Copper (II) ions modulate Angiogenin activity in human endothelial cells(424 views) Giacomelli C, Trincavelli ML, Satriano C, Hansson O, La Mendola D, Rizzarelli E, Martini C
Int J Biochem Cell B (ISSN: 1357-2725), 2015 Mar; 60: 185-196.
Keywords: Als, Angiogenesis, Copper, Human Endothelial Cells, Copper Ion, Messenger Rna, Mitogen Activated Protein Kinase 1, Alzheimer Disease, Article, Cell Migration, Cellular Distribution, Confocal Microscopy, Enzyme Phosphorylation, Gene Expression, Human Cell, Immunofluorescence, Parkinson Disease, Protein Expression, Protein Localization, Real Time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Umbilical Vein Endothelial Cell,
Affiliations: *** IBB - CNR ***
Department of Pharmacy, University of Pisa, ViaBonanno 6Pisa, Italy
Department of Chemical Sciences, University of Catania, Viale Andrea Doria, 6Catania, Italy
Institute of Biostructures and Bioimages, National Council of Research (CNR), Viale Andrea Doria, 6Catania, Italy
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Hu, G.F., Copper stimulates proliferation of human endothelial cells under culture (1998) J Cell Biochem, 69, pp. 326-335
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Jellinger, K.A., The relevance of metals in the pathophysiology of neurodegeneration, pathological considerations (2013) Int Rev Neurobiol, 110, pp. 1-47
Jimi, S.I., Ito, K.I., Kohno, K., Ono, M., Kuwano, M., Itagaki, Y., Ishikawa, H., Modulation by bovine angiogenin of tubular morphogenesis and expression of plasminogen activator in bovine endothelial cells (1995) Biochem Biophys Res Commun, 211, pp. 476-483
Kelleher, R.J., Soiza, R.L., Evidence of endothelial dysfunction in the development of Alzheimer's disease: Is Alzheimer's a vascular disorder? (2013) Am J Cardiovasc Dis, 3, pp. 197-226
Khoo, C.P., Micklem, K., Watt, S.M., A comparison of methods for quantifying angiogenesis in the Matrigel assay in vitro (2011) Tissue Eng Part C Methods, 17, pp. 895-906
Kim, Y.N., Kim, D.H., Decreased serum angiogenin level in Alzheimer's disease (2012) Prog Neuro-Psychoph, 38, pp. 116-120
Lee, F.S., Vallee, B.L., Characterization of ribonucleolytic activity of angiogenin towards tRNA. Biochem (1989) Biophys Res Commun, 161, pp. 121-126
Li, S., Hu, G.F., Emerging role of angiogenin in stress response and cell survival under adverse conditions (2012) J Cell Physiol, 227, pp. 2822-2826
McAuslan, B.R., Reilly, W., Endothelial cell phagokinesis in response to specific metal ions (1980) Exp Cell Res, 130, pp. 147-157
Padhi, A.K., Kumar, H., Vasaikar, S.V., Jayaram, B., Gomes, J., Mechanisms of loss of functions of human angiogenin variants implicated in amyotrophic lateral sclerosis (2012) PLoS One, p. e32479
Park, J.H., Lee, D.W., Park, K.S., Elevated serum copper and ceruloplasmin levels in Alzheimer's disease (2014) Asia Pac Psychiatry, 6, pp. 38-45
Peña, M.M., Lee, J., Thiele, D.J., A delicate balance: Homeostatic control of copper uptake and distribution (1999) J Nutr, 129, pp. 1251-1260
Raju, K.S., Alessandri, G., Ziche, M., Gullino, P.M., Ceruloplasmin, copper ions, and angiogenesis (1982) J Natl Cancer Inst, 69, pp. 1183-1188
Schafe, G.E., Swank, M.W., Rodrigues, S.M., Debiec, J., Doyère, V., Phosphorylation of ERK/MAP kinase is required for long-term potentiation in anatomically restricted regions of the lateral amygdala in vivo (2008) Learn Mem, 15, pp. 55-62
Sen, C.K., Khanna, S., Venojarvi, M., Trikha, P., Ellison, E.C., Hunt, T.K., Roy, S., Copper-induced vascular endothelial growth factor expression and wound healing (2002) Am J Physiol Heart Circ Physiol, 282, pp. H1821-H1827
Steidinger, T.U., Standaert, D.G., Yacoubian, T.A., A neuroprotective role for angiogenin in models of Parkinson's disease (2011) J Neurochem, 116, pp. 334-341
Wong, S.K., A 384-well cell-based phospho-ERK assay for dopamine D2 and D3 receptors (2004) Anal Biochem, 333, pp. 265-272
Yang, S.H., Sharrocks, A.D., Whitmarsh, A.J., MAP kinase signalling cascades and transcriptional regulation (2013) Gene, 513, pp. 1-13
Yeo, K.J., Hwang, E., Min, K.M., Jee, J.G., Lee, C.K., Hwang, K.Y., Jeon, Y.H., Cheong, H.K., The dual binding site of angiogenin and its inhibition mechanism: The crystal structure of the rat angiogenin-heparin complex (2014) Chem Commun (Camb), 50, pp. 12966-12969
Copper (II) ions modulate Angiogenin activity in human endothelial cells
Angiogenin (ANG), a member of the secreted ribonuclease family, is a potent angiogenesis stimulator that interacts with endothelial cells inducing a wide range of responses. Metal ions dyshomeostasis play a fundamental role in the onset of neurodegenerative diseases, in particular copper that is also involved in angiogenesis processes. It is known that vascular pathologies are present in neurodegenerative diseases and Angiogenin is down-regulated in Alzheimer and Parkinson diseases, as well as it has been found as one of the mutated genes in amyotrophic lateral sclerosis (ALS). Copper (II) induces an increase of Angiogenin binding to endothelial cells but, so far, the relationship between copper-ANG and angiogenesis induction remain unclear. Herein, the effects of copper (II) ions on Angiogenin activity and expression were evaluated. The binding of copper was demonstrated to affect the intracellular localization of the protein decreasing its nuclear translocation. Moreover, the ANG-copper (II) system negatively affects the protein-induced angiogenesis, as well as endothelial cells migration. Surprisingly, copper also reveals the ability to modulate the Angiogenin transcription. These results highlight the tight relationship between copper and Angiogenin, pointing out the biological relevance of ANG-copper system in the regulation of endothelial cell function, and revealing a possible new mechanism at the basis of vascular pathologies. Copyright 2015 Elsevier Ltd. All rights reserved
Copper (II) ions modulate Angiogenin activity in human endothelial cells
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