References
- Z.S. Galis, M. Muszynski, G.K. Sukhova, E. Simon-Morrissey, E.N. Unemori, W.W. Lark, E. Amento and P. Libby, Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling, Circ. Res. 75:181-189, 1994 https://doi.org/10.1161/01.RES.75.1.181
- R.P. Fabunmi, A.H. Baker, E.J. Murray, R.F.G. Booth and A.C. Newby, Divergent regulation by growth factors and cytokines of 95 kDa and 72 kDa gelatinases and tissue inhibitors or metalloproteinases-1, -2, and -3 in rabbit aortic smooth muscle cells Biochem. J. 315:335-342, 1996 https://doi.org/10.1042/bj3150335
- A. Cho, J. Graves and M.A. Reidy, Mitogen-activated protein kinases mediate matrix metalloproteinase-9 expression in vascular smooth muscle cells, Arterioscler. Thromb. Vasc. Biol. 20:2527-2532, 2000 https://doi.org/10.1161/01.ATV.20.12.2527
- S.K. Moon, B.Y. Cha and C.H. Kim. ERK1/2 mediates TNF-alpha-induced matrix metalloproteinase-9 expression in human vascular smooth muscle cells via the regulation of NF-kappaB and AP-1: Involvement of the ras dependent pathway. J. Cell. Physiol. 198:417-427, 2004 https://doi.org/10.1002/jcp.10435
- Y. Okada, Y. Gonoji, K. Naka, K. Tomita, I. Nakanishi, K. Iwata, K. Yamashita, and T. Hayakawa, Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase from HT 1080 human fibrosarcoma cells, Purification and activation of the precursor and enzymic properties, J. Biol. Chem. 267:21712-21719, 1992
- R.M. Senior, G.L. Griffin, C.J. Fliszar, S.D. Shapiro, G.I. Goldberg, H.G. Welgus, Human 92- and 72-kilodalton type IV collagenases are elastases, J Biol Chem. 266:7870-7875. 1991
- Z.S. Galis, M. Muszynski, G.K. Sukhova, E. Simon-Morrissey, E.N. Unemori, W.W. Lark, E. Amento, and P. Libby, Cytokine-stimulated human vascular smooth muscle cells synthesize a complement of enzymes required for extracellular matrix digestion, Circ. Res. 75:181-189, 1994 https://doi.org/10.1161/01.RES.75.1.181
- R.P. Fabunmi, A.H. Baker, E.J. Murray, R.F.G. Booth, and A.C. Newby, Divergent regulation by growth factors and cytokines of 95 kDa and 72 kDa gelatinases and tissue inhibitors or metalloproteinases-1, -2, and -3 in rabbit aortic smooth muscle cells, Biochem. J. 315:335-342, 1996 https://doi.org/10.1042/bj3150335
- H. Sato, M. Seiki, Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells, Oncogene. 8:395-405, 1993
- H, Sato, M. Kita, M. Seiki, v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines, J. Biol. Chem. 268:23460-23468, 1993
- A.R. Farina, A. Tacconelli, A. Vacca, M. Maroder, A. Gulino, A.R. Mackay, Transcriptional up-regulation of matrix metalloproteinase-9 expression during spontaneous epithelial to neuroblast phenotype conversion by SK-N-SH neuroblastoma cells, involved in enhanced invasivity, depends upon GT-box and nuclear factor kappaB elements, Cell Growth Differ. 10:353-367, 1999
- Gambhir, S.S., Goel, R.K., Das Gupta, G. Anti-inflammatory & anti-ulcerogenic activity of amentoflavone. Ind J Med Res. 85:689-693, 1987
- Kim, H.K., Son, K.H., Chang, H.W., Kang, S.S., Kim, H.P. Amentoflavone, a plant biflavone: a new potential anti-inflammatory agent. Arch Pharm Res. 21:406-410, 1998 https://doi.org/10.1007/BF02974634
- Tordera, M., Ferrandiz, M.L., Alcaraz, M.J. Influence of anti-inflammatory flavonoids on degranulation and arachidonic acid release in rat neutrophils. Z Naturforsch [C]. 49:235-240, 1994
- Huguet, A.I., Manez, S., Alcaraz, M.J. Superoxide scavenging properties of flavonoids in a non-enzymic system. Z Naturforsch [C]. 45:19-24, 1990
- Lee, H.S., Oh, W.K., Kim, B.Y., Ahn, S.C., Kang, D.O., Shin, D.I. et al. Inhibition of phospholipase C gamma 1 activity by amentoflavone isolated from Selaginella tamariscina. Planta Med. 62:293-296, 1996 https://doi.org/10.1055/s-2006-957887
- Saponara R, Bosisio E. Inhibition of cAMP-phosphodiesterase by biflavones of Ginkgo biloba in rat adipose tissue. J Nat Prod. 61:1386-1387, 1998 https://doi.org/10.1021/np970569m
- Banerjee, T., Valacchi, G., Ziboh, V.A., van der Vliet, A. Inhibition of TNFalpha-induced cyclooxygenase-2 expression by amentoflavone through suppression of NF-kappaB activation in A549 cells. Mol Cell Biochem. 238:105-110, 2002 https://doi.org/10.1023/A:1019963222510
- Woo, E.R., Lee, J.Y., Cho, I.J., Kim, S.G., Kang, K.W. Amentoflavone inhibits the induction of nitric oxide synthase by inhibiting NF-kB activation in macrophages. Pharmacological Research. 51:539-546, 2005 https://doi.org/10.1016/j.phrs.2005.02.002
- Kang, S.S., Kim, J.S., Kawk, W.J. and Kim, K.H. Biflavonoids from the aerial part of Lonicera japonica Kor. J. Pharmacognosy. 21:111-120, 1990
- Son, K.H., Park, J.O., Chung, K.C., Chang, H.W., Kim, H.P., Kim, J.S. and Kang, S.S. Flavonoids from the aerial part of Lonicera japonica. Arch. Pharm. Res. 15:365-370, 1992 https://doi.org/10.1007/BF02974114
- Shin, D.I. and J, Kim. Kor. J. Pharmacognosy. 22:207-210, 1991
- C. Patterson, J. Ruef, N.R. Madamanchi, P. Barry-Lane, Z. Hu, C. Horaist, C.A. Ballinger, A.R. Brasier, C. Bode, and M. S. Runge, Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin. Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo, J. Biol. Chem. 274:19814-19822, 1999 https://doi.org/10.1074/jbc.274.28.19814
- C. Yan, H. Wang, D. Boyd, KiSS-1 represses 92-kDa type IV collagenase expression by down-regulating NF-kappa B binding to the promoter as a consequence of Ikappa Balpha -induced block of p65/p50 nuclear translocation, J. Biol. Chem. 276:1164-1172, 2001 https://doi.org/10.1074/jbc.M008681200
- R. Gum, E. Lengyel, J. Juarez, J.H. Chen, H. Sato, M.Seiki, D. Boyd, Stimulation of 92-kDa gelatinase B promoter activity by ras is mitogen-activated protein kinase kinase 1-independent and requires multiple transcription factor binding sites including closely spaced PEA3/ets and AP-1 sequences, J. Biol. Chem. 271:10672-10680, 1996 https://doi.org/10.1074/jbc.271.18.10672
- P. Huhtala, A. Tuuttila, L.T. Chow, J. Lohi, J. Keski-Oja, K. Tryggvason, Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells, J. Biol. Chem. 266:16485-16490, 1991
- M. Bond, R.P. Fabunmi, A.H. Baker, A.C. Newby, Synergistic upregulation of metalloproteinase-9 by growth factors and inflammatory cytokines: an absolute requirement for transcription factor NF-kappa B, FEBS. Lett. 435:29-34, 1998 https://doi.org/10.1016/S0014-5793(98)01034-5
- R Ross, Cell biology of atherosclerosis, Annu. Rev. Physiol. 57:791-804, 1995 https://doi.org/10.1146/annurev.ph.57.030195.004043
- A. Cho, M.A. Reidy, Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury, Circ. Res. 91:845-851, 2002 https://doi.org/10.1161/01.RES.0000040420.17366.2E
- Z.S. Galis, C. Johnson, D. Godin, R. Magid, J.M. Shipley, R.M. Senior, E. Ivan, Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling, Circ. Res. 91:852-859, 2002 https://doi.org/10.1161/01.RES.0000041036.86977.14