA) and h-Prune form a protein complex that is part of a little-understood protein network. Modifications of this complex correlate with cancer status. Here, we focus on the role of the Nm23-H1-h-Prune complex in cellular physiology, through an analysis of the balance between the 'bound' and 'non-bound' states of Nm23-H1 and h-Prune, whereby we speculate on the 'read-out' during cell homeostasis under non-balanced conditions. We have analysed the biochemical activities of both Nm23-H1 and h-Prune alone and in combination, focussing on the anti-metastatic activity of Nm23-H1. We have then investigated the cellular mechanisms responsible for the formation of the Nm23-H1-h-Prune complex. To evaluate the importance of the equilibrium between the formation of the Nm23-H1-h-Prune complex and the 'free' levels of Nm23-H1 and h-Prune, we propose a model based on a pro-cancer condition where this equilibrium is negatively affected.
Nm23-H1(也称为NDPKA)和h-Prune形成一种蛋白质复合物,该复合物是一个了解较少的蛋白质网络的一部分。这种复合物的修饰与癌症状态相关。在这里,我们通过分析Nm23-H1和h-Prune的“结合”和“未结合”状态之间的平衡,来关注Nm23-H1-h-Prune复合物在细胞生理学中的作用,据此我们推测在非平衡条件下细胞稳态期间的“读出”情况。我们单独及联合分析了Nm23-H1和h-Prune的生化活性,重点关注Nm23-H1的抗转移活性。然后我们研究了负责形成Nm23-H1-h-Prune复合物的细胞机制。为了评估Nm23-H1-h-Prune复合物的形成与Nm23-H1和h-Prune的“游离”水平之间平衡的重要性,我们基于一种癌症发生条件提出了一个模型,在这种条件下这种平衡受到负面影响。