A proteomic study of the aortic media in human thoracic aortic dissection: Implication for oxidative stress Mingfang Liao, MD, PhD, Zhaoyang Liu, PhD,

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A proteomic study of the aortic media in human thoracic aortic dissection: Implication for oxidative stress Mingfang Liao, MD, PhD, Zhaoyang Liu, PhD, Junmin Bao, MD, Zhiqing Zhao, MD, Jianwen Hu, PhD, Xiang Feng, MD, Rui Feng, MD, Qingsheng Lu, MD, Zhijun Mei, MD, Yanling Liu, MS, Qingyu Wu, MD, PhD, Zaiping Jing, MD The Journal of Thoracic and Cardiovascular Surgery Volume 136, Issue 1, Pages 65-72.e3 (July 2008) DOI: 10.1016/j.jtcvs.2007.11.017 Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions

Figure 1 Histopathology of TAD. An image of an ascending aorta from a patient with TAD showing an enlarged and dissected aorta with large amounts of blood clots in the false lumen (A). Hematoxylin and eosin staining of TAD aortic tissue showing the dissected layer in the middle media (B). Fragmentation and rigidity of elastic fiber (blue) in TAD by Victoria blue staining (C). Verification of aortic media by immunostaining of alpha smooth muscle actin (brown) in the media (D). The Journal of Thoracic and Cardiovascular Surgery 2008 136, 65-72.e3DOI: (10.1016/j.jtcvs.2007.11.017) Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions

Figure 2 2-DE images of protein profiles of the aortic media. Representative 2-DE images of aortic media protein from a normal control (A) and patient with TAD (B). Protein spots identified by MS were marked with numbers. Enlarged pictures of silver-stained gels highlight the significant differences between samples from patients and controls (C). The Journal of Thoracic and Cardiovascular Surgery 2008 136, 65-72.e3DOI: (10.1016/j.jtcvs.2007.11.017) Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions

Figure 3 Peptide mass fingerprinting and tandem mass spectrophotometry spectrum of spot 15. Peptide mass fingerprinting spectrum of spot 15 by matrix-assisted laser desorption/ionization time-of-flight-MS (A). Three peptides (red) were selected for tandem mass spectrophotometry identification. Tandem mass spectrophotometry spectrum of spot 15 (B) was from 1418 m/z (A, gray circle). Spot 15 was identified to be EC-SOD. The Journal of Thoracic and Cardiovascular Surgery 2008 136, 65-72.e3DOI: (10.1016/j.jtcvs.2007.11.017) Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions

Figure 4 Western blotting verification for EC-SOD protein expression. EC-SOD and the internal control protein (beta-actin) were detected in aortic samples from the NA and TAD groups (A). Quantitative analysis of EC-SOD expression in TAD (n = 8) and NA (n = 6) groups (B). ∗P < .05. EC-SOD, Extracellular superoxide dismutase; NA, normal thoracic aorta; TAD, thoracic aortic dissection. The Journal of Thoracic and Cardiovascular Surgery 2008 136, 65-72.e3DOI: (10.1016/j.jtcvs.2007.11.017) Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions

Figure 5 MDA levels, catalase activity, and SOD activity in aortic samples. Increased MDA in the TAD group compared with that in the NA group (A). Catalase activity was lower in the TAD group than in the NA group, but the difference was not statistically significant (B). Total SOD activity and activities of cyanide-sensitive SOD (Cu/Zn-SOD plus EC-SOD) were also decreased in the TAD group compared with the NA group (C). ∗P < .05. MDA, Malondialdehyde; NA, normal thoracic aorta; TAD, thoracic aortic dissection; EC-SOD, extracellular superoxide dismutase; Mn-SOD, manganese-superoxide dismutase; SOD, superoxide dismutase. The Journal of Thoracic and Cardiovascular Surgery 2008 136, 65-72.e3DOI: (10.1016/j.jtcvs.2007.11.017) Copyright © 2008 The American Association for Thoracic Surgery Terms and Conditions