참고문헌
- Peterson, J. and Dwyer, J. : Flavonoids: dietary occurrence and biochemical activity. Nutr. Res. 18, 1995 (1988) https://doi.org/10.1016/S0271-5317(98)00169-9
- Lee, J. H., Zhou, H. Y., Cho, S. Y., Kim, Y. S., Lee, Y. S. and Jeong, C. S. : Anti-inflammatory mechanisms of apigenin: inhibition of cyclooxygenase-2 expression, adhesion of monocytes to human umbilical vein endothelial cells, and expression of cellular adhesion molecules. Arch. Pharm. Res. 30, 1318 (2007) https://doi.org/10.1007/BF02980273
- Rezai-Zadeh, K., Ehrhart, J., Bai, Y., Sanberg, P. R., Bickford, P., Tan, J. and Shytle, R. D. : Apigenin and luteolin modulate microglial activation via inhibition of STAT1-induced CD40 expression. J. Neuroinflammation 5, 41 (2008) https://doi.org/10.1186/1742-2094-5-41
- Psotova, J., Chlopcikova, S., Miketova, P., Hrbac, J. and Simanek, V. : Chemoprotective effect of plant phenolics against anthracycline-induced toxicity on rat cardiomyocytes. Part III. Apigenin, baicalelin, kaempherol, luteolin and quercetin. Phytother. Res. 18, 516 (2004) https://doi.org/10.1002/ptr.1462
- Caltagirone, S., Rossi, C., Poggi, A., Ranelletti, F. O., Natali, P. G., Brunetti, M., Aiello, F. B. and Piantelli, M. : Flavonoids apigenin and quercetin inhibit melanoma growth and metastatic potential. Int. J. Cancer 87, 595 (2000) https://doi.org/10.1002/1097-0215(20000815)87:4<595::AID-IJC21>3.0.CO;2-5
-
Wang, W., Heideman, L., Chung, C. S., Pelling, J. C., Koehler, K. J. and Birt, D. F. : Cell-cycle arrest at
$G_2$ /M and growth inhibition by apigenin in human colon carcinoma cell lines. Mol. Carcinog. 28, 102 (2000) https://doi.org/10.1002/1098-2744(200006)28:2<102::AID-MC6>3.0.CO;2-2 - Choi, S. I., Jeong, C. S., Cho, S. Y. and Lee, Y. S. : Mechanism of apoptosis induced by apigenin in HepG2 human hepatoma cells: involvement of reactive oxygen species generated by NADPH oxidase. Arch. Pharm. Res. 30, 1328 (2007) https://doi.org/10.1007/BF02980274
- Shindo, K., Saito, E., Sekiya, M., Matsui, T. and Koike, Y. : Antioxidative activity of the flower of Torenia fournieri. Nat. Med. (Tokyo) 62, 247 (2008)
- Ma, X., Li, Y. F., Gao, Q., Ye, Z. G., Lu, X. J., Wang, H. P., Jiang, H. D., Bruce, I. C. and Xia, Q. : Inhibition of superoxide anion-mediated impairment of endothelium by treatment with luteolin and apigenin in rat mesenteric artery. Life Sci. 83, 110 (2008) https://doi.org/10.1016/j.lfs.2008.05.010
- Panda, S. and Kar, A. : Apigenin (4',5,7-trihydroxyflavone) regulates hyperglycaemia, thyroid dysfunction and lipid peroxidation in alloxan-induced diabetic mice. J. Pharm. Pharmacol. 59, 1543 (2007) https://doi.org/10.1211/jpp.59.11.0012
- Sim, G. S., Lee, B. C., Cho, H. S., Lee, J. W., Kim, J. H., Lee, D. H., Kim, J. H., Pyo, H. B., Moon, D. C., Oh, K. W., Yun, Y. P. and Hong, J. T. : Structure activity relationship of antioxidative property of flavonoids and inhibitory effect on matrix metalloproteinase activity in UVA-irradiated human dermal fibroblast. Arch. Pharm. Res. 30, 290 (2007) https://doi.org/10.1007/BF02977608
- Shukla, S. and Gupta, S. : Apigenin-induced prostate cancer cell death is initiated by reactive oxygen species and p53 activation. Free Radic. Biol. Med. 44, 1833 (2008) https://doi.org/10.1016/j.freeradbiomed.2008.02.007
-
Kim, M. H., Jeong, C. S., Yoon, H. R., Kim, G. H. and Lee, Y. S. : Involvement of
$K^+-Cl^-$ -cotransport in the apigenin-Induced generation of reactive oxygen species in IMR-32 human neuroblastoma cells. J. Appl. Pharmacol. 14, 137 (2006) - Seiberg, M. : Kerationcytemelanocyte interaction during melanosome transfer. Piment Cell Res. 14, 236 (2001) https://doi.org/10.1034/j.1600-0749.2001.140402.x
- Hill, H. Z., Li, W., Xin, P. and Mitchell, D. L. : Melanin: a two edged sword? Pigment Cell Res. 10, 158 (1997) https://doi.org/10.1111/j.1600-0749.1997.tb00478.x
- Cabanes, J., Chazarra, S. and GarciaCarmona, F. : Kojic acid, a cosmetic skin whitening agent, is a slowbinding inhibitor of catecholase activity of tyrosinase. J. Pharm. Pharmacol. 46, 982 (1994) https://doi.org/10.1111/j.2042-7158.1994.tb03253.x
- Marmol, V. and Beermann, F. : Tyrosinase and related protein in mammalian pigmentation. FEBS Letters 381, 165 (1996) https://doi.org/10.1016/0014-5793(96)00109-3
- Hearing, V. J. and Tsukamoto, K. : Biochemical control of melanogenesis and melanosomal organization. J. Invest. Dermatol. Symp. Proc. 4, 24 (1999)
- Lee, K. E., Sim, G. S., Kim, J. H., Park, S. M., Lee. B. C., Yun, Y. P., Zhang, Y. H. and Pyo, H. B. : Effects of the Scirpi rhizoma on antixodiation and melanogenesis. Yakhak Hoeji 48, 323 (2004)
- Cho, Y. H., Lee, B. C., Kim, J. H., Kim, J. H., Pyo, H. B., Zhang, Y. H. and Park, H. D. : Effect of Aetemisia anomala S. Moore on antioxidant activity and melanogenesis, Kor. J. Pharmacognosy 36, 273 (2005)
- Cossins, A. R. and Gibson, J. S. : Volume-sensitive transport systems and volume homeostasis in vertebrate red blood cells. J. Exp. Biol. 200, 343 (1997)
- Lauf, P. K., Bauer, J., Adragna, N. C., Fujise, H., Zade-Oppen, A. M., Ryu, K. H. and Delpire, E. : Erythrocyte K-Cl cotransport: properties and regulation. Am. J. Physiol. 263, C917 (1992) https://doi.org/10.1152/ajpcell.1992.263.5.C917
-
Amlal, H., Paillard, M. and Bichara, M. :
$Cl^-$ -dependent$NH_4^{+_4}$ transport mechanisms in medullary thick ascending limb cells. Am. J. Physiol. 267, C1607 (1994) https://doi.org/10.1152/ajpcell.1994.267.6.C1607 - Greger, R. and Schlatter, E. : Properties of the basolateral membrane of the cortical thick ascending limb of Henle's loop of rabbit kidney. A model for secondary active chloride transport. Pflugers Arch. 396, 325 (1983) https://doi.org/10.1007/BF01063938
- Perry, P. B. and O'Neill, W. C. : Swelling-activated K fluxes in vascular endothelial cells: volume regulation via K-Cl cotransport and K channels. Am. J. Physiol. 265, C763 (1993) https://doi.org/10.1152/ajpcell.1993.265.3.C763
- Adragna, N. C., White, R. E., Orlov, S. N. and Lauf, P. K. : KCl cotransport in vascular smooth muscle and erythrocytes: possible implication in vasodilation. Am. J. Physiol. 278, C381 (2000) https://doi.org/10.1152/ajpcell.2000.278.2.C381
-
Yan, G. X., Chen, J., Yamada, K. A., Kleber, A. G. and Corr, P. B. : Contribution of shrinkage of extracellular space to extracellular
$K^+$ accumulation in myocardial ischaemia of the rabbit. J. Physiol. (London) 490, 215 (1996) https://doi.org/10.1113/jphysiol.1996.sp021137 -
Weil-Maslansky, E., Gutman, Y. and Sasson, S. : Insulin activates furosemide-sensitive
$K^+\;and\;Cl^-$ uptake system in BC3H1 cells. Am. J. Physiol. 267, C932 (1994) https://doi.org/10.1152/ajpcell.1994.267.4.C932 -
Rivera, C., Voipio, J., Payne, J. A., Ruusuvuori, E., Latineen, H., Lamsa, K., Pirvola, U., Saarma, M. and Kaila, K. : The
$K^+/Cl^-$ co-transporter KCC2 renders GABA hyperpolarizing during neuronal maturation. Nature 397, 251 (1999) https://doi.org/10.1038/16697 - Lauf, P. K., Bauer, J., Adragna, N. C., Fujise, H., Zade-Oppen, A. M., Ryu, K. H. and Delpire, E. : Erythrocyte K-Cl cotransport: properties and regulation. Am. J. Physiol. 263, C917 (1992) https://doi.org/10.1152/ajpcell.1992.263.5.C917
- Ellison, D. H., Velazquez, H. and Wright, F. S. : Stimulation of distal potassium secretion by low lumen chloride in the presence of barium. Am. J. Physiol. 248, F638 (1985)
-
Kim, J. A., Kang, Y. S. and Lee, Y. S. : Involvement of
$K%+-Cl^-$ -cotransport in the apoptosis induced by N-ethylmaleimide in HepG2 human hepatoblastoma cells. Eur. J. Pharmacol. 418, 1 (2001) https://doi.org/10.1016/S0014-2999(01)00861-5 - Wisman, K. N., Perkins, A. A., Jeffers, M. D. and Hagerman, A. E. : Accurate assessment of the bioactivities of redox-active polyphenolics in cell culture. J. Agric. Food Chem. 56, 7831 (2008) https://doi.org/10.1021/jf8011954
- Plochmann, K., Korte, G., Koutsilieri, E., Richling, E., Riederer, P., Rethwilm, A., Schreier, P. and Scheller, C. : Structure-activity relationships of flavonoid-induced cytotoxicity on human leukemia cells. Arch. Biochem. Biophys. 460, 1 (2007) https://doi.org/10.1016/j.abb.2007.02.003
- Choi, M. Y., Song, H. S., Hur, H. S. and Sim, S. S. : Whitening activity of luteolin related to the inhibition of cAMP pathway in alpha-MSH-stimulated B16 melanoma cells. Arch. Pharm. Res. 31, 1166 (2008) https://doi.org/10.1007/s12272-001-1284-4
- Kim, Y. J., Kang, K. S. and Yokozawa, T. : The anti-melanogenic effect of pycnogenol by its anti-oxidative actions. Food Chem. Toxicol. 46, 2466 (2008) https://doi.org/10.1016/j.fct.2008.04.002
- Nitoda, T., Isobe, T. and Kubo, I. : Effects of phenolic compounds isolated from Rabdosia japonica on B16-F10 melanoma cells. Phytother. Res. 22, 867 (2008) https://doi.org/10.1002/ptr.2373
- Ohguchi, K., Akao, Y. and Nozawa, Y. : Stimulation of melanogenesis by the citrus flavonoid naringenin in mouse B16 melanoma cells. Biosci. Biotechnol. Biochem. 70, 1499 (2006) https://doi.org/10.1271/bbb.50635
- Finn, G. J., Creaven, B. S. and Egan, D. A. : Activation of mitogen activated protein kinase pathways and melanogenesis by novel nitro-derivatives of 7-hydroxycomarin in human malignant melanoma cells. Eur. J. Pharm. Sci. 26, 16 (2005) https://doi.org/10.1016/j.ejps.2005.04.016
- Takeyama, R., Takekoshi, S., Nagata, H., Osamura, R. Y. and Kawana, S. : Quercetin-induced melanogenesis in a reconstituted three-dimensional human epidermal model. J. Mol. Histol. 35, 157 (2004) https://doi.org/10.1023/B:HIJO.0000023388.51625.6c
- Nagata, H., Takekoshi, S., Takeyama, R., Homma, T. and Yoshiyuki Osamura, R. : Quercetin enhances melanogenesis by increasing the activity and synthesis of tyrosinase in human melanoma cells and in normal human melanocytes. Pigment Cell Res. 17, 66 (2004) https://doi.org/10.1046/j.1600-0749.2003.00113.x
-
Fujii, T., Ohira, Y., Itomi, Y., Takahashi, Y., Asano, S., Morii, M., Takeguchi, N. and Sakai, H. : Inhibition of P-type ATPases by [(dihydroindenyl)oxy]acetic acid (DIOA), a
$K^+-Cl^-$ -cotransporter inhibitor. Eur. J. Pharmacol. 560, 123 (2007) https://doi.org/10.1016/j.ejphar.2006.12.031 - Bentley, N. J., Eisen, T. and Goding, C. R. : Melanocytespecific expression of the human tyrosinase promoter: activation by the microphthalmia gene product and role of the initiator. Mol. Cell. Biol. 14, 7996 (1994) https://doi.org/10.1128/MCB.14.12.7996
- Molina, D. M., Grewal, S. and Bardwell, L. : Characterization of an ERK-binding domain in microphthalmia-associated transcription factor and differential inhibition of ERK2-mediated substrate phosphorylation. J. Biol. Chem. 280, 42051 (2005) https://doi.org/10.1074/jbc.M510590200