Ultraviolet B-Mediated Phosphorylation of the Small Heat Shock Protein HSP27 in Human Keratinocytes Jon W. Wong, Biao Shi, Behnom Farboud, Marla McClaren,

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Ultraviolet B-Mediated Phosphorylation of the Small Heat Shock Protein HSP27 in Human Keratinocytes Jon W. Wong, Biao Shi, Behnom Farboud, Marla McClaren, Takayuki Shibamoto, Carroll E. Cross, R. Rivkah Isseroff Journal of Investigative Dermatology Volume 115, Issue 3, Pages 427-434 (September 2000) DOI: 10.1046/j.1523-1747.2000.00077.x Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 UVB causes decreases in cell survival and proliferation of keratinocytes. (A) Keratinocytes were irradiated with different doses of UVB and cell viability was measured at 1 h (clear bars) and 24 h (shaded bars) after irradiation using the Trypan blue exclusion assay. Each point is the average ±SD of three separate dishes. (B) Replicate plates were seeded with 7.5 × 103 cells and irradiated 10 h later, at the indicated UVB doses. At 24 h intervals, the number of viable cells was determined using the Trypan blue exclusion assay. Each point represents the average ±SD of three separate dishes. UVB doses (mJ per cm2): ♦, 0; ▪, 4.5; ▴, 9; ×, 18. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 UVB induces changes in HSP27 isoforms in keratinocytes. Cells were irradiated with 0, 4.5, 9, 13.5, 18, and 36 mJ per cm2, or sham-irradiated, and were extracted 30 min postrecovery. After treatments, cells were lyzed and samples with equal amounts of protein were loaded on to gels. HSP27 isoforms in samples were separated by 1D-IEF and detected by immunoblotting. The approximate pI value of each identified isoform is displayed on the vertical axis. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 UVB-induced phosphorylation of HSP27 is reversible. Keratinocytes were irradiated with 9 mJ per cm2 UVB. After irradiation, cells were rinsed with PBS and then incubated with fresh medium for the indicated times. Sham-irradiated cells are shown in the left lane (time 0). HSP27 isoforms in samples were separated by 1D-IEF and detected by immunoblotting. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 UVB induces subcellular relocalization of HSP27 and aggregation of actin. Cells were grown on coverslips, UVB irradiated, allowed to recover for 1 h, and then processed for visualization of HSP27 (a, c, e, g) or filamentous actin (b, d, f, h) as described in Materials and Methods. UVB irradiation was for 0 mJ per cm2 (a, b), 9 mJ per cm2 (c, d), or 18 mJ per cm2 (e, f). In (f) and (g) cells were allowed to recover for 4 h after irradiation with 9 mJ per cm2. Scale bar: 100 μm. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 5 UVB-induced HSP27 phosphorylation is mediated by EGFR tyrosine kinase and p38 MAP kinase, but not protein kinase C. (A) Keratinocytes were preincubated with 0.1 μM GF 109203X, an inhibitor of protein kinase C, for 30 min and then either exposed to UVB irradiation (9 mJ per cm2) or treated with 100 nM PMA for 30 min. (B) Cells were preincubated with 2.5 μM herbimycin A (H), an inhibitor of tyrosine kinase p60src, or 0.4 μM PD 153035 (PD), an inhibitor of EGFR tyrosine kinase activity, for 30 min, then exposed to UVB irradiation (9 mJ per cm2). (C) Cells were preincubated with 2.5 μM SB 203580, an inhibitor of p38, for 30 min, then either exposed to UVB irradiation (9 mJ per cm2), treated with 200 μM H2O2 (HO) or 200 μM sodium arsenite (As) for 90 min, or subjected to 45°C heat shock (Δ) for 30 min. After the treatments, cells were lyzed and equal amounts of cellular proteins were loaded on to gels followed by IEF and immunoblotting for analysis of HSP27 isoforms. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 6 UVB-induced phosphorylation of HSP27 is partially inhibited by the anti-oxidant, NAC. Keratinocytes were maintained in M 154 medium containing 25 mM NAC for 6 h, then either exposed to UVB irradiation (9 mJ per cm2), treated with 200 μM H2O2 (HO) or 200 μM sodium arsenite (As) for 90 min, or subjected to 45°C heat shock (Δ) for 30 min. HSP27 isoforms in cellular extracts were determined using IEF and immunoblotting. Journal of Investigative Dermatology 2000 115, 427-434DOI: (10.1046/j.1523-1747.2000.00077.x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions