Table of Contents Author Guidelines Submit a Manuscript
Erratum

An erratum for this article has been published. To view the erratum, please click here.

Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 901329, 28 pages
http://dx.doi.org/10.1155/2011/901329
Research Article

Protein Profiling of Human Nonpigmented Ciliary Epithelium Cell Secretome: The Differentiation Factors Characterization for Retinal Ganglion Cell line

1Department of Chemical and Material Engineering, National Yunlin University of Science and Technology, 123 University Road, Section 3, Douliou, Yunlin 64002, Taiwan
2Department of Pharmacology and Neuroscience, University of North Texas Health Science Center, USA
3Department of Medical Imaging and Radiological Sciences, Kaohsiung Medical University, 100 Shi-Chuan 1st Road, Kaohsiung 80708, Taiwan
4Department of Medical Laboratory Science and Biotechnology, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
5Department of Neurology, Kaohsiung Medical University Chung-Ho Memorial Hospital, Kaohsiung 80708, Taiwan
6Department of Fiber and Composite Materials, Feng Chia University, Taichung 40724, Taiwan
7National Sun Yat-Sen University and Kaohsiung Medical University Joint Research Center, Kaohsiung 80708, Taiwan
8Center for Research Resources and Development, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
9Center of Excellence for Environmental Medicine, Kaohsiung Medical University, Kaohsiung 80708, Taiwan

Received 5 April 2011; Revised 10 June 2011; Accepted 13 June 2011

Academic Editor: Daniel T. Monaghan

Copyright © 2011 Ming-Hui Yang 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.

Linked References

  1. V. R. Rao, R. R. Krishnamoorthy, and T. Yorio, “Endothelin-1 mediated regulation of extracellular matrix collagens in cells of human lamina cribrosa,” Experimental Eye Research, vol. 86, no. 6, pp. 886–894, 2008. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Hernández, J. H. Urcola, and E. Vecino, “Retinal ganglion cell neuroprotection in a rat model of glaucoma following brimonidine, latanoprost or combined treatments,” Experimental Eye Research, vol. 86, no. 5, pp. 798–806, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. H. Quigley and A. T. Broman, “The number of people with glaucoma worldwide in 2010 and 2020,” British Journal of Ophthalmology, vol. 90, no. 3, pp. 262–267, 2006. View at Publisher · View at Google Scholar · View at Scopus
  4. H. A. Quigley, “Glaucoma: macrocosm to microcosm the Friedenwald lecture,” Investigative Ophthalmology and Visual Science, vol. 46, no. 8, pp. 2663–2670, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. J. E. Morgan, H. Uchida, and J. Caprioli, “Retinal ganglion cell death in experimental glaucoma,” British Journal of Ophthalmology, vol. 84, no. 3, pp. 303–310, 2000. View at Publisher · View at Google Scholar · View at Scopus
  6. G. R. Howell, R. T. Libby, T. C. Jakobs et al., “Axons of retinal ganglion cells are insulted in the optic nerve early in DBA/2J glaucoma,” Journal of Cell Biology, vol. 179, no. 7, pp. 1523–1537, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. N. A. Castle, “Aquaporins as targets for drug discovery,” Drug Discovery Today, vol. 10, no. 7, pp. 485–493, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. R. W. Rodieck, The First Steps in Seeing, Sinauer Associates, Sunderland, Mass, USA, 1998.
  9. B. Schwartz, J. C. Rieser, and S. L. Fishbein, “Fluorescein angiographic defects of the optic disc in glaucoma,” Archives of Ophthalmology, vol. 95, no. 11, pp. 1961–1974, 1977. View at Google Scholar · View at Scopus
  10. C. J. Barnstable and U. C. Drager, “Thy-1 antigen: a ganglion cell specific marker in rodent retina,” Neuroscience, vol. 11, no. 4, pp. 847–855, 1984. View at Publisher · View at Google Scholar · View at Scopus
  11. Z. Q. Xiang, B. B. Knowles, J. W. McCarrick, and H. C. J. Ertl, “Immune effector mechanisms required for protection to rabies virus,” Virology, vol. 214, no. 2, pp. 398–404, 1995. View at Publisher · View at Google Scholar · View at Scopus
  12. Y. Otori, S. Kusaka, A. Kawasaki, H. Morimura, A. Miki, and Y. Tano, “Protective effect of nilvadipine against glutamate neurotoxicity in purified retinal ganglion cells,” Brain Research, vol. 961, no. 2, pp. 213–219, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. M. Coca-Prados, J. Escribano, and J. Ortego, “Differential gene expression in the human ciliary epithelium,” Progress in Retinal and Eye Research, vol. 18, no. 3, pp. 403–429, 1999. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Escribano, J. Ortego, and M. Coca-Prados, “Isolation and characterization of cell-specific cDNA clones from a subtractive library of the ocular ciliary body of a single normal human donor: transcription and synthesis of plasma proteins,” Journal of Biochemistry, vol. 118, no. 5, pp. 921–931, 1995. View at Google Scholar · View at Scopus
  15. J. Ortego and M. Coca-Prados, “Molecular characterization and differential gene induction of the neuroendocrine-specific genes neurotensin, neurotensin receptor, PC1, PC2, and 7B2 in the human ocular ciliary epithelium,” Journal of Neurochemistry, vol. 69, no. 5, pp. 1829–1839, 1997. View at Google Scholar · View at Scopus
  16. N. J. van Bergen, J. P. Wood, G. Chidlow et al., “Recharacterization of the RGC-5 retinal ganglion cell line,” Investigative Ophthalmology and Visual Science, vol. 50, no. 9, pp. 4267–4272, 2009. View at Publisher · View at Google Scholar · View at Scopus
  17. Y. C. Tyan, H. Y. Wu, W. C. Su, P. W. Chen, and P. C. Liao, “Proteomic analysis of human pleural effusion,” Proteomics, vol. 5, no. 4, pp. 1062–1074, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. Y. C. Tyan, H. Y. Wu, W. W. Lai, W. C. Su, and P. C. Liao, “Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry,” Journal of Proteome Research, vol. 4, no. 4, pp. 1274–1286, 2005. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Pandey, A. V. Podtelejnikov, B. Blagoev, X. R. Bustelo, M. Mann, and H. F. Lodish, “Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 1, pp. 179–184, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. C. O'Donovan, M. J. Martin, A. Gattiker, E. Gasteiger, A. Bairoch, and R. Apweiler, “High-quality protein knowledge resource: SWISS-PROT and TrEMBL,” Briefings in Bioinformatics, vol. 3, no. 3, pp. 275–284, 2002. View at Google Scholar · View at Scopus
  21. E. Gasteiger, A. Gattiker, C. Hoogland, I. Ivanyi, R. D. Appel, and A. Bairoch, “ExPASy: the proteomics server for in-depth protein knowledge and analysis,” Nucleic Acids Research, vol. 31, no. 13, pp. 3784–3788, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. S. R. Piersma, U. Fiedler, S. Span et al., “Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum,” Journal of Proteome Research, vol. 9, no. 4, pp. 1913–1922, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. M. Makridakis and A. Vlahou, “Secretome proteomics for discovery of cancer biomarkers,” Journal of Proteomics, vol. 73, no. 12, pp. 2291–2305, 2010. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Hathout, “Approaches to the study of the cell secretome,” Expert Review of Proteomics, vol. 4, no. 2, pp. 239–248, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. I. Surgucheva, A. D. Weisman, J. L. Goldberg, A. Shnyra, and A. Surguchov, “γ-synuclein as a marker of retinal ganglion cells,” Molecular Vision, vol. 14, pp. 1540–1548, 2008. View at Google Scholar · View at Scopus
  26. L. J. Frassetto, C. R. Schlieve, C. J. Lieven et al., “Kinase-dependent differentiation of a retinal ganglion cell precursor,” Investigative Ophthalmology and Visual Science, vol. 47, no. 1, pp. 427–438, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. J. P. Wood, G. Chidlow, T. Tran, J. G. Crowston, and R. J. Casson, “A comparison of differentiation protocols for RGC-5 cells,” Investigative Ophthalmology & Visual Science, vol. 51, no. 7, pp. 3774–3783, 2010. View at Google Scholar · View at Scopus
  28. R. R. Krishnamoorthy, P. Agarwal, G. Prasanna et al., “Characterization of a transformed rat retinal ganglion cell line,” Molecular Brain Research, vol. 86, no. 1-2, pp. 1–12, 2001. View at Publisher · View at Google Scholar · View at Scopus
  29. L. Gan, S. W. Wang, Z. Huang, and W. H. Klein, “POU domain factor Brn-3b is essential for retinal ganglion cell differentiation and survival but not for initial cell fate specification,” Developmental Biology, vol. 210, no. 2, pp. 469–480, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. X. Mu and W. H. Klein, “A gene regulatory hierarchy for retinal ganglion cell specification and differentiation,” Seminars in Cell and Developmental Biology, vol. 15, no. 1, pp. 115–123, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. J. D. Jaffe, H. C. Berg, and G. M. Church, “Proteogenomic mapping as a complementary method to perform genome annotation,” Proteomics, vol. 4, no. 1, pp. 59–77, 2004. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Guo, S. F. Ma, D. Grigoryev, J. Van Eyk, and J. G. N. Garcia, “1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome,” Proteomics, vol. 5, no. 17, pp. 4608–4624, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. N. M. Kumar, S. L. Sigurdson, D. Sheppard, and J. S. Lwebuga-Mukasa, “Differential modulation of integrin receptors and extracellular matrix laminin by transforming growth factor-β1 in rat alveolar epithelial cells,” Experimental Cell Research, vol. 221, no. 2, pp. 385–394, 1995. View at Publisher · View at Google Scholar · View at Scopus
  34. V. Alessandra, D. M. Lucia, G. Giuseppe et al., “Thrombospondin-1 is a mediator of the neurotypic differentiation induced by EGF in thymic epithelial cells,” Experimental Cell Research, vol. 248, no. 1, pp. 79–86, 1999. View at Publisher · View at Google Scholar · View at Scopus
  35. H. Miyajima-Uchida, H. Hayashi, R. Beppu et al., “Production and accumulation of thrombospondin-1 in human retinal pigment epithelial cells,” Investigative Ophthalmology and Visual Science, vol. 41, no. 2, pp. 561–567, 2000. View at Google Scholar · View at Scopus
  36. D. J. Liska, R. Hawkins, K. Wikstrom, and P. Bornstein, “Modulation of thrombospondin expression during differentiation of embryonal carcinoma cells,” Journal of Cellular Physiology, vol. 158, no. 3, pp. 495–505, 1994. View at Google Scholar · View at Scopus
  37. S. J. Suchard, P. J. Mansfield, and V. M. Dixit, “Modulation of thrombospondin receptor expression during HL-60 cell differentiation,” Journal of Immunology, vol. 152, no. 2, pp. 877–888, 1994. View at Google Scholar · View at Scopus
  38. M. Dreyfus, R. Dardik, B. S. Suh, A. Amsterdam, and J. Lahav, “Differentiation-controlled synthesis and binding of thrombospondin to granulosa cells,” Endocrinology, vol. 130, no. 5, pp. 2565–2570, 1992. View at Publisher · View at Google Scholar · View at Scopus
  39. K. S. O'Shea and V. M. Dixit, “Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo,” Journal of Cell Biology, vol. 107, no. 6, pp. 2737–2748, 1988. View at Google Scholar · View at Scopus
  40. K. Yu, J. Ge, J. B. Summers et al., “TSP-1 secreted by one marrow stroma cells contributes to retinal ganglion cell neurite outgrowth and survival,” PLoS One, vol. 3, no. 6, Article ID e2470, pp. 1–11, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. A. E. Canfield, A. B. Sutton, J. A. Hoyland, and A. M. Schor, “Association of thrombospondin-1 with osteogenic differentiation of retinal pericytes in vitro,” Journal of Cell Science, vol. 109, no. 2, pp. 343–353, 1996. View at Google Scholar · View at Scopus
  42. A. M. Delany and K. D. Hankenson, “Thrombospondin-2 and SPARC/osteonectin are critical regulators of bone remodeling,” Journal of Cell Communication and Signaling, vol. 3, no. 3-4, pp. 227–238, 2009. View at Publisher · View at Google Scholar · View at Scopus
  43. A. N. Qabar, Z. Lin, F. W. Wolf, K. S. O'Shea, J. Lawler, and V. M. Dixit, “Thrombospondin 3 is a developmentally regulated heparin binding protein,” Journal of Biological Chemistry, vol. 269, no. 2, pp. 1262–1269, 1994. View at Google Scholar · View at Scopus
  44. M. Blostein, J. Cuerquis, and J. Galipeau, “Galectin 3-binding protein is a potential contaminant of recombinantly produced factor IX,” Haemophilia, vol. 13, no. 6, pp. 701–706, 2007. View at Publisher · View at Google Scholar · View at Scopus
  45. T. Plavina, E. Wakshull, W. S. Hancock, and M. Hincapie, “Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery,” Journal of Proteome Research, vol. 6, no. 2, pp. 662–671, 2007. View at Publisher · View at Google Scholar · View at Scopus
  46. G. Calabrese, I. Sures, F. Pompetti, G. Natoli, G. Palka, and S. Iacobelli, “The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25,” Cytogenetics and Cell Genetics, vol. 69, no. 3-4, pp. 223–225, 1995. View at Google Scholar · View at Scopus
  47. K. Koths, E. Taylor, R. Halenbeck, C. Casipit, and A. Wang, “Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain,” Journal of Biological Chemistry, vol. 268, no. 19, pp. 14245–14249, 1993. View at Google Scholar · View at Scopus
  48. Y. Fukaya, H. Shimada, L. C. Wang, E. Zandi, and Y. A. DeClerck, “Identification of galectin-3-binding protein as a factor secreted by tumor cells that stimulates interleukin-6 expression in the bone marrow stroma,” Journal of Biological Chemistry, vol. 283, no. 27, pp. 18573–18581, 2008. View at Publisher · View at Google Scholar · View at Scopus
  49. S. A. Sullivan, L. K. Barthel, B. L. Largent, and P. A. Raymond, “A goldfish Notch-3 homologue is expressed in neurogenic regions of embryonic, adult and regenerating brain and retina,” Developmental Genetics, vol. 20, no. 3, pp. 208–223, 1997. View at Publisher · View at Google Scholar · View at Scopus
  50. Y. Qu, K. Sakamoto, S. Takeda, T. Kayano, M. Takagi, and K. Katsube, “Differential expression of notch genes in the neurogenesis of mouse embryos,” Oral Medicine & Pathology, vol. 3, pp. 21–28, 1998. View at Google Scholar
  51. M. Lardelli, R. Williams, T. Mitsiadis, and U. Lendahl, “Expression of the Notch 3 intracellular domain in mouse central nervous system progenitor cells is lethal and leads to disturbed neural tube development,” Mechanisms of Development, vol. 59, no. 2, pp. 177–190, 1996. View at Publisher · View at Google Scholar · View at Scopus
  52. A. Joutel, C. Corpechot, A. Ducros et al., “Tournier-Lasserve, Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia,” Nature, vol. 383, no. 6602, pp. 707–710, 1996. View at Google Scholar
  53. D. V. Tortoriello, Y. Sidis, D. A. Holtzman, W. E. Holmes, and A. L. Schneyer, “Human follistatin-related protein: a structural homologue of follistatin with nuclear localization,” Endocrinology, vol. 142, no. 8, pp. 3426–3434, 2001. View at Publisher · View at Google Scholar · View at Scopus
  54. J. Liu, T. Vänttinen, C. Hydén-Granskog, and R. Voutilainen, “Regulation of follistatin-related gene (FLRG) expression by protein kinase C and prostaglandin E(2) in cultured granulosa-luteal cells,” Molecular Human Reproduction, vol. 8, no. 11, pp. 992–997, 2002. View at Google Scholar · View at Scopus
  55. Y. Ehara, D. Sakurai, N. Tsuchiya et al., “Follistatin-related protein gene (FRP) is expressed in the synovial tissues of rheumatoid arthritis, but its polymorphisms are not associated with genetic susceptibility,” Clinical and Experimental Rheumatology, vol. 22, no. 6, pp. 707–712, 2004. View at Google Scholar · View at Scopus
  56. R. A. Brekken and E. H. Sage, “SPARC, a matricellular protein: at the crossroads of cell-matrix communication,” Matrix Biology, vol. 19, no. 8, pp. 815–827, 2001. View at Publisher · View at Google Scholar · View at Scopus
  57. A. D. Bradshaw and E. H. Sage, “SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury,” Journal of Clinical Investigation, vol. 107, no. 9, pp. 1049–1054, 2001. View at Google Scholar · View at Scopus
  58. A. D. Bradshaw, J. A. Bassuk, A. Francki, and E. H. Sage, “Expression and purification of recombinant human SPARC produced by baculovirus,” Molecular Cell Biology Research Communications, vol. 3, no. 6, pp. 345–351, 2000. View at Publisher · View at Google Scholar · View at Scopus
  59. M. J. Alvarez, F. Prada, E. Salvatierra et al., “Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity,” Cancer Research, vol. 65, no. 12, pp. 5123–5132, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. J. Nawarak, R. Huang-Liu, S. H. Kao et al., “Proteomics analysis of A375 human malignant melanoma cells in response to arbutin treatment,” Biochimica et Biophysica Acta, vol. 1794, no. 2, pp. 159–167, 2009. View at Publisher · View at Google Scholar · View at Scopus
  61. K. A. Daly, C. Lefévre, K. Nicholas, E. Deane, and P. Williamson, “Characterization and expression of Peroxiredoxin 1 in the neonatal tammar wallaby (Macropus eugenii),” Comparative Biochemistry and Physiology—B, vol. 149, no. 1, pp. 108–119, 2008. View at Publisher · View at Google Scholar · View at Scopus
  62. W. Lee, K. S. Choi, J. Riddell et al., “Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2,” Journal of Biological Chemistry, vol. 282, no. 30, pp. 22011–22022, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. P. Karihtala, A. Mäntyniemi, S. W. Kang, V. L. Kinnula, and Y. Soini, “Peroxiredoxins in breast carcinoma,” Clinical Cancer Research, vol. 9, no. 9, pp. 3418–3424, 2003. View at Google Scholar · View at Scopus
  64. S. H. Kim, M. Fountoulakis, N. Cairns, and G. Lubec, “Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down Syndrome,” Journal of Neural Transmission, Supplement, no. 61, pp. 223–235, 2001. View at Google Scholar · View at Scopus
  65. P. Lappalainen and D. G. Drubin, “Cofilin promotes rapid actin filament turnover in vivo,” Nature, vol. 388, no. 6637, pp. 78–82, 1997. View at Publisher · View at Google Scholar · View at Scopus
  66. A. McGough, B. Pope, W. Chiu, and A. Weeds, “Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function,” Journal of Cell Biology, vol. 138, no. 4, pp. 771–781, 1997. View at Publisher · View at Google Scholar · View at Scopus
  67. J. Toshima, J. Y. Toshima, T. Amano, N. Yang, S. Narumiya, and K. Mizuno, “Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation,” Molecular Biology of the Cell, vol. 12, no. 4, pp. 1131–1145, 2001. View at Google Scholar · View at Scopus
  68. P. Sinha, G. Hutter, E. Kottgen, M. Dietel, D. Schadendorf, and H. Lage, “Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas,” Electrophoresis, vol. 20, pp. 2952–2960, 1999. View at Google Scholar
  69. W. Witke, J. D. Sutherland, A. Sharpe, M. Arai, and D. J. Kwiatkowski, “Profilin I is essential for cell survival and cell division in early mouse development,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 7, pp. 3832–3836, 2001. View at Publisher · View at Google Scholar · View at Scopus
  70. M. Haugwitz, A. A. Noegel, J. Karakesisoglou, and M. Schleicher, “Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development,” Cell, vol. 79, no. 2, pp. 303–314, 1994. View at Publisher · View at Google Scholar · View at Scopus
  71. E. M. Verheyen and L. Cooley, “Profilin mutations disrupt multiple actin-dependent processes during Drosophila development,” Development, vol. 120, no. 4, pp. 717–728, 1994. View at Google Scholar · View at Scopus
  72. D. J. Mazzatti, G. Pawelec, R. Longdin, J. R. Powell, and R. J. Forsey, “SELDI-TOF-MS ProteinChip array profiling of T-cell clones propagated in long-term culture identifies human profilin-1 as a potential bio-marker of immunosenescence,” Proteome Science, vol. 5, article 7, pp. 1–13, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. L. Zou, M. Jaramillo, D. Whaley et al., “Profilin-1 is a negative regulator of mammary carcinoma aggressiveness,” British Journal of Cancer, vol. 97, no. 10, pp. 1361–1371, 2007. View at Publisher · View at Google Scholar · View at Scopus
  74. N. Wittenmayer, B. Jandrig, M. Rothkegel et al., “Tumor suppressor activity of profilin requires a functional actin binding site,” Molecular Biology of the Cell, vol. 15, no. 4, pp. 1600–1608, 2004. View at Publisher · View at Google Scholar · View at Scopus
  75. J. Hirabayashi, T. Hashidate, Y. Arata et al., “Oligosaccharide specificity of galectins: a search by frontal affinity chromatography,” Biochimica et Biophysica Acta, vol. 1572, no. 2-3, pp. 232–254, 2002. View at Publisher · View at Google Scholar · View at Scopus
  76. F. A. Van Den Brûle, P. L. Fernandez, C. Buicu et al., “Differential expression of galectin-1 and galectin-3 during first trimester human embryogenesis,” Developmental Dynamics, vol. 209, no. 4, pp. 399–405, 1997. View at Publisher · View at Google Scholar · View at Scopus
  77. G. A. Rabinovich, “Galectin-1 as a potential cancer target,” British Journal of Cancer, vol. 92, no. 7, pp. 1188–1192, 2005. View at Publisher · View at Google Scholar · View at Scopus
  78. K. Stowell, N. Pollock, and E. Langton, “Perinatal diagnosis of malignant hyperthermia susceptibility,” Anaesthesia and Intensive Care, vol. 35, no. 3, pp. 454–455, 2007. View at Google Scholar · View at Scopus
  79. H. J. Gabius, “Concepts of tumor lectinology,” Cancer Investigation, vol. 15, no. 5, pp. 454–464, 1997. View at Google Scholar · View at Scopus
  80. H. Legendre, C. Decaestecker, N. Nagy et al., “Prognostic values of galectin-3 and the macrophage migration inhibitory factor (MIF) in human colorectal cancers,” Modern Pathology, vol. 16, no. 5, pp. 491–504, 2003. View at Publisher · View at Google Scholar · View at Scopus
  81. S. Nakahara, N. Oka, and A. Raz, “On the role of galectin-3 in cancer apoptosis,” Apoptosis, vol. 10, no. 2, pp. 267–275, 2005. View at Publisher · View at Google Scholar · View at Scopus
  82. K. Goldring, G. E. Jones, R. Thiagarajah, and D. J. Watt, “The effect of galectin-1 on the differentiation of fibroblasts and myoblasts in vitro,” Journal of Cell Science, vol. 115, no. 2, pp. 355–366, 2002. View at Google Scholar · View at Scopus
  83. H. P. Hahn, M. Pang, J. He et al., “Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death,” Cell Death and Differentiation, vol. 11, no. 12, pp. 1277–1286, 2004. View at Publisher · View at Google Scholar · View at Scopus
  84. J. Ellerhorst, T. Nguyen, D. N. Cooper, Y. Estrov, D. Lotan, and R. Lotan, “Induction of differentiation and apoptosis in the prostate cancer cell line LNCaP by sodium butyrate and galectin-1,” International Journal of Oncology, vol. 14, pp. 225–232, 1999. View at Google Scholar
  85. R. J. O'Brien, I. Loke, J. E. Davies, I. B. Squire, and L. L. Ng, “Myotrophin in human heart failure,” Journal of the American College of Cardiology, vol. 42, no. 4, pp. 719–725, 2003. View at Publisher · View at Google Scholar · View at Scopus
  86. P. Sil, D. Mukherjee, and S. Sen, “Quantification of myotrophin from spontaneously hypertensive and normal rat hearts,” Circulation Research, vol. 76, no. 6, pp. 1020–1027, 1995. View at Google Scholar · View at Scopus
  87. D. P. Mukherjee, C. F. McTiernan, and S. Sen, “Myotrophin induces early response genes and enhances cardiac gene expression,” Hypertension, vol. 21, no. 2, pp. 142–148, 1993. View at Google Scholar · View at Scopus