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Association of smooth muscle cell phenotypes with extracellular matrix disorders in thoracic aortic dissection  Lixin Wang, MD, PhD, Jing Zhang, MD, PhD,

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Presentation on theme: "Association of smooth muscle cell phenotypes with extracellular matrix disorders in thoracic aortic dissection  Lixin Wang, MD, PhD, Jing Zhang, MD, PhD,"— Presentation transcript:

1 Association of smooth muscle cell phenotypes with extracellular matrix disorders in thoracic aortic dissection  Lixin Wang, MD, PhD, Jing Zhang, MD, PhD, Weiguo Fu, MD, PhD, Daqiao Guo, MD, PhD, Junhao Jiang, MD, PhD, Yuqi Wang, MD, PhD  Journal of Vascular Surgery  Volume 56, Issue 6, Pages e1 (December 2012) DOI: /j.jvs Copyright © 2012 Society for Vascular Surgery Terms and Conditions

2 Fig 1 Comparison in smooth muscle cell (SMC) morphology between the two group cultures (A-F). Control SMCs uniformly display an elongated, spindle-, or triangle-like shape (A, C, and E). A small number of oval cells aggregate locally in the dissection primary cultures and subcultures (B, D, and F). The scale bars in the lower right corner equal 10 μm (objective magnification, ×20). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

3 Fig 2 Proliferative curves and DNA synthesis indexes of the two group cultures (A and B). From day 5, cell growth rates are significantly elevated in the dissection cultures (A, n = 6). [3H] thymidine incorporation is also markedly increased in the dissection cultures compared with controls (B, n = 6). The error bars show the standard deviation. *P < .01. Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

4 Fig 3 Representative immunohistochemical results of tissue specimens for smooth muscle cell (SMC) phenotypic markers (A-H). Immunoreactivities for the phenotypic markers are predominantly localized in the cytoplasm of medial SMCs. Decreased staining for α-smooth muscle actin (α-SMA) (B), smooth muscle myosin heavy chain 2 (SM-MHC-2) (D), and smoothelin (F) are shown in the dissected media compared with the unaffected media of control tissues (A, C, and E). In contrast, the staining for osteopontin (OPN) is raised in the dissected media (H) compared with the unaffected media (G). The scale bars in the lower right corner equal 10 μm (objective magnification, ×20). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

5 Fig 4 Immunofluorescent results of cell cultures for smooth muscle cell (SMC) phenotypic markers (A-H). The staining for α-smooth muscle actin (α-SMA) (B) and smooth muscle myosin heavy chain 2 (SM-MHC-2) (D) is weak and the staining for smoothelin (F) is similar to background in the dissection cultures, while that for these contractile proteins is intense in control cultures (A, C, and E). Conversely, the dissection cultures show the positive staining for osteopontin (OPN) (H), which is lacked in control cultures (G). The nuclei are stained as blue with DAPI. The scale bars in the lower right corner equal 5 μm (objective magnification, ×20). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

6 Fig 5 In vivo and in vitro expression levels of smooth muscle cell (SMC) phenotypic markers (A-C). Compared with the unaffected media, in vivo protein levels of the contractile proteins are significantly decreased in the dissected media, whereas that of osteopontin (OPN) is elevated (A, n = 10). Compared with control cultures, in vitro protein levels of the contractile markers are markedly reduced in the dissection cultures, while that of OPN is increased (B, n = 6). In vitro mRNA levels of the phenotypic markers show the similar results (C, n = 6). The results are expressed as mean ± standard deviation (error bars). α-SMA, α-Smooth muscle actin; GAPDH, glyceraldehyde phosphate dehydrogenase; SM-MHC-2, smooth muscle myosin heavy chain 2. *P < .05, **P < .01. Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

7 Fig 6 Histopathologic alterations of collagen and elastin in the dissected media (A-H). Immunohistochemical staining demonstrates the strikingly increased collagens I and III in the dissected media (B and D) vs the unaffected media (A and C). Masson's trichrome staining shows the elevated deposition of total collagens in the dissected media (F, collagens are stained blue and smooth muscle cells [SMCs] are stained red) compared with controls (E). Gomori's staining displays the severe fragmentation and decrease of elastic fibers in the pathologic media (H, elastic fibers are stained violet or dark blue) compared with controls (G). The scale bars in the lower right corner equal 5 μm (objective magnification, ×40). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

8 Fig 7 In vivo protein levels and in vitro synthesis of collagens I and III (A and B). In vivo protein levels of collagens I and III are significantly higher in the dissected media compared with controls (A, n = 10). The band intensity of α2(I) and α1(III) labeled by [3H] proline is significantly raised in the dissection cultures compared with controls (B, n = 6). The results are expressed as mean ± standard deviation (error bars). GAPDH, Glyceraldehyde phosphate dehydrogenase. *P < .01, † P = .63. Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

9 Fig 8 Representative immunohistochemical results of matrix metalloproteinase (MMP)-1 and -2 (A-D). Immunoreactivities for MMP-2 extensively distribute in the dissected media (D), while those are scanty in the unaffected media (C). The staining for MMP-1 is weak both in the unaffected media and in the dissected media (A and B). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

10 Fig 9 In vivo and in vitro protein levels of matrix metalloproteinase (MMP)-1 and -2 (A and B). The data of Western blotting show increased protein level of MMP-2 in the dissected media, and there is no significant difference in that of MMP-1 between the dissected and unaffected media (A, n = 10). In vitro protein levels of MMP-1 and MMP-2 show the parallel patterns (B, n = 6). The results are expressed as mean ± SD (error bars). GAPDH, Glyceraldehyde phosphate dehydrogenase. †P = .32, *P < .01 (A); † P = .09, *P < .01 (B). Journal of Vascular Surgery  , e1DOI: ( /j.jvs ) Copyright © 2012 Society for Vascular Surgery Terms and Conditions

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