Department of Neurology, UT Medical School, University of Texas Health Science Center, Houston, TX, USA.
Department of Radiology, 167626The Methodist Hospital Research Institute, Houston, TX, USA.
Mol Imaging. 2020 Jan-Dec;19:1536012120942685. doi: 10.1177/1536012120942685.
Heat shock protein expression can be induced by heat shock making it possible to artificially modulate their levels noninvasively in vivo in a spatially and temporally controlled manner. Here, we report the use of the major heat shock protein 70 (HSP70) as an inducible target by using the small molecule deoxyspergualin (DSG) conjugated to the near-infrared fluorophore (Cy5.5). We demonstrate that heat induction in the form of localized hyperthermia of normal tissue in living mice results in sufficient HSP70 overexpression for detection with DSG-Cy5.5 conjugate. This effect is dependent on total energy delivered and reaches maximum fluorescence signal in 6 to 8 hours post heat induction and declines over a period of up to 24 hours. These results suggest that DSG-Cy5.5 agent accumulates in tissue with elevated HSP70 by heat.
热休克蛋白的表达可以被热休克诱导,从而可以在体内以非侵入性、空间和时间控制的方式人为地调节其水平。在这里,我们报告了使用小分子去氧精胍(DSG)与近红外荧光染料(Cy5.5)缀合,将主要热休克蛋白 70(HSP70)作为一种可诱导的靶标。我们证明,以活小鼠正常组织局部高热的形式进行热诱导,会导致 HSP70 的过度表达,足以用 DSG-Cy5.5 缀合物检测到。这种效应依赖于传递的总能量,在热诱导后 6 至 8 小时达到最大荧光信号,并在长达 24 小时的时间内下降。这些结果表明,DSG-Cy5.5 试剂通过热在 HSP70 升高的组织中积累。