Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2017, Article ID 1074054, 10 pages
https://doi.org/10.1155/2017/1074054
Research Article

Identification of Three Novel Splicing Variants and Expression Analysis of Chicken GPR1 Gene

Institute of Animal Genetics and Breeding, Sichuan Agricultural University, Chengdu, Sichuan 611130, China

Correspondence should be addressed to Qing Zhu; moc.361@9595gniquhz

Received 12 July 2016; Revised 8 November 2016; Accepted 24 November 2016; Published 22 January 2017

Academic Editor: Rita Casadio

Copyright © 2017 Xueyou Zhang 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. G. Vauquelin and B. von Mentzer, G Protein-Coupled Receptors, G Protein-Coupled Receptors: Molecular Pharmacology from Academic Concept to Pharmaceutical Research, 2007.
  2. N. King, C. T. Hittinger, and S. B. Carroll, “Evolution of key cell signaling and adhesion protein families predates animal origins,” Science, vol. 301, no. 5631, pp. 361–363, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Marchese, J. M. Docherty, T. Nguyen et al., “Cloning of human genes encoding novel G protein-coupled receptors,” Genomics, vol. 23, no. 3, pp. 609–618, 1994. View at Publisher · View at Google Scholar · View at Scopus
  4. B. A. Zabel, S. Nakae, L. Zúñiga et al., “Mast cell–expressed orphan receptor CCRL2 binds chemerin and is required for optimal induction of IgE-mediated passive cutaneous anaphylaxis,” The Journal of Experimental Medicine, vol. 205, no. 10, pp. 2207–2220, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. G. Barnea, W. Strapps, G. Herrada et al., “The genetic design of signaling cascades to record receptor activation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 1, pp. 64–69, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. J. Huang, J. Zhang, T. Lei et al., “Cloning of porcine chemerin, ChemR23 and GPR1 and their involvement in regulation of lipogenesis,” BMB Reports, vol. 43, no. 7, pp. 491–498, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. K. B. Goralski, T. C. McCarthy, E. A. Hanniman et al., “Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism,” Journal of Biological Chemistry, vol. 282, no. 38, pp. 28175–28188, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Takahashi, Y. Okimura, G. Iguchi et al., “Chemerin regulates β-cell function in mice,” Scientific Reports, vol. 1, article 123, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. J. B. Regard, I. T. Sato, and S. R. Coughlin, “Anatomical profiling of G protein-coupled receptor expression,” Cell, vol. 135, no. 3, pp. 561–571, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. J. L. Rourke, S. Muruganandan, H. J. Dranse, N. M. McMullen, and C. J. Sinal, “Gpr1 is an active chemerin receptor influencing glucose homeostasis in obese mice,” Journal of Endocrinology, vol. 222, no. 2, pp. 201–215, 2014. View at Publisher · View at Google Scholar · View at Scopus
  11. J. L. Rourke, H. J. Dranse, and C. J. Sinal, “CMKLR1 and GPR1 mediate chemerin signaling through the RhoA/ROCK pathway,” Molecular and Cellular Endocrinology, vol. 417, pp. 36–51, 2015. View at Publisher · View at Google Scholar
  12. C. Albanesi, C. Scarponi, S. Pallotta et al., “Chemerin expression marks early psoriatic skin lesions and correlates with plasmacytoid dendritic cell recruitment,” Journal of Experimental Medicine, vol. 206, no. 1, pp. 249–258, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. N. Shimizu, Y. Soda, K. Kanbe et al., “An orphan G protein-coupled receptor, GPR1, acts as a coreceptor to allow replication of human immunodeficiency virus types 1 and 2 in brain-derived cells,” Journal of Virology, vol. 73, no. 6, pp. 5231–5239, 1999. View at Google Scholar · View at Scopus
  14. N. Le Touz, J. Dumoulin, and F. Soldovieri, “Numerical study of the coupling of two identification methods—thermal and electromagnetic—for the reconstruction of inclusions in thick walls,” in Proceedings of the European Geosciences Union General Assembly, Vienna, Austria, April 2016.
  15. L. Woodley and J. Valcárcel, “Regulation of alternative pre-mRNA splicing,” Briefings in Functional Genomics and Proteomics, vol. 1, no. 3, pp. 266–277, 2002. View at Publisher · View at Google Scholar · View at Scopus
  16. Q. Pan, O. Shai, L. J. Lee, B. J. Frey, and B. J. Blencowe, “Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing,” Nature Genetics, vol. 40, no. 12, pp. 1413–1415, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. M. J. Fedor, “Alternative splicing minireview series: combinatorial control facilitates splicing regulation of gene expression and enhances genome diversity,” Journal of Biological Chemistry, vol. 283, no. 3, pp. 1209–1210, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. D. L. Black, “Protein diversity from alternative splicing: a challenge for bioinformatics and post-genome biology,” Cell, vol. 103, no. 3, pp. 367–370, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. J. Wen and S. Brogna, “Splicing-dependent NMD does not require the EJC in Schizosaccharomyces pombe,” EMBO Journal, vol. 29, no. 9, pp. 1537–1551, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Ogawa, H. Obinata, T. Hattori et al., “Identification and analysis of two splice variants of human G2A generated by alternative splicing,” The Journal of Pharmacology and Experimental Therapeutics, vol. 332, no. 2, pp. 469–478, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. E. T. Wang, R. Sandberg, S. Luo et al., “Alternative isoform regulation in human tissue transcriptomes,” Nature, vol. 456, no. 7221, pp. 470–476, 2008. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Alam, H. T. T. Phan, M. Okazaki et al., “Computational extraction of a neural molecular network through alternative splicing,” BMC Research Notes, vol. 7, no. 1, article 934, 2014. View at Publisher · View at Google Scholar · View at Scopus
  23. B.-B. Xie, D. Li, W.-L. Shi et al., “Deep RNA sequencing reveals a high frequency of alternative splicing events in the fungus Trichoderma longibrachiatum,” BMC Genomics, vol. 16, no. 1, article no. 54, 2015. View at Publisher · View at Google Scholar · View at Scopus
  24. H. J. Lee, B. Wall, and S. Chen, “G-protein-coupled receptors and melanoma,” Pigment Cell & Melanoma Research, vol. 21, no. 4, pp. 415–428, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. D. Markovic and R. A. J. Challiss, “Alternative splicing of G protein-coupled receptors: physiology and pathophysiology,” Cellular and Molecular Life Sciences, vol. 66, no. 20, pp. 3337–3352, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. F. A. Oladosu, W. Maixner, and A. G. Nackley, “Alternative splicing of G protein-coupled receptors: relevance to pain management,” Mayo Clinic Proceedings, vol. 90, no. 8, pp. 1135–1151, 2015. View at Publisher · View at Google Scholar · View at Scopus
  27. J. Vandesompele, K. De Preter, F. Pattyn et al., “Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes,” Genome biology, vol. 3, no. 7, 2002. View at Google Scholar · View at Scopus
  28. Y. Zhang, “I-TASSER server for protein 3D structure prediction,” BMC Bioinformatics, vol. 9, no. 3, article 40, pp. 297–315, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Roy, A. Kucukural, and Y. Zhang, “I-TASSER: a unified platform for automated protein structure and function prediction,” Nature Protocols, vol. 5, no. 4, pp. 725–738, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Roy, J. Yang, and Y. Zhang, “COFACTOR: an accurate comparative algorithm for structure-based protein function annotation,” Nucleic Acids Research, vol. 40, no. 1, pp. W471–W477, 2012. View at Publisher · View at Google Scholar · View at Scopus
  31. B. Webb and A. Sali, “Protein Structure Modeling with MODELLER,” in Protein Structure Prediction, vol. 1137 of Methods in Molecular Biology, pp. 1–15, Springer, New York, NY, USA, 2014. View at Publisher · View at Google Scholar
  32. L. Schrödinger, The PyMOL molecular graphics system, version 1.3 r1, 2010.
  33. Y. Zhang, “Progress and challenges in protein structure prediction,” Current Opinion in Structural Biology, vol. 18, no. 3, pp. 342–348, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. P.-L. Chiu, B. H. Ng, G.-W. Chang, S. Gordon, and H.-H. Lin, “Putative alternative trans-splicing of leukocyte adhesion-GPCR pre-mRNAs generates functional chimeric receptors,” FEBS Letters, vol. 582, no. 5, pp. 792–798, 2008. View at Publisher · View at Google Scholar · View at Scopus
  35. D. Markovic and D. K. Grammatopoulos, “Focus on the splicing of Secretin GPCRs transmembrane-domain 7,” Trends in Biochemical Sciences, vol. 34, no. 9, pp. 443–452, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. D. Markovic, “Alternative mRNA splicing of g protein-coupled receptors,” Methods in Enzymology, vol. 520, pp. 323–335, 2013. View at Publisher · View at Google Scholar · View at Scopus
  37. A. M. Case, I. A. Sawyer, M. Dundr, and M. L. Hastings, “Pre-mRNA splicing: function and dysfunction,” in Encyclopedia of Cell Biology, pp. 503–511, Academic Press, Waltham, Mass, USA, 2016. View at Google Scholar
  38. U. Braunschweig, S. Gueroussov, A. M. Plocik, B. R. Graveley, and B. J. Blencowe, “Dynamic integration of splicing within gene regulatory pathways,” Cell, vol. 152, no. 6, pp. 1252–1269, 2013. View at Publisher · View at Google Scholar · View at Scopus
  39. G. J. Kilpatrick, F. M. Dautzenberg, G. R. Martin, and R. M. Eglen, “7TM receptors: the splicing on the cake,” Trends in Pharmacological Sciences, vol. 20, no. 7, pp. 294–301, 1999. View at Publisher · View at Google Scholar · View at Scopus
  40. W. Gu, T. Zhou, and C. O. Wilke, “A universal trend of reduced mRNA stability near the translation-initiation site in prokaryotes and eukaryotes,” PLoS Computational Biology, vol. 6, no. 2, Article ID e1000664, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. F. M. Hamid and E. V. Makeyev, “Emerging functions of alternative splicing coupled with nonsense-mediated decay,” Biochemical Society Transactions, vol. 42, no. 4, pp. 1168–1173, 2014. View at Publisher · View at Google Scholar · View at Scopus
  42. K. J. Hertel, “Combinatorial control of exon recognition,” Journal of Biological Chemistry, vol. 283, no. 3, pp. 1211–1215, 2008. View at Publisher · View at Google Scholar · View at Scopus
  43. D. C. Di Giammartino, K. Nishida, and J. L. Manley, “Mechanisms and consequences of alternative polyadenylation,” Molecular Cell, vol. 43, no. 6, pp. 853–866, 2011. View at Publisher · View at Google Scholar · View at Scopus
  44. M. B. Warf and J. A. Berglund, “Role of RNA structure in regulating pre-mRNA splicing,” Trends in Biochemical Sciences, vol. 35, no. 3, pp. 169–178, 2010. View at Publisher · View at Google Scholar · View at Scopus
  45. N. L. Barbosa-Morais, M. Irimia, Q. Pan et al., “The evolutionary landscape of alternative splicing in vertebrate species,” Science, vol. 338, no. 6114, pp. 1587–1593, 2012. View at Publisher · View at Google Scholar · View at Scopus
  46. P. A. F. Galante, N. J. Sakabe, N. Kirschbaum-Slager, and S. J. De Souza, “Detection and evaluation of intron retention events in the human transcriptome,” RNA, vol. 10, no. 5, pp. 757–765, 2004. View at Publisher · View at Google Scholar · View at Scopus
  47. U. Braunschweig, N. L. Barbosa-Morais, Q. Pan et al., “Widespread intron retention in mammals functionally tunes transcriptomes,” Genome Research, vol. 24, no. 11, pp. 1774–1786, 2014. View at Publisher · View at Google Scholar · View at Scopus
  48. J. L. Rourke, The Chemerin Receptor GPR1 Signals Through a RhoA/ROCK Pathway and Contributes to Glucose Homeostasis in Obese Mice, Dalhousie University, Halifax, Canada, 2015.
  49. X.-F. Tian, W.-J. Ma, G.-G. Fang, T.-X. Xiao, J. Chen, and J. Zhang, “The effects of experimental mice adipose accumulation by targeting GPR1 pathway,” Progress in Biochemistry and Biophysics, vol. 42, no. 5, pp. 457–467, 2015. View at Publisher · View at Google Scholar · View at Scopus
  50. M. C. Ernst, M. Issa, K. B. Goralski, and C. J. Sinal, “Chemerin exacerbates glucose intolerance in mouse models of obesity and diabetes,” Endocrinology, vol. 151, no. 5, pp. 1998–2007, 2010. View at Publisher · View at Google Scholar · View at Scopus
  51. M. Knobloch, S. M. G. Braun, L. Zurkirchen et al., “Metabolic control of adult neural stem cell activity by Fasn-dependent lipogenesis,” Nature, vol. 493, no. 7431, pp. 226–230, 2013. View at Publisher · View at Google Scholar · View at Scopus
  52. G. E. Atilla-Gokcumen, E. Muro, J. Relat-Goberna et al., “Dividing cells regulate their lipid composition and localization,” Cell, vol. 156, no. 3, pp. 428–439, 2014. View at Publisher · View at Google Scholar · View at Scopus
  53. A. Marchese, R. Cheng, M. C. Lee et al., “Mapping studies of two G-protein-coupled receptor genes: an amino acid difference may confer a functional variation between a human and rodent receptor,” Biochemical and Biophysical Research Communications, vol. 205, no. 3, pp. 1952–1958, 1994. View at Publisher · View at Google Scholar · View at Scopus
  54. K. B. Goralski, T. C. McCarthy, E. A. Hanniman et al., “Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism,” The Journal of Biological Chemistry, vol. 282, no. 38, pp. 28175–28188, 2007. View at Publisher · View at Google Scholar · View at Scopus
  55. R. C. Silva, S. N. Báo, J. L. P. R. Jivago, and C. M. Lucci, “Ultrastructural characterization of porcine oocytes and adjacent follicular cells during follicle development: lipid component evolution,” Theriogenology, vol. 76, no. 9, pp. 1647–1657, 2011. View at Publisher · View at Google Scholar · View at Scopus
  56. Y. Yang, L. Ren, L. Sun et al., “The role of GPR1 signaling in mice corpus luteum,” Journal of Endocrinology, vol. 230, no. 1, pp. 55–65, 2016. View at Publisher · View at Google Scholar