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Oxidative Medicine and Cellular Longevity
Volume 2013 (2013), Article ID 628615, 10 pages
Albumin-Like Proteins Are Critical Regulators of Vascular Redox Signaling
Department of Biochemistry and Molecular Biology, University of Louisville School of Medicine, 580 South Preston Street, Louisville, KY 40202, USA
Received 30 October 2012; Accepted 20 December 2012
Academic Editor: Swaran J. S. Flora
Copyright © 2013 Kenneth S. Ramos et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- Y. Li and A. K. Jaiswal, “Regulation of human NAD(P)H: quinone oxidoreductase gene: role of AP1 binding site contained within human antioxidant response element,” Journal of Biological Chemistry, vol. 267, no. 21, pp. 15097–15104, 1992.
- Y. H. Chen and K. S. Ramos, “A CCAAT/enhancer-binding protein site within antioxidant/electrophile response element along with CREB-binding protein participate in the negative regulation of rat GST-Ya, gene in vascular smooth muscle cells,” Journal of Biological Chemistry, vol. 275, no. 35, pp. 27366–27376, 2000.
- J. K. Kerzee and K. S. Ramos, “Activation of c-Ha-ras by benzo(a)pyrene in vascular smooth muscle cells involves redox stress and aryl hydrocarbon receptor,” Molecular Pharmacology, vol. 58, no. 1, pp. 152–158, 2000.
- C. R. Partridge, Q. He, M. Brun, and K. S. Ramos, “Genetic networks of cooperative redox regulation of osteopontin,” Matrix Biology, vol. 27, no. 5, pp. 462–474, 2008.
- S. Liu and C. B. Pickett, “The rat liver glutathione S-transferase Ya subunit gene: characterization of the binding properties of a nuclear protein from HepG2 cells that has high affinity for the antioxidant response element,” Biochemistry, vol. 35, no. 35, pp. 11517–11521, 1996.
- T. Satoh, S. Saitoh, M. Hosaka, and K. Kosaka, “Simple ortho- and para-hydroquinones as compounds neuroprotective against oxidative stress in a manner associated with specific transcriptional activation,” Biochemical and Biophysical Research Communications, vol. 379, no. 2, pp. 537–541, 2009.
- K. P. Miller and K. S. Ramos, “Molecular mechanisms of environmental atherogenesis,” in Atherosclerosis and Oxidant Stress, J. L. Holzman, Ed., chapter 8, pp. 161–211, Springer, New York, NY, USA, 2007.
- M. T. Holderman, K. P. Miller, L. J. Dangott, and K. S. Ramos, “Identification of albumin precursor protein, phi AP3, and α-smooth muscle actin as novel components of redox sensing machinery in vascular smooth muscle cells,” Molecular Pharmacology, vol. 61, no. 5, pp. 1174–1183, 2002.
- K. Itoh, N. Wakabayashi, Y. Katoh et al., “Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain,” Genes and Development, vol. 13, no. 1, pp. 76–86, 1999.
- T. Nguyen, H. C. Huang, and C. B. Pickett, “Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK,” Journal of Biological Chemistry, vol. 275, no. 20, pp. 15466–15473, 2000.
- K. D. Huynh and V. J. Bardwell, “The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT,” Oncogene, vol. 17, no. 19, pp. 2473–2484, 1998.
- K. Igarashi, H. Hoshino, A. Muto, N. Suwabe, S. Nishikawa, H. Nakauchi, et al., “Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 3' enhancer,” Journal of Biological Chemistry, vol. 273, pp. 11783–11790, 1998.
- H. Hoshino, A. Kobayashi, M. Yoshida et al., “Oxidative stress abolishes leptomycin B-sensitive nuclear export of transcription repressor Bach2 that counteracts activation of Maf recognition element,” Journal of Biological Chemistry, vol. 275, no. 20, pp. 15370–15376, 2000.
- P. N. MacDonald, T. A. Baudino, H. Tokumaru, D. R. Dowd, and C. Zhang, “Vitamin D receptor and nuclear receptor coactivators: crucial interactions in vitamin D-mediated transcription,” Steroids, vol. 66, no. 3–5, pp. 171–176, 2001.
- I. Bogaerts, C. Verboven, A. Rabijns, E. Waelkens, H. Van Baelen, and C. De Ranter, “Purification, crystallization and preliminary X-ray investigation of the complex of human vitamin D binding protein and rabbit muscle actin,” Acta Crystallographica Section D, vol. 57, no. 5, pp. 740–742, 2001.
- H. Falahatpisheh, A. Nanez, D. Montoya-Durango, Y. Qian, E. Tiffany-Castiglioni, and K. S. Ramos, “Activation profiles of HSPA5 during the glomerular mesangial cell stress response to chemical injury,” Cell Stress and Chaperones, vol. 12, no. 3, pp. 209–218, 2007.
- S. S. Siddiqui, Z. K. Siddiqui, and A. B. Malik, “Albumin endocytosis in endothelial cells induces TGF-β receptor II signaling,” American Journal of Physiology-Lung Cellular and Molecular Physiology, vol. 286, no. 5, pp. L1016–L1026, 2004.
- J. K. Kerzee and K. S. Ramos, “Constitutive and inducible expression of Cyp1a1 and Cyp1b1 in vascular smooth muscle cells: role of the Ahr bHLH/PAS transcription factor,” Circulation Research, vol. 89, no. 7, pp. 573–582, 2001.
- R. Barouki and Y. Morel, “Repression of cytochrome P450 1A1 gene expression by oxidative stress: mechanisms and biological implications,” Biochemical Pharmacology, vol. 61, no. 5, pp. 511–516, 2001.
- N. Yamamoto and V. R. Naraparaju, “Role of vitamin D3-binding protein in activation of mouse macrophages,” Journal of Immunology, vol. 157, no. 4, pp. 1744–1749, 1996.
- L. Zhu and R. K. Crouch, “Albumin in the cornea is oxidized by hydrogen peroxide,” Cornea, vol. 11, no. 6, pp. 567–572, 1992.
- J. Jeyapaul and A. K. Jaiswal, “Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of γ-glutamylcysteine synthetase heavy subunit gene,” Biochemical Pharmacology, vol. 59, no. 11, pp. 1433–1439, 2000.
- A. M. Cantin, B. Paquette, M. Richter, and P. Larivée, “Albumin-mediated regulation of cellular glutathione and nuclear factor kappa B activation,” American Journal of Respiratory and Critical Care Medicine, vol. 162, no. 4, pp. 1539–1546, 2000.
- J. T. Barron, L. Gu, E. R. Rodriguez, and J. E. Parrillo, “Effect of serum albumin on vascular smooth muscle metabolism,” Biochimica et Biophysica Acta, vol. 1459, no. 1, pp. 35–48, 2000.
- C. Bennett and K. B. Cooke, “Further characterization of a melanoma-specific protein from human urine,” British Journal of Cancer, vol. 41, no. 5, pp. 734–744, 1980.
- J. J. Marchalonis, C. Schwabe, D. M. Gersten, and V. J. Hearing, “Amino-terminal variation in melanoma antigens,” Biochemical and Biophysical Research Communications, vol. 121, no. 1, pp. 196–202, 1984.
- Y. Tomita, P. M. Montague, and V. J. Hearing, “Monoclonal antibody production to a B16 melanoma associated antigen,” International Journal of Cancer, vol. 35, no. 4, pp. 543–547, 1985.
- V. J. Hearing, D. M. Gersten, and P. M. Montague, “Murine melanoma-specific tumor rejection activity elicited by a purified, melanoma-associated antigen,” Journal of Immunology, vol. 137, no. 1, pp. 379–384, 1986.
- D. M. Gertsen, D. Moody, W. D. Vieira, L. W. Law, and V. J. Hearing, “Production of monoclonal antibodies against the B700 murine melanoma antigen and their antimetastatic properties,” Biochimica et Biophysica Acta, vol. 1138, no. 2, pp. 109–114, 1992.
- N. K. Farzaneh, T. L. Walden Jr., V. J. Hearing, and D. M. Gersten, “B700, a melanoma-specific antigen, catalyzes metabolism of prostaglandin E2,” International Journal of Cancer, vol. 45, no. 1, pp. 104–108, 1990.
- N. K. Farzaneh, T. L. Walden, V. J. Hearing, and D. M. Gersten, “Comparison of the metabolic fate and tissue distribution of B700, an albumin-like melanoma-specific antigen with serum albumin in normal and tumor-bearing mice,” International Journal of Biochemistry, vol. 23, no. 12, pp. 1385–1391, 1991.
- N. K. Farzaneh, T. L. Walden, V. J. Hearing, and D. M. Gersten, “B700, an albumin-like melanoma-specific antigen, is a vitamin D binding protein,” European Journal of Cancer, vol. 27, no. 9, pp. 1158–1162, 1991.
- A. A. Karelin, M. M. Phylippova, Y. E. Blishchenko et al., “Albumin-like glycoprotein from human fetal tissue,” Biochemistry and Molecular Biology International, vol. 33, no. 1, pp. 73–80, 1994.
- S. Tang, J. C. K. Leung, K. Abe et al., “Albumin stimulates interleukin-8 expression in proximal tubular epithelial cells in vitro and in vivo,” Journal of Clinical Investigation, vol. 111, no. 4, pp. 515–527, 2003.
- M. Roche, P. Rondeau, N. R. Singh, E. Tarnus, and E. Bourdon, “The antioxidant properties of serum albumin,” FEBS Letters, vol. 582, no. 13, pp. 1783–1787, 2008.
- M. Fasano, S. Curry, E. Terreno et al., “The extraordinary ligand binding properties of human serum albumin,” IUBMB Life, vol. 57, no. 12, pp. 787–796, 2005.
- J. S. Koh, W. Lieberthal, S. Heydrick, and J. S. Levine, “Lysophosphatidic acid is a major serum noncytokine survival factor for murine macrophages which acts via the phosphatidylinositol 3-kinase signaling pathway,” Journal of Clinical Investigation, vol. 102, no. 4, pp. 716–727, 1998.
- J. Lu, A. J. Stewart, P. J. Sadler, T. J. T. Pinheiro, and C. A. Blindauer, “Albumin as a zinc carrier: properties of its high-affinity zinc-binding site,” Biochemical Society Transactions, vol. 36, no. 6, pp. 1317–1321, 2008.
- A. Maczurek, K. Hager, M. Kenklies et al., “Lipoic acid as an anti-inflammatory and neuroprotective treatment for Alzheimer's disease,” Advanced Drug Delivery Reviews, vol. 60, no. 13-14, pp. 1463–1470, 2008.
- A. Saifer and L. Goldman, “The free fatty acids bound to human serum albumin,” Journal of Lipid Research, vol. 2, pp. 268–270, 1961.
- S. S. Siddiqui, Z. K. Siddiqui, S. Uddin, R. D. Minshall, and A. B. Malik, “p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity,” American Journal of Physiology-Lung Cellular and Molecular Physiology, vol. 292, no. 1, pp. L114–L124, 2007.