Martin Carla A, Kurkowski Danielle L, Valentino Alisa M, Santiago-Schwarz Frances
Department of Biology, State University of New York, Farmingdale, 11735, USA.
J Immunol. 2009 Jul 1;183(1):388-99. doi: 10.4049/jimmunol.0802688.
Physiologic triggers and functional consequences of endogenous heat shock protein (HSP) responses in dendritic cells (DC) are poorly defined. In this study, we show that even in the absence of heat stress and infection, a specific cohort of DC/proinflammatory cytokines (IL-4-IL-13/IL-6/GM-CSF) institutes an enhanced inducible (i)HSP70 intracellular and extracellular response in human monocyte-derived DC, especially during the monocyte to DC transition. Interestingly, whereas heat stress alone initiated an intracellular iHSP70 response in monocyte DC precursors, it did not promote cell surface or secreted iHSP70 responses, both of which were induced by cytokines independently of heat. The cytokine-induced iHSP70 response, which did not occur in lymphocytes, or monocytes-macrophages generated with M-CSF, was instituted within 48 h of cytokine exposure, and peaked upon commitment to DC growth at 72 h. Although a return to baseline levels was noted after this period, a distinct rise in iHSP70 occurred again during terminal DC maturation. Chemical inhibition of the iHSP70 response with either triptolide or KNK-437 was coupled with inhibition of DC differentiation and yielded cells displaying features of monocytes-macrophages. Exogenously supplied riHSP70 amplified events associated with cytokine-advanced DC differentiation/maturation, most notably the up-regulation of antiapoptotic proteins (Bcl-x(L)). Engaging the HSP receptor CD40 with CD40L produced identical results as extracellular riHSP70, and, moreover, an enhanced iHSP70 response. Thus, distinct iHSP70 and HSP receptor-mediated responses are triggered by cytokines irrespective of heat stress and infection in monocyte-derived DC and may function to positively regulate monocyte-derived DC, especially during critical periods of their growth.
树突状细胞(DC)内源性热休克蛋白(HSP)反应的生理触发因素和功能后果目前尚不清楚。在本研究中,我们发现即使在没有热应激和感染的情况下,特定的DC/促炎细胞因子(IL-4-IL-13/IL-6/GM-CSF)群体也会在人单核细胞衍生的DC中引发增强的诱导型(i)HSP70细胞内和细胞外反应,尤其是在单核细胞向DC转变期间。有趣的是,虽然单独的热应激在单核细胞DC前体中引发了细胞内iHSP70反应,但它并未促进细胞表面或分泌的iHSP70反应,而这两种反应均由细胞因子独立于热诱导产生。细胞因子诱导的iHSP70反应在淋巴细胞或用M-CSF生成的单核细胞-巨噬细胞中未发生,在细胞因子暴露后48小时内开始,并在72小时承诺DC生长时达到峰值。尽管在此期间后观察到iHSP70恢复到基线水平,但在DC终末成熟期间iHSP70再次明显升高。用雷公藤内酯醇或KNK-437对iHSP70反应进行化学抑制与DC分化抑制相关,并产生显示单核细胞-巨噬细胞特征的细胞。外源性提供的riHSP70放大了与细胞因子促进的DC分化/成熟相关的事件,最显著的是抗凋亡蛋白(Bcl-x(L))的上调。用CD40L激活HSP受体CD40产生与细胞外riHSP70相同的结果,此外,还增强了iHSP70反应。因此,在单核细胞衍生的DC中,无论热应激和感染如何,细胞因子都会触发不同的iHSP70和HSP受体介导的反应,并且可能在正向调节单核细胞衍生的DC中发挥作用,尤其是在其生长的关键时期。