Mastroiacovo Federica, Biagioni Francesca, Lenzi Paola, Ryskalin Larisa, Puglisi-Allegra Stefano, Nicoletti Ferdinando, Frati Alessandro, Fornai Francesco
I.R.C.C.S. Neuromed, Via Atinense 18, 86077 Pozzilli, IS, Italy.
Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, Via Roma 55, 56126 Pisa, Italy.
Molecules. 2021 Jun 11;26(12):3578. doi: 10.3390/molecules26123578.
The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia. This protein is also considered as a potential disease modifier, which may improve the outcome of ischemic damage. In fact, the molecule HSP70 acts as a chaperonine being able to impact at several level the homeostasis of neurons. Despite being used routinely to stain area penumbra in light microscopy, the subcellular placement of this protein within area penumbra neurons, to our knowledge, remains undefined. This is key mostly when considering studies aimed at deciphering the functional role of this protein as a determinant of neuronal survival. The general subcellular placement of HSP70 was grossly reported in studies using confocal microscopy, although no direct visualization of this molecule at electron microscopy was carried out. The present study aims to provide a direct evidence of HSP70 within various subcellular compartments. In detail, by using ultrastructural morphometry to quantify HSP70 stoichiometrically detected by immuno-gold within specific organelles we could compare the compartmentalization of the molecule within area penumbra compared with control brain areas. The study indicates that two cell compartments in control conditions own a high density of HSP70, cytosolic vacuoles and mitochondria. In these organelles, HSP70 is present in amount exceeding several-fold the presence in the cytosol. Remarkably, within area penumbra a loss of such a specific polarization is documented. This leads to the depletion of HSP70 from mitochondria and mostly cell vacuoles. Such an effect is expected to lead to significant variations in the ability of HSP70 to exert its physiological roles. The present findings, beyond defining the neuronal compartmentalization of HSP70 within area penumbra may lead to a better comprehension of its beneficial/detrimental role in promoting neuronal survival.
热休克蛋白(HSP)70被认为是临床前研究中的主要标志,用于在脑缺血临床前模型中标记梗死周边区域即明确界定的半暗带。这种蛋白质也被视为一种潜在的疾病调节剂,可能改善缺血性损伤的结果。事实上,HSP70分子作为一种伴侣蛋白,能够在多个层面影响神经元的稳态。尽管在光学显微镜下常规用于标记半暗带区域,但据我们所知,该蛋白在半暗带神经元内的亚细胞定位仍不明确。这一点在考虑旨在解读该蛋白作为神经元存活决定因素的功能作用的研究时尤为关键。在使用共聚焦显微镜的研究中大致报道了HSP70的一般亚细胞定位,尽管未在电子显微镜下对该分子进行直接观察。本研究旨在提供HSP70在各种亚细胞区室中的直接证据。具体而言,通过使用超微结构形态计量学以化学计量方式量化免疫金在特定细胞器中检测到的HSP70,我们可以比较该分子在半暗带区域与对照脑区中的区室化情况。研究表明,在对照条件下,两个细胞区室即胞质空泡和线粒体拥有高密度的HSP70。在这些细胞器中,HSP70的含量超过胞质中的数倍。值得注意的是,在半暗带区域记录到这种特定极化的丧失。这导致HSP70从线粒体和主要是细胞空泡中耗竭。预计这种效应会导致HSP70发挥其生理作用的能力发生显著变化。本研究结果除了明确HSP70在半暗带区域内的神经元区室化外,可能有助于更好地理解其在促进神经元存活中的有益/有害作用。