Department of Dermatology, Medical University of Vienna, Vienna, Austria.
Int J Cosmet Sci. 2006 Aug;28(4):233-41. doi: 10.1111/j.1467-2494.2006.00327.x.
Heat shock proteins (hsp) are expressed in all cells and organisms. Their expression is induced by heat shock (temperatures above 42 degrees C) and other forms of pathophysiological stress. Elevated levels of hsp protect cells from further stress exposure. Hsp are expressed intracellularly. They are highly conserved throughout evolution indicating hsp being necessary for survival under potentially harmful environmental conditions. Hsp are divided into families according to their molecular weight. The majority of hsp function as molecular chaperones. Chaperone function is characterized by binding to other proteins and mediating their folding, transport and interaction with other molecules. In human epidermis hsp are abundantly expressed and have been linked with functions in cell differentiation and photobiology. Recent research has mainly focused on the 27 and 72 kD hsp that are constitutively expressed in human keratinocytes. ultraviolet radiation (UV)-induced cell death and sunburn cell formation can be inhibited by previous heat shock exposure and UV itself can induce hsp expression. The expression of the 27 kD hsp (hsp27) in epidermal keratinocytes in situ and in culture correlates with differentiation. Expression of hsp27 increases simultaneously with keratinocyte differentiation. For that reason, hsp27 is described as a marker of epidermal differentiation. Changes in the expression and inducibility of hsp have been linked with ageing. In the skin, recent data indicate that hsp72 expression remains remarkably stable with intrinsic ageing. In contrast, levels of hsp27 have been found to be elevated in sun-protected aged skin indicating a link between hsp27 expression and age-dependent epidermal alterations. Regulation of hsp can be modified by pharmacological intervention and the development of safe topical and systemic treatments for the prevention of skin damage and disorders of keratinocyte differentiation can be expected for the future.
热休克蛋白（hsp）存在于所有细胞和生物体中。它们的表达受热休克（高于 42 摄氏度的温度）和其他形式的病理生理应激诱导。hsp 的高水平表达可保护细胞免受进一步的应激暴露。hsp 在细胞内表达。它们在整个进化过程中高度保守，表明 hsp 在潜在有害的环境条件下对生存是必要的。hsp 根据其分子量分为不同的家族。大多数 hsp 作为分子伴侣发挥作用。伴侣功能的特点是与其他蛋白质结合，并介导它们的折叠、运输和与其他分子的相互作用。在人类表皮中，hsp 大量表达，并与细胞分化和光生物学功能有关。最近的研究主要集中在 27 和 72 kD hsp 上，它们在人类角质形成细胞中持续表达。先前的热休克暴露和 UV 本身可以抑制紫外线辐射（UV）诱导的细胞死亡和晒伤细胞的形成，诱导 hsp 表达。表皮角质形成细胞原位和培养物中 27 kD hsp（hsp27）的表达与分化相关。hsp27 的表达随着角质形成细胞的分化而增加。因此，hsp27 被描述为表皮分化的标志物。hsp 的表达和诱导变化与衰老有关。在皮肤中，最近的数据表明，hsp72 的表达随着内在衰老而保持显著稳定。相比之下，在防晒的老年皮肤中发现 hsp27 水平升高，表明 hsp27 表达与年龄相关的表皮改变之间存在联系。hsp 的调节可以通过药理学干预进行修饰，预计未来可以开发出安全的局部和全身治疗方法，以预防皮肤损伤和角质形成细胞分化障碍。
