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Volumn 580, Issue 2, 2006, Pages 469-473

Bi-directional regulation of emodin and quercetin on smooth muscle myosin of gizzard

Author keywords

Bidirectional regulation; Emodin; Myosin Mg2+ ATPase activity; Myosin phosphorylation; Quercetin

Indexed keywords

1 (5 CHLORO 1 NAPHTHALENESULFONYL)HEXAHYDRO 1H 1,4 DIAZEPINE; CALMODULIN; EMODIN; MYOSIN; QUERCETIN;

EID: 30644465173     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.12.041     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 24344500775 scopus 로고    scopus 로고
    • Determination of active anthraquinones in Rheum and its tea preparations by micellar electrokinetic capillary electrophoresis
    • W.J. Zheng, X.G. Chen, and W. Jia Determination of active anthraquinones in Rheum and its tea preparations by micellar electrokinetic capillary electrophoresis Zhongguo Zhong Yao Za Zhi 29 2004 870 873
    • (2004) Zhongguo Zhong Yao Za Zhi , vol.29 , pp. 870-873
    • Zheng, W.J.1    Chen, X.G.2    Jia, W.3
  • 2
    • 4744366757 scopus 로고    scopus 로고
    • Preparative isolation and purification of hydroxyanthraquinones and cinnamic acid from the Chinese medicinal herb Rheum officinale Baill. by high-speed counter-current chromatography
    • R. Liu, A. Li, and A. Sun Preparative isolation and purification of hydroxyanthraquinones and cinnamic acid from the Chinese medicinal herb Rheum officinale Baill. by high-speed counter-current chromatography J. Chromatogr. A 1052 2004 217 221
    • (2004) J. Chromatogr. a , vol.1052 , pp. 217-221
    • Liu, R.1    Li, A.2    Sun, A.3
  • 4
    • 20944445254 scopus 로고    scopus 로고
    • Emodin inhibits tumor cell migration through suppression of the phosphatidylinositol 3-kinase-Cdc42/Rac1 pathway
    • Q. Huang, H.M. Shen, and C.N. Ong Emodin inhibits tumor cell migration through suppression of the phosphatidylinositol 3-kinase-Cdc42/Rac1 pathway Cell Mol. Life Sci. 62 2005 1167 1175
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 1167-1175
    • Huang, Q.1    Shen, H.M.2    Ong, C.N.3
  • 5
    • 0025864834 scopus 로고
    • Vasorelaxants from Chinese herbs, emodin and scoparone, possess immunosuppressive properties
    • H.C. Huang, S.H. Chu, and P.D. Chao Vasorelaxants from Chinese herbs, emodin and scoparone, possess immunosuppressive properties Eur. J. Pharmacol. 198 1991 211 213
    • (1991) Eur. J. Pharmacol. , vol.198 , pp. 211-213
    • Huang, H.C.1    Chu, S.H.2    Chao, P.D.3
  • 7
    • 3543084042 scopus 로고    scopus 로고
    • Concentration-dependent differential effects of quercetin on rat aortic smooth muscle cells
    • C.M. Shih, H. Lin, Y.C. Liang, W.S. Lee, W.F. Bi, and S.H. Juan Concentration-dependent differential effects of quercetin on rat aortic smooth muscle cells Eur. J. Pharmacol. 496 2004 41 48
    • (2004) Eur. J. Pharmacol. , vol.496 , pp. 41-48
    • Shih, C.M.1    Lin, H.2    Liang, Y.C.3    Lee, W.S.4    Bi, W.F.5    Juan, S.H.6
  • 9
    • 0037526211 scopus 로고    scopus 로고
    • Study on the chemical components of Alpinia officinarum
    • H. Luo, C. Cai, J. Zhang, and L. Mo Study on the chemical components of Alpinia officinarum Zhong Yao Cai 21 1998 349 351
    • (1998) Zhong Yao Cai , vol.21 , pp. 349-351
    • Luo, H.1    Cai, C.2    Zhang, J.3    Mo, L.4
  • 10
    • 0025719407 scopus 로고
    • Vasorelaxant effect of emodin, an anthraquinone from a Chinese herb
    • H.C. Huang, C.R. Lee, P.D. Chao, C.C. Chen, and S.H. Chu Vasorelaxant effect of emodin, an anthraquinone from a Chinese herb Eur. J. Pharmacol. 205 1991 289 294
    • (1991) Eur. J. Pharmacol. , vol.205 , pp. 289-294
    • Huang, H.C.1    Lee, C.R.2    Chao, P.D.3    Chen, C.C.4    Chu, S.H.5
  • 11
    • 0242667857 scopus 로고    scopus 로고
    • Effects of flavonoids on vascular smooth muscle of the isolated rat thoracic aorta
    • M. Ajay, A.U. Gilani, and M.R. Mustafa Effects of flavonoids on vascular smooth muscle of the isolated rat thoracic aorta Life Sci. 74 2003 603 612
    • (2003) Life Sci. , vol.74 , pp. 603-612
    • Ajay, M.1    Gilani, A.U.2    Mustafa, M.R.3
  • 12
    • 4444339390 scopus 로고    scopus 로고
    • Signal pathways involved in emodin-induced contraction of smooth muscle cells from rat colon
    • T. Ma, Q.H. Qi, J. Xu, Z.L. Dong, and W.X. Yang Signal pathways involved in emodin-induced contraction of smooth muscle cells from rat colon World J. Gastroenterol. 10 2004 1476 1479
    • (2004) World J. Gastroenterol. , vol.10 , pp. 1476-1479
    • Ma, T.1    Qi, Q.H.2    Xu, J.3    Dong, Z.L.4    Yang, W.X.5
  • 13
    • 10644262162 scopus 로고    scopus 로고
    • The stimulant cathartic, emodin, contracts the rat isolated ileum by triggering release of endogenous acetylcholine
    • S. Ali, M.S. Watson, and R.H. Osborne The stimulant cathartic, emodin, contracts the rat isolated ileum by triggering release of endogenous acetylcholine Auton Autacoid Pharmacol. 24 2004 103 105
    • (2004) Auton Autacoid Pharmacol. , vol.24 , pp. 103-105
    • Ali, S.1    Watson, M.S.2    Osborne, R.H.3
  • 14
    • 0344197642 scopus 로고    scopus 로고
    • Inhibition of guinea pig intestinal peristalsis by the flavonoids quercetin, naringenin, apigenin and genistein
    • K. Gharzouli, and P. Holzer Inhibition of guinea pig intestinal peristalsis by the flavonoids quercetin, naringenin, apigenin and genistein Pharmacology 70 2004 5 14
    • (2004) Pharmacology , vol.70 , pp. 5-14
    • Gharzouli, K.1    Holzer, P.2
  • 15
    • 0028270216 scopus 로고
    • Calcium-antagonist effect of quercetin and its relation with the spasmolytic properties of Psidium guajava. L.
    • M.A. Morales, J. Tortoriello, M. Meckes, D. Paz, and X. Lozoya Calcium-antagonist effect of quercetin and its relation with the spasmolytic properties of Psidium guajava. L. Arch. Med. Res. 25 1994 17 21
    • (1994) Arch. Med. Res. , vol.25 , pp. 17-21
    • Morales, M.A.1    Tortoriello, J.2    Meckes, M.3    Paz, D.4    Lozoya, X.5
  • 17
    • 0028124493 scopus 로고
    • Calcium and smooth muscle contraction
    • H. Jiang, and N.L. Stephens Calcium and smooth muscle contraction Mol. Cell. Biochem. 135 1994 1 9
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 1-9
    • Jiang, H.1    Stephens, N.L.2
  • 18
    • 0028053647 scopus 로고
    • Stimulation of the ATP-dependent interaction between actin and myosin by a myosin-binding fragment of smooth muscle caldesmon
    • Y. Lin, R. Ishikawa, T. Okagaki, L.H. Ye, and K. Kohama Stimulation of the ATP-dependent interaction between actin and myosin by a myosin-binding fragment of smooth muscle caldesmon Cell Motil. Cytoskeleton 29 1994 250 258
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 250-258
    • Lin, Y.1    Ishikawa, R.2    Okagaki, T.3    Ye, L.H.4    Kohama, K.5
  • 19
    • 0347982646 scopus 로고    scopus 로고
    • The bi-directional regulation of filamin on the ATPase activity of smooth muscle myosin
    • Y. Lin, H.J. Sun, S.F. Dai, Z.Y. Tang, X. He, and H. Chen The bi-directional regulation of filamin on the ATPase activity of smooth muscle myosin Chin. Med. Sci. J. 15 2000 162 164
    • (2000) Chin. Med. Sci. J. , vol.15 , pp. 162-164
    • Lin, Y.1    Sun, H.J.2    Dai, S.F.3    Tang, Z.Y.4    He, X.5    Chen, H.6
  • 20
    • 0347134399 scopus 로고    scopus 로고
    • The characterization of myosin light chain phosphorylation by the constitutively active fragment of MLCK
    • J.X. Yang, X.M. Wang, Z.Y. Tang, H. Chen, S.F. Dai, and Y. Lin The characterization of myosin light chain phosphorylation by the constitutively active fragment of MLCK Chin. Med. Sci. J. 18 2003 206 212
    • (2003) Chin. Med. Sci. J. , vol.18 , pp. 206-212
    • Yang, J.X.1    Wang, X.M.2    Tang, Z.Y.3    Chen, H.4    Dai, S.F.5    Lin, Y.6
  • 21
    • 0025719442 scopus 로고
    • Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon
    • R. Ishikawa, T. Okagaki, S. Higashi-Fujime, and K. Kohama Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon J. Biol. Chem. 266 1991 21784 21790
    • (1991) J. Biol. Chem. , vol.266 , pp. 21784-21790
    • Ishikawa, R.1    Okagaki, T.2    Higashi-Fujime, S.3    Kohama, K.4
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0026289054 scopus 로고
    • The Ayerst Award Lecture. Calcium-dependent mechanisms of regulation of smooth muscle contraction
    • M.P. Walsh The Ayerst Award Lecture. Calcium-dependent mechanisms of regulation of smooth muscle contraction Biochem. Cell Biol. 69 1990 771 800
    • (1990) Biochem. Cell Biol. , vol.69 , pp. 771-800
    • Walsh, M.P.1
  • 24
    • 0026634314 scopus 로고
    • Regulation of contraction and relaxation in arterial smooth muscle
    • C.M. Rembold Regulation of contraction and relaxation in arterial smooth muscle Hypertension 20 1992 129 137
    • (1992) Hypertension , vol.20 , pp. 129-137
    • Rembold, C.M.1
  • 26
    • 2442561626 scopus 로고    scopus 로고
    • The influence of trace amount of calponin on the smooth muscle myosins in different states
    • J.X. Yang, X.H. Feng, Y. Zhang, Z.Y. Tang, and Y. Lin The influence of trace amount of calponin on the smooth muscle myosins in different states Biochem. Biophys. Res. Commun. 318 2004 904 910
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 904-910
    • Yang, J.X.1    Feng, X.H.2    Zhang, Y.3    Tang, Z.Y.4    Lin, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.