Heat Shock Modulates UVB-Induced Cell Death in Human Epidermal Keratinocytes: Evidence for a Hyperthermia-Inducible Protective Response

Maytin, Edward V.; Wimberly, Joanne; Kane, Kay S.

doi:10.1111/1523-1747.ep12396274

Cited by 61 publications

(40 citation statements)

References 41 publications

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“…Nevertheless, previous studies have shown that exposure to heat stress, for 1 hour at 38-40°C, prior to UVB irradiation, protects keratinocytes against UVB-induced DNA damage (Kane and Maytin, 1995;Maytin et al, 1994;Trautinger et al, 1995). However, concomitant exposure to UV and heat in mice lead to increased skin cancer incidence (Bain et al, 1943b;Freeman and Knox, 1964).…”

Section: General Discussion Chapter 5: Heat Stress and Skin Carcinogementioning

confidence: 99%

“…It is important to note that previous studies adhered to a single heat-then-UVB exposure experimental protocol, with a four-hour interval between heat and UVB exposures (Jantschitsch et al, 1998;Kane and Maytin, 1995;Maytin et al, 1994). Pre-treatment to heat stress prior to UVB irradiation activates the heat shock response and HSP70 (Jantschitsch and Trautinger, 2003;Roti Roti, 2007), and thus, these cells were provided with a pre-established protective mechanism against UVBinduced DNA damage.…”

Section: Uvb Plus Heat and Cpd Damagementioning

confidence: 99%

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Heat stress: A risk factor for skin carcinogenesis

2013

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Section: General Discussion Chapter 5: Heat Stress and Skin Carcinogementioning

confidence: 99%

Section: Uvb Plus Heat and Cpd Damagementioning

confidence: 99%

Heat stress: A risk factor for skin carcinogenesis

2013

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“…UVB irradiation of keratinocytes induces the expression of HSP70 not only in vitro but also in vivo (11,(13)(14)(15)(16)(17). Furthermore, artificial expression of HSP70 in keratinocytes confers protection against UVB and ROS in vitro (8,16,18,19). The protective role of HSP70 against UVB-induced epidermal damage was also suggested by in vivo studies: the whole body hyperthermia of mice prevented UVBinduced sunburn cell formation, and HSP70-null mice showed a sensitive phenotype to UVB-induced epidermal damage (20 -22).…”

mentioning

confidence: 98%

Prevention of UVB Radiation-induced Epidermal Damage by Expression of Heat Shock Protein 70

Matsuda

Hoshino

Yamashita

et al. 2010

Journal of Biological Chemistry

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Irradiation with UV light, especially UVB, causes epidermal damage via the induction of apoptosis, inflammatory responses, and DNA damage. Various stressors, including UV light, induce heat shock proteins (HSPs) and the induction, particularly that of HSP70, provides cellular resistance to such stressors. The anti-inflammatory activity of HSP70, such as its inhibition of nuclear factor kappa B (NF-B), was recently revealed. These in vitro results suggest that HSP70 protects against UVB-induced epidermal damage. Here we tested this idea by using transgenic mice expressing HSP70 and cultured keratinocytes. Irradiation of wild-type mice with UVB caused epidermal damage such as induction of apoptosis, which was suppressed in transgenic mice expressing HSP70. UVB-induced apoptosis in cultured keratinocytes was suppressed by overexpression of HSP70. Irradiation of wild-type mice with UVB decreased the cutaneous level of IB-␣ (an inhibitor of NF-B) and increased the infiltration of leukocytes and levels of pro-inflammatory cytokines and chemokines in the epidermis. These inflammatory responses were suppressed in transgenic mice expressing HSP70. In vitro, the overexpression of HSP70 suppressed the expression of pro-inflammatory cytokines and chemokines and increased the level of IB-␣ in keratinocytes irradiated with UVB. UVB induced an increase in cutaneous levels of cyclobutane pyrimidine dimers and 8-hydroxy-2-deoxyguanosine, both of which were suppressed in transgenic mice expressing HSP70. This study provides genetic evidence that HSP70 protects the epidermis from UVB-induced radiation damage. The findings here also suggest that the protective action of HSP70 is mediated by anti-apoptotic, anti-inflammatory, and anti-DNA damage effects.The skin can be structurally classified into several layers, including the most apical layer, the epidermis, containing large numbers of keratinocytes, and a second layer, immediately under this, the dermis, which has a high fibroblast content (1). Skin provides a major interface between the environment and the body and is constantly exposed to an array of physical and chemical stressors. Therefore, in addition to intrinsic causes, harmful exogenous causes are involved in the process of skin damage. Among exogenous harmful agents, UV irradiation is the most relevant to skin damage (photo-damage). UV light can be separated, based on wavelength, into three categories: UVA (320 -400 nm), UVB (290 -320 nm), and UVC (100 -290 nm). Of these, the celldamaging effect of UVA is relatively weak, whereas most UVC is absorbed by the ozone layer (2). Thus, UVB seems to play the central role in photo-damage, such as clinical sunburn, hyperpigmentation, erythema, plaque-like thickening, loss of skin tone, deep furrowing, and fine wrinkle formation, all of which constitute both clinical and cosmetic problems. Furthermore, UVB irradiation induces the development of skin cancer (photo-carcinogenesis) (3). UVB-induced photodamage and photo-carcinogenesis both involve epidermal damage (such as induction...

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“…Our data demonstrate that this physiologic level of UVB irradiation was enough to cause severe damage and death in cultured human corneal epithelial cells. UVB can induce cell death either through apoptosis or necrosis, dependent on the dose of UVB irradiation received (Maytin et al, 1994). In a rabbit corneal epithelial cell line, 50 mJ/cm 2 of UVB caused caspase activation and apoptosis, which was not observed when higher levels of UVB (450 mJ/cm 2 ) were employed (Shimmura et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Arsenite pre‐conditioning reduces UVB‐induced apoptosis in corneal epithelial cells through the anti‐apoptotic activity of 27 kDa heat shock protein (HSP27)

Shi

Isseroff

2005

Journal Cellular Physiology

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Exposure to ultraviolet (UV) light poses a health risk for eye disease, and solar ultraviolet in the B range (UVB, 280-320 nm) is known to be related to various corneal disorders. In this study, we investigated whether pre-conditioning of cells with arsenite (AsO2(-1)) can reduce UVB-induced apoptosis in human corneal epithelial cells, and whether the anti-apoptotic activity of 27 kDa heat shock protein (HSP27), a small heat shock protein, plays a role in this protection. UVB at levels comparable to physiologic solar exposure induces apoptosis of corneal epithelial cells in culture, demonstrated by activation of caspase 9 and caspase 3, and DNA fragmentation. When cells were pre-conditioned with arsenite prior to UVB exposure, the UVB-induced cell death was reduced, and UVB-induced activation of caspases and DNA fragmentation was inhibited. When cells were pre-treated with SB 203580, which inhibits HSP27 phosphorylation through inhibition of p38 MAP kinase activation, the arsenite-induced reduction of UVB-induced apoptosis was partially reversed. Arsenite pre-conditioning inhibited UVB-induced apoptosis in a two-phase pattern, which was temporally correlated with arsenite-induced HSP27 expression and phosphorylation. Neutralization of intracellular HSP27 with its antibody reduced arsenite's inhibition of UVB-induced caspase3 activation. Our results suggest that forms of stress that upregulate HSP27 and its phosphorylation may be useful as novel approaches to prevent adverse ocular effects arising from UV exposure in humans.

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Heat Shock Modulates UVB-Induced Cell Death in Human Epidermal Keratinocytes: Evidence for a Hyperthermia-Inducible Protective Response

Cited by 61 publications

References 41 publications

Heat stress: A risk factor for skin carcinogenesis

Heat stress: A risk factor for skin carcinogenesis

Prevention of UVB Radiation-induced Epidermal Damage by Expression of Heat Shock Protein 70

Arsenite pre‐conditioning reduces UVB‐induced apoptosis in corneal epithelial cells through the anti‐apoptotic activity of 27 kDa heat shock protein (HSP27)

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