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BioMed Research International
Volume 2016, Article ID 4819327, 10 pages
http://dx.doi.org/10.1155/2016/4819327
Research Article

Serum Amyloid a Promotes Visfatin Expression in Macrophages

Department of Cardiology II, Weifang People’s Hospital, Weifang 261041, China

Received 8 December 2015; Revised 24 January 2016; Accepted 27 January 2016

Academic Editor: Fabrizio Montecucco

Copyright © 2016 Shixun Wang 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. S. Sandeep, K. Velmurugan, R. Deepa, and V. Mohan, “Serum visfatin in relation to visceral fat, obesity, and type 2 diabetes mellitus in Asian Indians,” Metabolism, vol. 56, no. 4, pp. 565–570, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. P. Wang, T.-Y. Xu, Y.-F. Guan, D.-F. Su, G.-R. Fan, and C.-Y. Miao, “Perivascular adipose tissue-derived visfatin is a vascular smooth muscle cell growth factor: role of nicotinamide mononucleotide,” Cardiovascular Research, vol. 81, no. 2, pp. 370–380, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. S.-R. Kim, Y.-H. Bae, S.-K. Bae et al., “Visfatin enhances ICAM-1 and VCAM-1 expression through ROS-dependent NF-κB activation in endothelial cells,” Biochimica et Biophysica Acta—Molecular Cell Research, vol. 1783, no. 5, pp. 886–895, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. R. Adya, B. K. Tan, J. Chen, and H. S. Randeva, “Pre-B cell colony enhancing factor (PBEF)/visfatin induces secretion of MCP-1 in human endothelial cells: role in visfatin-induced angiogenesis,” Atherosclerosis, vol. 205, no. 1, pp. 113–119, 2009. View at Publisher · View at Google Scholar
  5. W.-J. Lee, C.-S. Wu, H. Lin et al., “Visfatin-induced expression of inflammatory mediators in human endothelial cells through the NF-κB pathway,” International Journal of Obesity, vol. 33, no. 4, pp. 465–472, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Adya, B. K. Tan, A. Punn, J. Chen, and H. S. Randeva, “Visfatin induces human endothelial VEGF and MMP-2/9 production via MAPK and PI3K/Akt signalling pathways: novel insights into visfatin-induced angiogenesis,” Cardiovascular Research, vol. 78, no. 2, pp. 356–365, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. T. B. Dahl, A. Yndestad, M. Skjelland et al., “Increased expression of visfatin in macrophages of human unstable carotid and coronary atherosclerosis: possible role in inflammation and plaque destabilization,” Circulation, vol. 115, no. 8, pp. 972–980, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. I. Kushner, “The phenomenon of the acute phase response,” Annals of the New York Academy of Sciences, vol. 389, pp. 39–48, 1982. View at Publisher · View at Google Scholar · View at Scopus
  9. J. S. Hoffman and E. P. Benditt, “Changes in high density lipoprotein content following endotoxin administration in the mouse. Formation of serum amyloid protein-rich subfractions,” The Journal of Biological Chemistry, vol. 257, no. 17, pp. 10510–10517, 1982. View at Google Scholar · View at Scopus
  10. M.-S. Lee, S.-A. Yoo, C.-S. Cho, P.-G. Suh, W.-U. Kim, and S. H. Ryu, “Serum amyloid A binding to formyl peptide receptor-like 1 induces synovial hyperplasia and angiogenesis,” The Journal of Immunology, vol. 177, no. 8, pp. 5585–5594, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Song, K. Hsu, E. Yamen et al., “Serum amyloid A induction of cytokines in monocytes/macrophages and lymphocytes,” Atherosclerosis, vol. 207, no. 2, pp. 374–383, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. C. J. Furlaneto and A. Campa, “A novel function of serum amyloid A: a potent stimulus for the release of tumor necrosis factor-α, interleukin-1β, and interleukin-8 by human blood neutrophil,” Biochemical and Biophysical Research Communications, vol. 268, no. 2, pp. 405–408, 2000. View at Publisher · View at Google Scholar · View at Scopus
  13. B. Li, Z. Dong, H. Liu et al., “Serum amyloid A stimulates lipoprotein-associated phospholipase A2 expression in vitro and in vivo,” Atherosclerosis, vol. 228, no. 2, pp. 370–379, 2013. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Segawa, A. Fukuhara, N. Hosogai et al., “Visfatin in adipocytes is upregulated by hypoxia through HIF1α-dependent mechanism,” Biochemical and Biophysical Research Communications, vol. 349, no. 3, pp. 875–882, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. L. Björkman, J. Karlsson, A. Karlsson et al., “Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1,” Journal of Leukocyte Biology, vol. 83, no. 2, pp. 245–253, 2008. View at Publisher · View at Google Scholar · View at Scopus
  16. S. B. Su, W. Gong, J.-L. Gao et al., “A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells,” The Journal of Experimental Medicine, vol. 189, no. 2, pp. 395–402, 1999. View at Publisher · View at Google Scholar · View at Scopus
  17. L. R. Liu, S. P. Lin, C. C. Chen et al., “Serum amyloid a induces lipolysis by downregulating perilipin through ERK1/2 and PKA signaling pathways,” Obesity, vol. 19, no. 12, pp. 2301–2309, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. H. Y. Lee, M.-K. Kim, K. S. Park et al., “Serum amyloid A induces contrary immune responses via formyl peptide receptor-like 1 in human monocytes,” Molecular Pharmacology, vol. 70, no. 1, pp. 241–248, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. R. He, H. Sang, and R. D. Ye, “Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R,” Blood, vol. 101, no. 4, pp. 1572–1581, 2003. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Hector, B. Schwarzloh, J. Goehring et al., “TNF-α alters visfatin and adiponectin levels in human fat,” Hormone and Metabolic Research, vol. 39, no. 4, pp. 250–255, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. Y.-S. Bae, H. Y. Lee, E. J. Jo et al., “Identification of peptides that antagonize formyl peptide receptor-like 1-mediated signaling,” The Journal of Immunology, vol. 173, no. 1, pp. 607–614, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Karlsson, H. Fu, F. Boulay, J. Bylund, and C. Dahlgren, “The peptide Trp-Lys-Tyr-Met-Val-D-Met activates neutrophils through the formyl peptide receptor only when signaling through the formylpeptde receptor like 1 is blocked: a receptor switch with implications for signal transduction studies with inhibitors and receptor antagonists,” Biochemical Pharmacology, vol. 71, no. 10, pp. 1488–1496, 2006. View at Publisher · View at Google Scholar · View at Scopus