摘要
热休克蛋白(heat shock protein,HSP)一直被认为是细胞内蛋白质,在胞内通过帮助蛋白质正确折叠、组装以及促进变性蛋白质降解而发挥生物学功能。HSP能被主动地分泌到胞外,成为细胞外HSP(extracellularHSPe,HSP),但其分泌及作用机制尚未定论。HSP偶然释放到外周循环是通过细胞坏死,生理性释放则是通过活化分泌系统。HSP有一种重要的前炎症因子可通过相同的分泌系统分泌,抗HSP自身抗体可以促进HSP的细胞因子样、辅佐样活性,抗HSP自身抗体与HSP或者HSP受体交联是放大HSP免疫信号作用的可能机制。
Heat shock protein(HSP) was originally thought to be exclusively located inside cells,where they exerts multiple function such as assisting,correct folding,assembling of proteins and promoting the degradation of unrecoverable denatured proteins.In recently years,many studies show that HSP can be secreted by cells and switch to extracellular HSP.But the mechanisms for secretion and the functions of extracellular HSP are not clear.The accidental release of HSP into the systemic circulation occurs via necrotic cells while physiological release occurs via an active secretion system.It has been shown that HSP shares the same secretion system with an important inflammatory cytokine.Anti-HSP auto-antibodies may enhance the cytokine-and adjuvant-like activities of HSP.The cross-linking of anti-HSP auto-antibodies cross-linking with HSP or HSP receptors is a possible mechanism for the enhancement of HSP signaling.
出处
《国际病理科学与临床杂志》
CAS
2011年第5期439-443,共5页
Journal of International Pathology and Clinical Medicine