Table of Contents Author Guidelines Submit a Manuscript
International Journal of Inflammation
Volume 2014 (2014), Article ID 248240, 9 pages
http://dx.doi.org/10.1155/2014/248240
Research Article

Neurotensin Decreases the Proinflammatory Status of Human Skin Fibroblasts and Increases Epidermal Growth Factor Expression

1Faculdade de Ciências e Tecnologia, Universidade de Coimbra, 3000-456 Coimbra, Portugal
2Centro de Neurociências e Biologia Celular, Universidade de Coimbra, 3004-504 Coimbra, Portugal
3Faculdade de Farmácia, Universidade de Coimbra, 3000-548 Coimbra, Portugal
4Associação Portuguesa de Diabetes (APDP), 1250-189 Lisboa, Portugal

Received 30 May 2014; Revised 14 July 2014; Accepted 15 July 2014; Published 11 August 2014

Academic Editor: Francesco Maione

Copyright © 2014 Lucília Pereira da Silva 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. L. da Silva, E. Carvalho, and M. T. Cruz, “Role of neuropeptides in skin inflammation and its involvement in diabetic wound healing,” Expert Opinion on Biological Therapy, vol. 10, no. 10, pp. 1427–1439, 2010. View at Publisher · View at Google Scholar · View at Scopus
  2. A. Tellechea, E. Leal, A. Veves, and E. Carvalho, “Inflammatory and angiogenic abnormalities in diabetic wound healing: role of neuropeptides and therapeutic perspectives,” The Open Circulation and Vascular Journal, vol. 2, p. 42, 2010. View at Google Scholar
  3. W. Hartschuh, E. Weihe, and M. Reinecke, “Peptidergic (neurotensin, VIP, substance P) nerve fibres in the skin: immunohistochemical evidence of an involvement of neuropeptides in nociception, pruritus and inflammation,” British Journal of Dermatology, vol. 109, no. 25, pp. 14–17, 1983. View at Google Scholar · View at Scopus
  4. J. Donelan, W. Boucher, N. Papadopoulou et al., “Corticotropin-releasing hormone induces skin vascular permeability through a neurotensin-dependent process,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 20, pp. 7759–7764, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. L. K. Singh, X. Pang, N. Alexacos, R. Letourneau, and T. C. Theoharides, “Acute immobilization stress triggers skin mast cell degranulation via corticotropin releasing hormone, neurotensin, and substance P: a link to neurogenic skin disorders,” Brain, Behavior, and Immunity, vol. 13, no. 3, pp. 225–239, 1999. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Vasiadi, A. Therianou, K. D. Alysandratos et al., “Serum neurotensin (NT) is increased in psoriasis and NT induces vascular endothelial growth factor release from human mast cells,” British Journal of Dermatology, vol. 166, no. 6, pp. 1349–1352, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. T. C. Theoharides, K. D. Alysandratos, and A. Angelidou, “Mast cells and inflammation,” Biochimica et Biophysica Acta, vol. 1822, no. 1, pp. 21–33, 2012. View at Google Scholar
  8. K. Alysandratos, S. Asadi, A. Angelidou et al., “Neurotensin and CRH interactions augment human mast cell activation,” PLoS ONE, vol. 7, no. 11, Article ID e48934, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Carraway, D. E. Cochrane, and J. B. Lansman, “Neurotensin stimulates exocytotic histamine secretion from rat mast cells and elevates plasma histamine levels,” Journal of Physiology, vol. 323, pp. 403–414, 1982. View at Google Scholar · View at Scopus
  10. D. E. Cochrane, R. E. Carraway, K. Harrington, M. Laudano, S. Rawlings, and R. S. Feldberg, “HMC-1 human mast cells synthesize neurotensin (NT) precursor, secrete bioactive NT-like peptide(s) and express NT receptor NTS1,” Inflammation Research, vol. 60, no. 12, pp. 1139–1151, 2011. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Ramez, M. Bagot, M. Nikolova et al., “Functional characterization of neurotensin receptors in human cutaneous T cell lymphoma malignant lymphocytes,” Journal of Investigative Dermatology, vol. 117, no. 3, pp. 687–693, 2001. View at Publisher · View at Google Scholar · View at Scopus
  12. L. da Silva, B. M. Neves, L. Moura, M. T. Cruz, and E. Carvalho, “Neurotensin downregulates the pro-inflammatory properties of skin dendritic cells and increases epidermal growth factor expression,” Biochimica et Biophysica Acta, vol. 1813, no. 10, pp. 1863–1871, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. J. M. Sorrell and A. I. Caplan, “Fibroblast heterogeneity: more than skin deep,” Journal of Cell Science, vol. 117, no. 5, pp. 667–675, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. R. S. Smith, T. J. Smith, T. M. Blieden, and R. P. Phipps, “Fibroblasts as sentinel cells: synthesis of chemokines and regulation of inflammation,” The American Journal of Pathology, vol. 151, no. 2, pp. 317–322, 1997. View at Google Scholar · View at Scopus
  15. R. K. Winkelmann, “The cutaneous innervation of human newborn prepuce.,” The Journal of Investigative Dermatology, vol. 26, no. 1, pp. 53–67, 1956. View at Google Scholar · View at Scopus
  16. A. K. Antony, W. Kong, and H. P. Lorenz, “Upregulation of neurodevelopmental genes during scarless healing,” Annals of Plastic Surgery, vol. 64, no. 2, pp. 247–250, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. B. M. Neves, M. T. Cruz, V. Francisco et al., “Differential roles of PI3-Kinase, MAPKs and NF-κB on the manipulation of dendritic cell Th1/Th2 cytokine/chemokine polarizing profile,” Molecular Immunology, vol. 46, no. 13, pp. 2481–2492, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. R. Goldman, Z. B. Shavit, and D. Romeo, “Neurotensin modulates human neutrophil locomotion and phagocytic capability,” FEBS Letters, vol. 159, no. 1-2, pp. 63–67, 1983. View at Publisher · View at Google Scholar · View at Scopus
  19. I. Lemaire, “Neurotensin enhances IL-1 production by activated alveolar macrophages,” Journal of Immunology, vol. 140, no. 9, pp. 2983–2988, 1988. View at Google Scholar · View at Scopus
  20. J. J. Garrido, R. M. Arahuetes, A. Hernanz, and M. De la Fuente, “Modulation by neurotensin and neuromedin N of adherence and chemotaxis capacity of murine lymphocytes,” Regulatory Peptides, vol. 41, no. 1, pp. 27–37, 1992. View at Publisher · View at Google Scholar · View at Scopus
  21. I. Castagliuolo, C. Wang, L. Valenick et al., “Neurotensin is a proinflammatory neuropeptide in colonic inflammation,” Journal of Clinical Investigation, vol. 103, no. 6, pp. 843–849, 1999. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Martin, J. Vincent, and J. Mazella, “Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia,” Journal of Neuroscience, vol. 23, no. 4, pp. 1198–1205, 2003. View at Google Scholar · View at Scopus
  23. D. Zhao, S. Kuhnt-Moore, H. Zeng, J. S. Wu, M. P. Moyer, and C. Pothoulakis, “Neurotensin stimulates IL-8 expression in human colonic epithelial cells through Rho GTPase-mediated NF-κB pathways,” The American Journal of Physiology—Cell Physiology, vol. 284, no. 6, pp. C1397–C1404, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. E. Dicou, J. P. Vincent, and J. Mazella, “Neurotensin receptor-3/sortilin mediates neurotensin-induced cytokine/chemokine expression in a marine microglial cell line,” Journal of Neuroscience Research, vol. 78, no. 1, pp. 92–99, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. S. F. Assimakopoulos, C. D. Scopa, V. N. Nikolopoulou, and C. E. Vagianos, “Pleiotropic effects of bombesin and neurotensin on intestinal mucosa: not just trefoil peptides,” World Journal of Gastroenterology, vol. 14, no. 22, pp. 3602–3603, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. K. L. Bost, S. A. L. Breeding, and D. W. Pascual, “Modulation of the mRNAs encoding substance P and its receptor in rat macrophages by LPS,” Regional Immunology, vol. 4, no. 2, pp. 105–112, 1992. View at Google Scholar · View at Scopus
  27. A. P. Silva, C. Cavadas, B. Baïsse-Agushi, O. Spertini, H. R. Brunner, and E. Grouzmann, “NPY, NPY receptors, and DPP IV activity are modulated by LPS, TNF-α and IFN-κ in HUVEC,” Regulatory Peptides, vol. 116, no. 1–3, pp. 71–79, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. J. Grzybowski, E. Ołdak, and M. K. Janiak, “Local application of G-CSF, GM-CSF and EGF in treatment of wounds,” Postępy Higieny i Medycyny Doświadczalnej, vol. 53, no. 1, pp. 75–86, 1999. View at Google Scholar · View at Scopus
  29. M. Jost, C. Kari, and U. Rodeck, “The EGF receptor—an essential regulator of multiple epidermal functions,” European Journal of Dermatology, vol. 10, no. 7, pp. 505–510, 2000. View at Google Scholar · View at Scopus
  30. C. Esche, C. Stellato, and L. A. Beck, “Chemokines: key players in innate and adaptive immunity,” Journal of Investigative Dermatology, vol. 125, no. 4, pp. 615–628, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Baggiolini, A. Walz, and S. L. Kunkel, “Neutrophil-activating peptide-1/interleukin 8, a novel cytokine that activates neutrophils,” The Journal of Clinical Investigation, vol. 84, no. 4, pp. 1045–1049, 1989. View at Publisher · View at Google Scholar · View at Scopus
  32. E. A. Garcia-Zepeda, M. E. Rothenberg, R. T. Ownbey, J. Celestin, P. Leder, and A. D. Luster, “Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia,” Nature Medicine, vol. 2, no. 4, pp. 449–456, 1996. View at Publisher · View at Google Scholar · View at Scopus
  33. U. Forssmann, M. Uguccioni, P. Loetscher et al., “Eotaxin-2, a novel CC chemokine that is selective for the chemokine receptor CCR3, and acts like eotaxin on human eosinophil and basophil leukocytes,” Journal of Experimental Medicine, vol. 185, no. 12, pp. 2171–2176, 1997. View at Publisher · View at Google Scholar · View at Scopus
  34. F. Sallusto, C. R. Mackay, and A. Lanzavecchia, “Selective expression of the eotaxin receptor CCR3 by human T helper 2 cells,” Science, vol. 277, no. 5334, pp. 2005–2007, 1997. View at Publisher · View at Google Scholar · View at Scopus
  35. A. de Paulis, F. Annunziato, L. di Gioia et al., “Expression of the chemokine receptor CCR3 on human mast cells,” International Archives of Allergy and Immunology, vol. 124, no. 1–3, pp. 146–150, 2001. View at Publisher · View at Google Scholar · View at Scopus
  36. T. Fujisawa, Y. Kato, H. Nagase et al., “Chemokines induce eosinophil degranulation through CCR-3,” Journal of Allergy and Clinical Immunology, vol. 106, no. 3, pp. 507–513, 2000. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Uguccioni, C. R. Mackay, B. Ochensberger et al., “High expression of the chemokine receptor CCR3 in human blood basophils. Role in activation by eotaxin, MCP-4, and other chemokines,” The Journal of Clinical Investigation, vol. 100, no. 5, pp. 1137–1143, 1997. View at Publisher · View at Google Scholar · View at Scopus
  38. S. J. Ono, T. Nakamura, D. Miyazaki, M. Ohbayashi, M. Dawson, and M. Toda, “Chemokines: roles in leukocyte development, trafficking, and effector function,” Journal of Allergy and Clinical Immunology, vol. 111, no. 6, pp. 1185–1199, 2003. View at Publisher · View at Google Scholar · View at Scopus
  39. X. Lai, Z. Wang, L. Wei, and L. Wang, “Effect of substance P released from peripheral nerve ending on endogenous expression of epidermal growth factor and its receptor in wound healing,” Chinese Journal of Traumatology, vol. 5, no. 3, pp. 176–179, 2002. View at Google Scholar · View at Scopus
  40. Y. Shirakata, “Regulation of epidermal keratinocytes by growth factors,” Journal of Dermatological Science, vol. 59, no. 2, pp. 73–80, 2010. View at Publisher · View at Google Scholar · View at Scopus