摘要
原文 | 英語 |
---|---|
頁(從 - 到) | 1594-1602 |
頁數 | 9 |
期刊 | Biochemical Pharmacology |
卷 | 85 |
發行號 | 11 |
DOIs | |
出版狀態 | 已發佈 - 2013 |
對外發佈 | 是 |
指紋
深入研究「Thalidomide inhibits fibronectin production in TGF-β1-treated normal and keloid fibroblasts via inhibition of the p38/Smad3 pathway」主題。共同形成了獨特的指紋。引用此
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於: Biochemical Pharmacology, 卷 85, 編號 11, 2013, p. 1594-1602.
研究成果: 雜誌貢獻 › 文章 › 同行評審
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TY - JOUR
T1 - Thalidomide inhibits fibronectin production in TGF-β1-treated normal and keloid fibroblasts via inhibition of the p38/Smad3 pathway
AU - Liang, Chan-Jung
AU - Yen, Yuh-Siu
AU - Hung, Ling Yi
AU - Wang, Shu-Huei
AU - Pu, Chi-Ming
AU - Chien, Hsiung-Fei
AU - Tsai, Jaw-Shiun
AU - Lee, Chiang-Wen
AU - Yen, Feng-Lin
AU - Chen, Yuh-Lien
N1 - 被引用次數:6 Export Date: 16 March 2016 CODEN: BCPCA 通訊地址: Chen, Y.-L.; Department of Anatomy and Cell Biology, College of Medicine, National Taiwan University, No. 1, Section 1, Ren-Ai Rd, Taipei 100, Taiwan; 電子郵件: [email protected] 化學物質/CAS: 2 (2 amino 3 methoxyphenyl)chromone, 167869-21-8; 4 (4 fluorophenyl) 2 (4 methylsulfinylphenyl) 5 (4 pyridyl)imidazole, 152121-47-6; Smad2 protein, 253862-89-4; Smad3 protein, 237417-78-6, 237417-96-8, 237418-00-7; anthra[1,9 cd]pyrazol 6(2h) one, 129-56-6; fibronectin, 86088-83-7; gelatinase B, 146480-36-6; mitogen activated protein kinase 1, 137632-08-7; mitogen activated protein kinase 3, 137632-07-6; thalidomide, 50-35-1; Fibronectins; RNA, Small Interfering; SMAD3 protein, human; Smad3 Protein; Thalidomide, 4Z8R6ORS6L; Transforming Growth Factor beta1; p38 Mitogen-Activated Protein Kinases, 2.7.11.24 參考文獻: Rekha, A., Keloids - A frustrating hurdle in wound healing (2004) Int Wound J, 1, pp. 145-148; Marneros, A.G., Krieg, T., Keloids - Clinical diagnosis, pathogenesis, and treatment options (2004) J Dtsch Dermatol Ges, 2, pp. 905-913; Seifert, O., Mrowietz, U., Keloid scarring: Bench and bedside (2009) Arch Dermatol Res, 301, pp. 259-272; Wolfram, D., Tzankov, A., Pülzl, P., Piza-Katzer, H., Hypertrophic scars and keloids - A review of their pathophysiology, risk factors, and therapeutic management (2009) Dermatol Surg, 35, pp. 171-181; Al-Attar, A., Mess, S., Thomassen, J.M., Kauffman, C.L., Davison, S.P., Keloid pathogenesis and treatment (2006) Plast Reconstr Surg, 117, pp. 286-300; Kelly, A.P., Medical and surgical therapies for keloids (2004) Dermatol Ther, 17, pp. 212-218; Hsu, Y.C., Chen, M.J., Yu, Y.M., Ko, S.Y., Chang, C.C., Suppression of TGF-β1/SMAD pathway and extracellular matrix production in primary keloid fibroblasts by curcuminoids: Its potential therapeutic use in the chemoprevention of keloid (2010) Arch Dermatol Res, 302, pp. 717-724; Leask, A., Abraham, D.J., TGF-beta signaling and the fibrotic response (2004) FASEB J, 18, pp. 816-827; Kryger, Z.B., Sisco, M., Roy, N.K., Lu, L., Rosenberg, D., Mustoe, T.A., Temporal expression of the transforming growth factor-Beta pathway in the rabbit ear model of wound healing and scarring (2007) J Am Coll Surg, 205, pp. 78-88; Derynck, R., Zhang, Y.E., Smad-dependent and Smad-independent pathways in TGF-beta family signalling (2003) Nature, 425, pp. 577-584; He, S., Liu, X., Yang, Y., Huang, W., Xu, S., Yang, S., Mechanisms of transforming growth factor beta(1)/Smad signalling mediated by mitogen-activated protein kinase pathways in keloid fibroblasts (2010) Br J Dermatol, 162, pp. 538-546; Lim, I.J., Phan, T.T., Tan, E.K., Nguyen, T.T., Tran, E., Longaker, M.T., Synchronous activation of ERK and phosphatidylinositol 3-kinase pathways is required for collagen and extracellular matrix production in keloids (2003) J Biol Chem, 278, pp. 40851-40858; Phan, T.T., Lim, I.J., Chan, S.Y., Tan, E.K., Lee, S.T., Longaker, M.T., Suppression of transforming growth factor beta/smad signaling in keloid-derived fibroblasts by quercetin: Implications for the treatment of excessive scars (2004) J Trauma, 57, pp. 1032-1037; McBride, W., Health of thalidomide victims and their progeny (2004) Lancet, 363, p. 169; Tseng, S., Pak, G., Washenik, K., Pomeranz, M.K., Shupack, J.L., Rediscovering thalidomide: A review of its mechanism of action, side effects and potential uses (1996) J Am Acad Dermatol, 35, pp. 969-979; Sheskin, J., The treatment of lepra reaction in lepromatous leprosy. Fifteen years' experience with thalidomide (1980) Int J Dermatol, 19, pp. 318-322; Barnhill, R.L., Doll, N.J., Millikan, L.E., Hastings, R.C., Studies on the anti-inflammatory properties of thalidomide: Effects on polymorphonuclear leukocytes and monocytes (1984) J Am Acad Dermatol, 11, pp. 814-819; D'Amato, R.J., Loughnan, M.S., Flynn, E., Folkman, J., Thalidomide is an inhibitor of angiogenesis (1994) Proc Natl Acad Sci USA, 91, pp. 4082-4085; Lv, P., Luo, H.S., Zhou, X.P., Chireyath, P.S., Xiao, Y.J., Si, X.M., Thalidomide prevents rat liver cirrhosis via inhibition of oxidative stress (2006) Pathol Res Pract, 202, pp. 777-788; Tucci-Viegas, V.M., Hochman, B., França, J.P., Ferreira, L.M., Keloid explant culture: A model for keloid fibroblasts isolation and cultivation based on the biological differences of its specific regions (2010) Int Wound J, 7, pp. 339-348; Liang, C.J., Wang, S.H., Chen, Y.H., Chang, S.S., Hwang, T.L., Leu, Y.L., Viscolin reduces VCAM-1 expression in TNF-α-treated endothelial cells via the JNK/NF-κB and ROS pathway (2011) Free Radic Biol Med, 51, pp. 1337-1346; Massagué, J., Wotton, D., Transcriptional control by the TGF-beta/Smad signaling system (2000) EMBO J, 19, pp. 1745-1754; Zhang, G.Y., Cheng, T., Luan, Q., Liao, T., Nie, C.L., Zheng, X., Vitamin D: A novel therapeutic approach for keloid, an in vitro analysis (2011) Br J Dermatol, 164, pp. 729-737; Eriksson, T., Bjorkman, S., Hoglund, P., Clinical pharmacology of thalidomide (2001) Eur J Clin Pharmacol, 57, pp. 365-376; Meierhofer, C., Dunzendorfer, S., Wiedermann, C.J., Theoretical basis for the activity of thalidomide (2001) BioDrugs, 15, pp. 681-703; Yeh, T.S., Ho, Y.P., Huang, S.F., Yeh, J.N., Jan, Y.Y., Chen, M.F., Thalidomide salvages lethal hepatic necroinflammation and accelerates recovery from cirrhosis in rats (2004) J Hepatol, 41, pp. 606-612; Sampaio, E.P., Sarno, E.N., Galilly, R., Cohn, Z.A., Kaplan, G., Thalidomide selectively inhibits tumor necrosis factor alpha production by stimulated human monocytes (1991) J Exp Med, 173, pp. 699-703; Yasui, K., Kobayashi, N., Yamazaki, T., Agematsu, K., Thalidomide as an immunotherapeutic agent: The effects on neutrophil-mediated inflammation (2005) Curr Pharm des, 11, pp. 395-401; Lee, C.J., Kim, K.W., Lee, H.M., Nahm, F.S., Lim, Y.J., Park, J.H., The effect of thalidomide on spinal cord ischemia/reperfusion injury in a rabbit model (2007) Spinal Cord, 45, pp. 149-157; Tabata, C., Tabata, R., Kadokawa, Y., Hisamori, S., Takahashi, M., Mishima, M., Thalidomide prevents bleomycin-induced pulmonary fibrosis in mice (2007) J Immunol, 179, pp. 708-714; Laffitte, E., Revuz, J., Thalidomide: An old drug with new clinical applications (2004) Expert Opin Drug Saf, 3, pp. 47-56; Govinden, R., Bhoola, K.D., Genealogy, expression, and cellular function of transforming growth factor-beta (2003) Pharmacol Ther, 98, pp. 257-265; Kobayashi, T., Liu, X., Wen, F.Q., Kohyama, T., Shen, L., Wang, X.Q., Smad3 mediates TGF-beta1-induced collagen gel contraction by human lung fibroblasts (2006) Biochem Biophys Res Commun, 339, pp. 290-295; Flanders, K.C., Smad3 as a mediator of the fibrotic response (2004) Int J Exp Pathol, 85, pp. 47-64; Yan, J.D., Yang, S., Zhang, J., Zhu, T.H., BMP6 reverses TGF-beta1-induced changes in HK-2 cells: Implications for the treatment of renal fibrosis (2009) Acta Pharmacol Sin, 30, pp. 994-1000; Furukawa, F., Matsuzaki, K., Mori, S., Tahashi, Y., Yoshida, K., Sugano, Y., P38 MAPK mediates fibrogenic signal through Smad3 phosphorylation in rat myofibroblasts (2003) Hepatology, 38, pp. 879-889; Isono, M., Chen, S., Hong, S.W., Iglesias-De La Cruz, M.C., Ziyadeh, F.N., Smad pathway is activated in the diabetic mouse kidney and Smad3 mediates TGF-beta-induced fibronectin in mesangial cells (2002) Biochem Biophys Res Commun, 296, pp. 1356-1365; Ferguson, H.E., Kulkarni, A., Lehmann, G.M., Garcia-Bates, T.M., Thatcher, T.H., Huxlin, K.R., Electrophilic peroxisome proliferator-activated receptor-gamma ligands have potent antifibrotic effects in human lung fibroblasts (2009) Am J Respir Cell Mol Biol, 41, pp. 722-730; Luo, S., Benathan, M., Raffoul, W., Panizzon, R.G., Egloff, D.V., Abnormal balance between proliferation and apoptotic cell death in fibroblasts derived from keloid lesions (2001) Plast Reconstr Surg, 107, pp. 87-96; Lim, C.P., Phan, T.T., Lim, I.J., Cao, X., Stat3 contributes to keloid pathogenesis via promoting collagen production, cell proliferation and migration (2006) Oncogene, 25, pp. 5416-5425; Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Identification of a primary target of thalidomide teratogenicity (2010) Science, 327, pp. 1345-1350; Zhu, Y.X., Braggio, E., Shi, C.X., Bruins, L.A., Schmidt, J.E., Van Wier, S., Cereblon expression is required for the antimyeloma activity of lenalidomide and pomalidomide (2011) Blood, 118, pp. 4771-4779
PY - 2013
Y1 - 2013
N2 - Keloids are characterized by the vigorously continuous production of extracellular matrix protein and aberrant cytokine activity in the dermis. There is a growing body of evidence that thalidomide, α-N- phthalimidoglutarimide, has anti-fibrotic properties. The aims were to examine possible therapeutic effects of thalidomide on fibronectin expression in transforming growth factor-β1 (TGF-β1)-treated normal fibroblasts (NFs) and keloid-derived fibroblasts (KFs) and the underlying mechanism of action, especially the involvement of mitogen-activated protein kinase (MAPKs) and Sma- and Mad-related family (Smads) pathways. In surgically removed human tissues, TGF-β1 and fibronectin immunoreactivity was high in keloid tissue, but barely detectable in normal tissue. TGF-β1 induced significant fibronectin expression in NFs and KFs and the effect was inhibited by pretreatment with thalidomide. TGF-β1 also induced phosphorylation of MAPKs (ERK1/2, p38, and JNK) and Smad2/3 and pretreatment with PD98059 (an ERK1/2 inhibitor), SB203580 (a p38 inhibitor), or SP600125 (a JNK inhibitor) inhibited TGF-β1-induced fibronectin expression. Furthermore, pretreatment with thalidomide inhibited the TGF-β1-induced phosphorylation of p38 and Smad3, but not that of ERK1/2, JNK, and Smad2. In addition, thalidomide pretreatment inhibited the TGF-β-induced DNA binding activity of AP-1 and Smad3/4, caused fibronectin degradation by increasing the activity of matrix metalloproteinase 9, and decreased production of TGF-β1 and fibronectin and the number of fibroblasts in an in vivo keloid model. These results show that thalidomide has an antifibrotic effect on keloid fibroblasts that is caused by suppression of TGF-β1-induced p38 and Smad3 signaling. Our findings indicate that thalidomide may be a potential candidate drug for the treatment and prevention of keloids. © 2013 Elsevier Inc. All rights reserved.
AB - Keloids are characterized by the vigorously continuous production of extracellular matrix protein and aberrant cytokine activity in the dermis. There is a growing body of evidence that thalidomide, α-N- phthalimidoglutarimide, has anti-fibrotic properties. The aims were to examine possible therapeutic effects of thalidomide on fibronectin expression in transforming growth factor-β1 (TGF-β1)-treated normal fibroblasts (NFs) and keloid-derived fibroblasts (KFs) and the underlying mechanism of action, especially the involvement of mitogen-activated protein kinase (MAPKs) and Sma- and Mad-related family (Smads) pathways. In surgically removed human tissues, TGF-β1 and fibronectin immunoreactivity was high in keloid tissue, but barely detectable in normal tissue. TGF-β1 induced significant fibronectin expression in NFs and KFs and the effect was inhibited by pretreatment with thalidomide. TGF-β1 also induced phosphorylation of MAPKs (ERK1/2, p38, and JNK) and Smad2/3 and pretreatment with PD98059 (an ERK1/2 inhibitor), SB203580 (a p38 inhibitor), or SP600125 (a JNK inhibitor) inhibited TGF-β1-induced fibronectin expression. Furthermore, pretreatment with thalidomide inhibited the TGF-β1-induced phosphorylation of p38 and Smad3, but not that of ERK1/2, JNK, and Smad2. In addition, thalidomide pretreatment inhibited the TGF-β-induced DNA binding activity of AP-1 and Smad3/4, caused fibronectin degradation by increasing the activity of matrix metalloproteinase 9, and decreased production of TGF-β1 and fibronectin and the number of fibroblasts in an in vivo keloid model. These results show that thalidomide has an antifibrotic effect on keloid fibroblasts that is caused by suppression of TGF-β1-induced p38 and Smad3 signaling. Our findings indicate that thalidomide may be a potential candidate drug for the treatment and prevention of keloids. © 2013 Elsevier Inc. All rights reserved.
KW - Fibroblasts
KW - Fibronectin
KW - Keloid
KW - Mitogen-activated protein kinases (MAPKs)
KW - SMADS
KW - Thalidomide
KW - 2 (2 amino 3 methoxyphenyl)chromone
KW - 4 (4 fluorophenyl) 2 (4 methylsulfinylphenyl) 5 (4 pyridyl)imidazole
KW - anthra[1,9 cd]pyrazol 6(2h) one
KW - fibronectin
KW - gelatinase B
KW - mitogen activated protein kinase 1
KW - mitogen activated protein kinase 3
KW - mitogen activated protein kinase p38
KW - Smad2 protein
KW - Smad3 protein
KW - thalidomide
KW - transforming growth factor beta1
KW - adult
KW - article
KW - cell count
KW - clinical article
KW - controlled study
KW - DNA binding
KW - fibroblast
KW - human
KW - human cell
KW - human tissue
KW - keloid
KW - male
KW - priority journal
KW - protein expression
KW - protein phosphorylation
KW - signal transduction
KW - Adult
KW - Animals
KW - Base Sequence
KW - Electrophoretic Mobility Shift Assay
KW - Female
KW - Fibronectins
KW - Humans
KW - Immunohistochemistry
KW - Male
KW - Mice
KW - Mice, Nude
KW - Middle Aged
KW - p38 Mitogen-Activated Protein Kinases
KW - RNA, Small Interfering
KW - Smad3 Protein
KW - Transforming Growth Factor beta1
U2 - 10.1016/j.bcp.2013.02.038
DO - 10.1016/j.bcp.2013.02.038
M3 - Article
SN - 0006-2952
VL - 85
SP - 1594
EP - 1602
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 11
ER -