Landry J, Huot J
Centre de recherche en cancérologie de l'Université Laval, Centre Hospitalier Universitaire de Québec, Canada.
Biochem Soc Symp. 1999;64:79-89.
Activation of the mitogen-activated protein kinase (MAP kinase) SAPK2 (stress-activated protein kinase 2) leads to the phosphorylation of several transcription factors and cytoplasmic proteins, and thereby presumably orchestrates important specific cellular responses to numerous cytokines, stressing agents and agonists of tyrosine kinase or serpentine receptors. The heat-shock protein of 27 kDa (Hsp27), a downstream target of the SAPK2-activated MAP-kinase-activated protein kinase-2/3, has a documented function as an actin polymerization modulator. Accordingly, recent evidence implicates the SAPK2 pathway in the modulation of microfilament dynamics in response to stress and agonist stimulation. In vascular endothelial cells, where the basal level of expression of Hsp27 is high, SAPK2 mediates oxidative stress- and vascular endothelial growth factor (VEGF)-induced actin reorganization and VEGF-induced cell migration, suggesting a key role for this MAP kinase pathway in inflammation and angiogenic processes.
丝裂原活化蛋白激酶（MAP激酶）SAPK2（应激激活蛋白激酶2）的激活会导致多种转录因子和细胞质蛋白的磷酸化，因此可能协调细胞对多种细胞因子、应激剂以及酪氨酸激酶或蛇形受体激动剂的重要特异性反应。27 kDa的热休克蛋白（Hsp27）是SAPK2激活的MAP激酶激活的蛋白激酶-2/3的下游靶点，其作为肌动蛋白聚合调节剂的功能已得到证实。因此，最近的证据表明，SAPK2途径参与了应激和激动剂刺激下微丝动力学的调节。在Hsp27基础表达水平较高的血管内皮细胞中，SAPK2介导氧化应激和血管内皮生长因子（VEGF）诱导的肌动蛋白重组以及VEGF诱导的细胞迁移，表明该MAP激酶途径在炎症和血管生成过程中起关键作用。
