Skip to main content
Erschienen in: Lasers in Medical Science 8/2020

30.05.2020 | Original Article

42 °C heat stress pretreatment protects human melanocytes against 308-nm laser-induced DNA damage in vitro

verfasst von: Wenzhi Hu, Na Mi, Yanfang Xu, Guang Zhao, Weijie Gu

Erschienen in: Lasers in Medical Science | Ausgabe 8/2020

Einloggen, um Zugang zu erhalten

Abstract

Vitiligo is a common depigment of skin disorder due to loss of functional melanocytes. Recently, the phototherapy with a 308-nm xenon-chloride excimer laser (UVB laser) is wildly used in vitiligo treatment. However, excessive UVB will induce photo-damage and photo-carcinogenesis in melanocytes. Previous studies revealed a protective effect of heat on UVB-induced melanocyte damage. In this study, we combined heat stress pretreatment with UVB to evaluate whether heat stress pretreatment has an ameliorative effect on UVB-induced damage. Human primary melanocytes (HMCs) were cultured and irradiated with a 308-nm laser with/without heat treatment. MTT assay, apoptosis analysis, and comet assay were conducted to monitor the damage of HMCs. Western blot and immunofluorescence staining were performed to assess the expression and subcellular localization of HSP70. HMCs heated at 42 °C for 1 h exhibit no cytotoxicity. Furthermore, preheat treatment attenuated the UVB laser-induced injury, reduced the DNA damage, and attenuated the cell apoptosis. The level and the localization of HSP70 determined the protective effects against UVB-induced DNA damage. Combining preheat treatment with a 308-nm xenon-chloride excimer laser would be a potential therapeutic method not only promotes the repigment of vitiligo but also reduces the UVB-induced photo-damage.
Anhänge
Nur mit Berechtigung zugänglich
Literatur
1.
Zurück zum Zitat Bishnoi A, Parsad D (2018) Clinical and molecular aspects of vitiligo treatments [J]. Int J Mol Sci 19(5): 1-15 Bishnoi A, Parsad D (2018) Clinical and molecular aspects of vitiligo treatments [J]. Int J Mol Sci 19(5): 1-15
2.
Zurück zum Zitat Beggs S, Short J, Rengifo-Pardo M, Ehrlich A (2015) Applications of the excimer laser: a review [J]. Dermatol Surg 41(11):1201–1211CrossRef Beggs S, Short J, Rengifo-Pardo M, Ehrlich A (2015) Applications of the excimer laser: a review [J]. Dermatol Surg 41(11):1201–1211CrossRef
3.
Zurück zum Zitat Mohania D, Chandel S, Kumar P, Verma V, Digvijay K, Tripathi D, Choudhury K, Mitten SK, Shah D (2017) Ultraviolet radiations: skin defense-damage mechanism [J]. Adv Exp Med Biol 996:71–87CrossRef Mohania D, Chandel S, Kumar P, Verma V, Digvijay K, Tripathi D, Choudhury K, Mitten SK, Shah D (2017) Ultraviolet radiations: skin defense-damage mechanism [J]. Adv Exp Med Biol 996:71–87CrossRef
4.
Zurück zum Zitat Nakazawa K, Sahuc F, Damour O, Collombel C, Nakazawa H (1998) Regulatory effects of heat on normal human melanocyte growth and melanogenesis: comparative study with UVB [J]. J Invest Dermatol 110(6):972–977CrossRef Nakazawa K, Sahuc F, Damour O, Collombel C, Nakazawa H (1998) Regulatory effects of heat on normal human melanocyte growth and melanogenesis: comparative study with UVB [J]. J Invest Dermatol 110(6):972–977CrossRef
5.
Zurück zum Zitat Gu WJ, Ma HJ, Zhao G, Yuan XY, Zhang P, Liu W, Ma LJ, Lei XB (2014) Additive effect of heat on the UVB-induced tyrosinase activation and melanogenesis via ERK/p38/MITF pathway in human epidermal melanocytes [J]. Arch Dermatol Res 306(6):583–590CrossRef Gu WJ, Ma HJ, Zhao G, Yuan XY, Zhang P, Liu W, Ma LJ, Lei XB (2014) Additive effect of heat on the UVB-induced tyrosinase activation and melanogenesis via ERK/p38/MITF pathway in human epidermal melanocytes [J]. Arch Dermatol Res 306(6):583–590CrossRef
6.
Zurück zum Zitat Gu Y, Chen J, Wang T, Zhou C, Liu Z, Ma L (2016) Hsp70 inducer, 17-allylamino-demethoxygeldanamycin, provides neuroprotection via anti-inflammatory effects in a rat model of traumatic brain injury [J]. Exp Ther Med 12(6):3767–3772CrossRef Gu Y, Chen J, Wang T, Zhou C, Liu Z, Ma L (2016) Hsp70 inducer, 17-allylamino-demethoxygeldanamycin, provides neuroprotection via anti-inflammatory effects in a rat model of traumatic brain injury [J]. Exp Ther Med 12(6):3767–3772CrossRef
7.
Zurück zum Zitat Kiemer AK, Gerbes AL, Bilzer M, Vollmar AM (2002) The atrial natriuretic peptide and cGMP: novel activators of the heat shock response in rat livers [J]. Hepatology (Baltimore, Md) 35(1):88–94CrossRef Kiemer AK, Gerbes AL, Bilzer M, Vollmar AM (2002) The atrial natriuretic peptide and cGMP: novel activators of the heat shock response in rat livers [J]. Hepatology (Baltimore, Md) 35(1):88–94CrossRef
8.
Zurück zum Zitat Kuboki S, Schuster R, Blanchard J, Pritts TA, Wong HR, Lentsch AB (2007) Role of heat shock protein 70 in hepatic ischemia-reperfusion injury in mice [J]. Am J Physiol Gastrointest Liver Physiol 292(4):G1141–G1149CrossRef Kuboki S, Schuster R, Blanchard J, Pritts TA, Wong HR, Lentsch AB (2007) Role of heat shock protein 70 in hepatic ischemia-reperfusion injury in mice [J]. Am J Physiol Gastrointest Liver Physiol 292(4):G1141–G1149CrossRef
9.
Zurück zum Zitat Tashiro S, Miyake H, Rokutan K (2018) Role of geranylgeranylacetone as non-toxic HSP70 inducer in liver surgery: clinical application [J]. J Hepatobiliary Pancreat Sci 25(5):269–274CrossRef Tashiro S, Miyake H, Rokutan K (2018) Role of geranylgeranylacetone as non-toxic HSP70 inducer in liver surgery: clinical application [J]. J Hepatobiliary Pancreat Sci 25(5):269–274CrossRef
10.
Zurück zum Zitat Tanimoto T, Parseghian MH, Nakahara T, Kawai H, Narula N, Kim D, Nishimura R, Weisbart RH, Chan G, Richieri RA, Haider N, Chaudhry F, Reynolds GT, Billimek J, Blankenberg FG, Sengupta PP, Petrov AD, Akasaka T, Strauss HW, Narula J (2017) Cardioprotective effects of HSP72 administration on ischemia-reperfusion injury [J]. J Am Coll Cardiol 70(12):1479–1492CrossRef Tanimoto T, Parseghian MH, Nakahara T, Kawai H, Narula N, Kim D, Nishimura R, Weisbart RH, Chan G, Richieri RA, Haider N, Chaudhry F, Reynolds GT, Billimek J, Blankenberg FG, Sengupta PP, Petrov AD, Akasaka T, Strauss HW, Narula J (2017) Cardioprotective effects of HSP72 administration on ischemia-reperfusion injury [J]. J Am Coll Cardiol 70(12):1479–1492CrossRef
11.
Zurück zum Zitat Ateş GB, Ak A, Garipcan B, Gülsoy M (2018) Indocyanine green-mediated photobiomodulation on human osteoblast cells [J]. Lasers Med Sci 33(7):1591–1599CrossRef Ateş GB, Ak A, Garipcan B, Gülsoy M (2018) Indocyanine green-mediated photobiomodulation on human osteoblast cells [J]. Lasers Med Sci 33(7):1591–1599CrossRef
12.
Zurück zum Zitat Konca K, Lankoff A, Banasik A, Lisowska H, Kuszewski T, Gozdz S, Koza Z, Wojcik A (2003) A cross-platform public domain PC image-analysis program for the comet assay [J]. Mutat Res 534(1–2):15–20CrossRef Konca K, Lankoff A, Banasik A, Lisowska H, Kuszewski T, Gozdz S, Koza Z, Wojcik A (2003) A cross-platform public domain PC image-analysis program for the comet assay [J]. Mutat Res 534(1–2):15–20CrossRef
13.
Zurück zum Zitat Ramsby ML, Makowski GS, Khairallah EA (1994) Differential detergent fractionation of isolated hepatocytes: biochemical, immunochemical and two-dimensional gel electrophoresis characterization of cytoskeletal and noncytoskeletal compartments [J]. Electrophoresis 15(2):265–277CrossRef Ramsby ML, Makowski GS, Khairallah EA (1994) Differential detergent fractionation of isolated hepatocytes: biochemical, immunochemical and two-dimensional gel electrophoresis characterization of cytoskeletal and noncytoskeletal compartments [J]. Electrophoresis 15(2):265–277CrossRef
14.
Zurück zum Zitat Palleros DR, Welch WJ, Fink AL (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding [J]. Proc Natl Acad Sci U S A 88(13):5719–5723CrossRef Palleros DR, Welch WJ, Fink AL (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding [J]. Proc Natl Acad Sci U S A 88(13):5719–5723CrossRef
15.
Zurück zum Zitat Kampinga HH, Craig EA (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity [J]. Nat Rev Mol Cell Biol 11(8):579–592CrossRef Kampinga HH, Craig EA (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity [J]. Nat Rev Mol Cell Biol 11(8):579–592CrossRef
16.
Zurück zum Zitat Clerico EM, Tilitsky JM, Meng W, Gierasch LM (2015) How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions [J]. J Mol Biol 427(7):1575–1588CrossRef Clerico EM, Tilitsky JM, Meng W, Gierasch LM (2015) How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions [J]. J Mol Biol 427(7):1575–1588CrossRef
17.
Zurück zum Zitat Rudiger S, Buchberger A, Bukau B (1997) Interaction of Hsp70 chaperones with substrates [J]. Nat Struct Biol 4(5):342–349CrossRef Rudiger S, Buchberger A, Bukau B (1997) Interaction of Hsp70 chaperones with substrates [J]. Nat Struct Biol 4(5):342–349CrossRef
18.
Zurück zum Zitat Tavaria M, Gabriele T, Kola I, Anderson RL (1996) A hitchhiker’s guide to the human Hsp70 family [J]. Cell Stress Chaperones 1(1):23–28CrossRef Tavaria M, Gabriele T, Kola I, Anderson RL (1996) A hitchhiker’s guide to the human Hsp70 family [J]. Cell Stress Chaperones 1(1):23–28CrossRef
19.
Zurück zum Zitat Chung J, Nguyen AK, Henstridge DC, Holmes AG, Chan MH, Mesa JL, Lancaster GI, Southgate RJ, Bruce CR, Duffy SJ, Horvath I, Mestril R, Watt MJ, Hooper PL, Kingwell BA, Vigh L, Hevener A, Febbraio MA (2008) HSP72 protects against obesity-induced insulin resistance [J]. Proc Natl Acad Sci U S A 105(5):1739–1744CrossRef Chung J, Nguyen AK, Henstridge DC, Holmes AG, Chan MH, Mesa JL, Lancaster GI, Southgate RJ, Bruce CR, Duffy SJ, Horvath I, Mestril R, Watt MJ, Hooper PL, Kingwell BA, Vigh L, Hevener A, Febbraio MA (2008) HSP72 protects against obesity-induced insulin resistance [J]. Proc Natl Acad Sci U S A 105(5):1739–1744CrossRef
20.
Zurück zum Zitat Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP (2015) Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases [J]. Annu Rev Pharmacol Toxicol 55:353–371CrossRef Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP (2015) Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases [J]. Annu Rev Pharmacol Toxicol 55:353–371CrossRef
21.
Zurück zum Zitat Levada K, Guldiken N, Zhang X, Vella G, Mo FR, James LP, Haybaeck J, Kessler SM, Kiemer AK, Ott T, Hartmann D, Huser N, Ziol M, Trautwein C, Strnad P (2018) Hsp72 protects against liver injury via attenuation of hepatocellular death, oxidative stress, and JNK signaling [J]. J Hepatol 68(5):996–1005CrossRef Levada K, Guldiken N, Zhang X, Vella G, Mo FR, James LP, Haybaeck J, Kessler SM, Kiemer AK, Ott T, Hartmann D, Huser N, Ziol M, Trautwein C, Strnad P (2018) Hsp72 protects against liver injury via attenuation of hepatocellular death, oxidative stress, and JNK signaling [J]. J Hepatol 68(5):996–1005CrossRef
22.
Zurück zum Zitat Bivik C, Rosdahl I, Ollinger K (2007) Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes [J]. Carcinogenesis 28(3):537–544CrossRef Bivik C, Rosdahl I, Ollinger K (2007) Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes [J]. Carcinogenesis 28(3):537–544CrossRef
23.
Zurück zum Zitat Stankiewicz AR, Lachapelle G, Foo CP, Radicioni SM, Mosser DD (2005) Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation [J]. J Biol Chem 280(46):38729–38739CrossRef Stankiewicz AR, Lachapelle G, Foo CP, Radicioni SM, Mosser DD (2005) Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation [J]. J Biol Chem 280(46):38729–38739CrossRef
24.
Zurück zum Zitat Li H, Liu L, Xing D, Chen WR (2010) Inhibition of the JNK/Bim pathway by Hsp70 prevents Bax activation in UV-induced apoptosis [J]. FEBS Lett 584(22):4672–4678CrossRef Li H, Liu L, Xing D, Chen WR (2010) Inhibition of the JNK/Bim pathway by Hsp70 prevents Bax activation in UV-induced apoptosis [J]. FEBS Lett 584(22):4672–4678CrossRef
25.
Zurück zum Zitat Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C (2007) Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy [J]. J Leukoc Biol 81(1):15–27CrossRef Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C (2007) Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy [J]. J Leukoc Biol 81(1):15–27CrossRef
26.
Zurück zum Zitat Ruchalski K, Mao H, Li Z, Wang Z, Gillers S, Wang Y, Mosser DD, Gabai V, Schwartz JH, Borkan SC (2006) Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation [J]. J Biol Chem 281(12):7873–7880CrossRef Ruchalski K, Mao H, Li Z, Wang Z, Gillers S, Wang Y, Mosser DD, Gabai V, Schwartz JH, Borkan SC (2006) Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation [J]. J Biol Chem 281(12):7873–7880CrossRef
27.
Zurück zum Zitat Beere HM, Wolf BB, Cain K, Mosser DD, Mahboubi A, Kuwana T, Tailor P, Morimoto RI, Cohen GM, Green DR (2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome [J]. Nat Cell Biol 2(8):469–475CrossRef Beere HM, Wolf BB, Cain K, Mosser DD, Mahboubi A, Kuwana T, Tailor P, Morimoto RI, Cohen GM, Green DR (2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome [J]. Nat Cell Biol 2(8):469–475CrossRef
28.
Zurück zum Zitat Senf SM, Dodd SL, McClung JM, Judge AR (2008) Hsp70 overexpression inhibits NF-kappaB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy [J]. FASEB J 22(11):3836–3845CrossRef Senf SM, Dodd SL, McClung JM, Judge AR (2008) Hsp70 overexpression inhibits NF-kappaB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy [J]. FASEB J 22(11):3836–3845CrossRef
29.
Zurück zum Zitat Chen H, Wu Y, Zhang Y, Jin L, Luo L, Xue B, Lu C, Zhang X, Yin Z (2006) Hsp70 inhibits lipopolysaccharide-induced NF-kappaB activation by interacting with TRAF6 and inhibiting its ubiquitination [J]. FEBS Lett 580(13):3145–3152CrossRef Chen H, Wu Y, Zhang Y, Jin L, Luo L, Xue B, Lu C, Zhang X, Yin Z (2006) Hsp70 inhibits lipopolysaccharide-induced NF-kappaB activation by interacting with TRAF6 and inhibiting its ubiquitination [J]. FEBS Lett 580(13):3145–3152CrossRef
30.
Zurück zum Zitat Matsuda M, Hoshino T, Yamashita Y, Tanaka K, Maji D, Sato K, Adachi H, Sobue G, Ihn H, Funasaka Y, Mizushima T (2010) Prevention of UVB radiation-induced epidermal damage by expression of heat shock protein 70 [J]. J Biol Chem 285(8):5848–5858CrossRef Matsuda M, Hoshino T, Yamashita Y, Tanaka K, Maji D, Sato K, Adachi H, Sobue G, Ihn H, Funasaka Y, Mizushima T (2010) Prevention of UVB radiation-induced epidermal damage by expression of heat shock protein 70 [J]. J Biol Chem 285(8):5848–5858CrossRef
31.
Zurück zum Zitat Kayama M, Nakazawa T, Thanos A, Morizane Y, Murakami Y, Theodoropoulou S, Abe T, Vavvas D, Miller JW (2011) Heat shock protein 70 (HSP70) is critical for the photoreceptor stress response after retinal detachment via modulating anti-apoptotic Akt kinase [J]. Am J Pathol 178(3):1080–1091CrossRef Kayama M, Nakazawa T, Thanos A, Morizane Y, Murakami Y, Theodoropoulou S, Abe T, Vavvas D, Miller JW (2011) Heat shock protein 70 (HSP70) is critical for the photoreceptor stress response after retinal detachment via modulating anti-apoptotic Akt kinase [J]. Am J Pathol 178(3):1080–1091CrossRef
32.
Zurück zum Zitat Lennikov A, Kitaichi N, Kase S, Noda K, Horie Y, Nakai A, Ohno S, Ishida S (2013) Induction of heat shock protein 70 ameliorates ultraviolet-induced photokeratitis in mice [J]. Int J Mol Sci 14(1):2175–2189CrossRef Lennikov A, Kitaichi N, Kase S, Noda K, Horie Y, Nakai A, Ohno S, Ishida S (2013) Induction of heat shock protein 70 ameliorates ultraviolet-induced photokeratitis in mice [J]. Int J Mol Sci 14(1):2175–2189CrossRef
33.
Zurück zum Zitat Svobodova A, Walterova D, Vostalova J (2006) Ultraviolet light induced alteration to the skin [J]. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 150(1):25–38CrossRef Svobodova A, Walterova D, Vostalova J (2006) Ultraviolet light induced alteration to the skin [J]. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 150(1):25–38CrossRef
34.
Zurück zum Zitat Glady A, Tanaka M, Moniaga CS, Yasui M, Hara-Chikuma M (2018) Involvement of NADPH oxidase 1 in UVB-induced cell signaling and cytotoxicity in human keratinocytes [J]. Biochem Biophys Rep 14:7–15PubMedPubMedCentral Glady A, Tanaka M, Moniaga CS, Yasui M, Hara-Chikuma M (2018) Involvement of NADPH oxidase 1 in UVB-induced cell signaling and cytotoxicity in human keratinocytes [J]. Biochem Biophys Rep 14:7–15PubMedPubMedCentral
35.
Zurück zum Zitat Yurinskaya MM, Kochetkova OY, Shabarchina LI, Antonova OY, Suslikov AV, Evgen’ev MB, Vinokurov MG (2017) Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFalpha in human phagocytes [J]. Cell Stress Chaperones 22(1):163–171CrossRef Yurinskaya MM, Kochetkova OY, Shabarchina LI, Antonova OY, Suslikov AV, Evgen’ev MB, Vinokurov MG (2017) Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFalpha in human phagocytes [J]. Cell Stress Chaperones 22(1):163–171CrossRef
36.
Zurück zum Zitat Gilbert CS, van den Bosch M, Green CM, Vialard JE, Grenon M, Erdjument-Bromage H, Tempst P, Lowndes NF (2003) The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function [J]. EMBO Rep 4(10):953–958CrossRef Gilbert CS, van den Bosch M, Green CM, Vialard JE, Grenon M, Erdjument-Bromage H, Tempst P, Lowndes NF (2003) The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function [J]. EMBO Rep 4(10):953–958CrossRef
37.
Zurück zum Zitat Kotoglou P, Kalaitzakis A, Vezyraki P, Tzavaras T, Michalis LK, Dantzer F, Jung JU, Angelidis C (2009) Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks [J]. Cell Stress Chaperones 14(4):391–406CrossRef Kotoglou P, Kalaitzakis A, Vezyraki P, Tzavaras T, Michalis LK, Dantzer F, Jung JU, Angelidis C (2009) Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks [J]. Cell Stress Chaperones 14(4):391–406CrossRef
38.
Zurück zum Zitat Liu-Smith F, Jia J, Zheng Y (2017) UV-induced molecular signaling differences in melanoma and non-melanoma skin cancer [J]. Advances in experimental medicine and biology 996:27–40CrossRef Liu-Smith F, Jia J, Zheng Y (2017) UV-induced molecular signaling differences in melanoma and non-melanoma skin cancer [J]. Advances in experimental medicine and biology 996:27–40CrossRef
Metadaten
Titel
42 °C heat stress pretreatment protects human melanocytes against 308-nm laser-induced DNA damage in vitro
verfasst von
Wenzhi Hu
Na Mi
Yanfang Xu
Guang Zhao
Weijie Gu
Publikationsdatum
30.05.2020
Verlag
Springer London
Erschienen in
Lasers in Medical Science / Ausgabe 8/2020
Print ISSN: 0268-8921
Elektronische ISSN: 1435-604X
DOI
https://doi.org/10.1007/s10103-020-03012-3

Weitere Artikel der Ausgabe 8/2020

Lasers in Medical Science 8/2020 Zur Ausgabe