Volume 92, Issue 3, Pages (September 2017)

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Volume 92, Issue 3, Pages 770-772 (September 2017) Yan Y, Ma L, Zhou X, et al. Src inhibition blocks renal interstitial fibroblast activation and ameliorates renal fibrosis. Kidney Int. 2016;89:68–81    Kidney International  Volume 92, Issue 3, Pages 770-772 (September 2017) DOI: 10.1016/j.kint.2017.06.007 Copyright © 2017 International Society of Nephrology Terms and Conditions

Figure 8 (c,d) Src inhibition attenuates renal expression of p-Histone H3 (Ser 10) in mice after unilateral ureteral obstruction (UUO) injury. Photomicrographs illustrate the staining of p-Histone H3(Ser10) in the tissue section of the kidney after treatments as indicated (c).The tubular cells with positive staining of p-H3Ser10 were calculated in 10 high-power fields and expressed as means ± SEM (d). Bars with different letters (a–c) are significantly different from one another (P < 0.05). To optimize viewing of this image, please see the online version of this article at www.kidney-international.org. Kidney International 2017 92, 770-772DOI: (10.1016/j.kint.2017.06.007) Copyright © 2017 International Society of Nephrology Terms and Conditions

Figure 9 (a–d) Src inhibition blocks transforming growth factor-β1 receptor I (TGFβRI) expression and Smad-3 phosphorylation in the kidney after unilateral ureteral obstruction (UUO) injury. The kidneys were collected at day 7 after sham and UUO injury with or without PP1. Tissue lysates were subject to immunoblot analysis with specific antibodies against TGFβRI, phospho-Smad3, Smad3, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Expression levels of indicated proteins were quantified by densitometry, normalized with GAPDH, and expressed as % controls (b,d) or % UUO alone (c). Data are represented as the mean ± SEM. Bars with different letters (a–c) are significantly different from one another (P < 0.05). To optimize viewing of this image, please see the online version of this article at www.kidney-international.org. Kidney International 2017 92, 770-772DOI: (10.1016/j.kint.2017.06.007) Copyright © 2017 International Society of Nephrology Terms and Conditions

Figure S1 (a–d) Inhibition of Src with PP1 reduces angiotensin II–induced activation of renal interstitial fibroblasts. Serum-starved NRK-49F cells were incubated with 1 ng/ml angiotensin II for 24 hours in the absence or presence of 5 μM PP1. Cell lysates were subject to immunoblot analysis with antibodies to collagen 1, α-SMA, fibronectin, or glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (a). Representative immunoblots from 3 experiments are shown. Expression levels of indicated proteins were quantified by densitometry and normalized with GAPDH as indicated (b,c,d). Data are represented as the mean ± SEM. Bars with different letters (a–d) are significantly different from one another (P < 0.05). To optimize viewing of this image, please see the online version of this article at www.kidney-international.org. Kidney International 2017 92, 770-772DOI: (10.1016/j.kint.2017.06.007) Copyright © 2017 International Society of Nephrology Terms and Conditions

Figure S4 (a–d) Src inhibition attenuates the deposition of ECM and development of fibrosis in obstructed kidneys. Lysates of kidney tissue collected at day 14 after sham and unilateral ureteral obstruction (UUO) injury with or without PP1 were subject to immunoblot analysis with specific antibodies against fibronectin, collagen 1, α-smooth muscle actin, or glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (a). The levels of these proteins were quantified by densitometry, normalized with GAPDH, and expressed as % controls (b,c,d). Data are represented as the mean ± SEM. Bars with different letters (a–c) are significantly different from one another (P < 0.05). To optimize viewing of this image, please see the online version of this article at www.kidney-international.org. Kidney International 2017 92, 770-772DOI: (10.1016/j.kint.2017.06.007) Copyright © 2017 International Society of Nephrology Terms and Conditions

Figure S5 (a–c) Src inhibition potentiates the apoptosis of cultured renal interstitial fibroblasts and renal tubular cells. Rat renal interstitial fibroblasts (NRK-49F) and mouse renal proximal tubular cells were cultured for 24 hours in the absence or presence of PP1 at various concentrations (0–5 μM), and then cells were harvested for immunoblot analysis for caspase-3 and PARP cleavage using antibodies against active form of caspase-3 at 17 kDa, PARP fragment at 89 kDa, or tubulin. Representative immunoblots from 3 experiments are shown (a). Expression levels of indicated proteins were quantified by densitometry and normalized with tubulin as indicated (b,c). Data are represented as the mean ± SEM. Bars with different letters (a–c) are significantly different from one another (P < 0.05). To optimize viewing of this image, please see the online version of this article at www.kidney-international.org. Kidney International 2017 92, 770-772DOI: (10.1016/j.kint.2017.06.007) Copyright © 2017 International Society of Nephrology Terms and Conditions