Department of Clinical Pharmacology, Medical University of Bialystok, Poland.
Eur J Med Res. 2009 Dec 7;14 Suppl 4(Suppl 4):104-7. doi: 10.1186/2047-783x-14-s4-104.
Heat shock proteins assist cellular protein folding and are required for the normal activity of steroid receptors. In this study we assessed nuclear HSP90 and HSP70 proteins and mRNA levels in cells isolated from induced sputum of chronic obstructive pulmonary disease patients treated for 4 weeks with formoterol (F) or formoterol+budesonide (F/ICS).
Nuclear heat shock protein levels were assessed by Western blot and specific mRNAs were quantified in cell lysates using qRT-PCR.
Both HSP90 and HSP70 protein levels were higher in the F/ICS-treated patients in comparison with the F-treated group (by 31%, P<0.05 and 28%, P<0.05, respectively), while specific mRNAs were lowered. HSP86/HSP89 and D6S182/HSP90-BETA were repressed by about 40% (P<0.05) while HSP70-1/HSP70-1A, HSP70-1B/HSP70-2, and HSP70-HSC54/HSC70 were repressed by 47% (P<0.01), 57% (P<0.01) and 65% (P<0.01), respectively.
It is possible that increased nuclear heat shock proteins may play a role in the attenuation of the response to glucocorticoids in COPD patients.
热休克蛋白有助于细胞蛋白折叠，是甾体激素受体正常活动所必需的。本研究评估了慢性阻塞性肺疾病患者诱导痰中分离的细胞内核 HSP90 和 HSP70 蛋白及 mRNA 水平，这些患者接受福莫特罗（F）或福莫特罗+布地奈德（F/ICS）治疗 4 周。
采用 Western blot 法评估核热休克蛋白水平，并使用 qRT-PCR 定量细胞裂解物中的特异性 mRNA。
与 F 治疗组相比，F/ICS 治疗组患者的 HSP90 和 HSP70 蛋白水平均升高（分别升高 31%，P<0.05 和 28%，P<0.05），而特异性 mRNA 水平降低。HSP86/HSP89 和 D6S182/HSP90-BETA 分别下调约 40%（P<0.05），而 HSP70-1/HSP70-1A、HSP70-1B/HSP70-2 和 HSP70-HSC54/HSC70 分别下调 47%（P<0.01）、57%（P<0.01）和 65%（P<0.01）。
核内热休克蛋白增加可能在 COPD 患者对糖皮质激素反应减弱中起作用。
