論文

査読有り 国際誌
2016年1月1日

Two zebrafish G2A homologs activate multiple intracellular signaling pathways in acidic environment.

Biochemical and biophysical research communications
  • Yuta Ichijo
  • Yuta Mochimaru
  • Morio Azuma
  • Kazuhiro Satou
  • Jun Negishi
  • Takashi Nakakura
  • Natsuki Oshima
  • Chihiro Mogi
  • Koichi Sato
  • Kouhei Matsuda
  • Fumikazu Okajima
  • Hideaki Tomura
  • 全て表示

469
1
開始ページ
81
終了ページ
86
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbrc.2015.11.075

Human G2A is activated by various stimuli such as lysophosphatidylcholine (LPC), 9-hydroxyoctadecadienoic acid (9-HODE), and protons. The receptor is coupled to multiple intracellular signaling pathways, including the Gs-protein/cAMP/CRE, G12/13-protein/Rho/SRE, and Gq-protein/phospholipase C/NFAT pathways. In the present study, we examined whether zebrafish G2A homologs (zG2A-a and zG2A-b) could respond to these stimuli and activate multiple intracellular signaling pathways. We also examined whether histidine residue and basic amino acid residue in the N-terminus of the homologs also play roles similar to those played by human G2A residues if the homologs sense protons. We found that the zG2A-a showed the high CRE, SRE, and NFAT activities, however, zG2A-b showed only the high SRE activity under a pH of 8.0. Extracellular acidification from pH 7.4 to 6.3 ameliorated these activities in zG2A-a-expressing cells. On the other hand, acidification ameliorated the SRE activity but not the CRE and NFAT activities in zG2A-b-expressing cells. LPC or 9-HODE did not modify any activity of either homolog. The substitution of histidine residue at the 174(th) position from the N-terminus of zG2A-a to asparagine residue attenuated proton-induced CRE and NFAT activities but not SRE activity. The substitution of arginine residue at the 32nd position from the N-terminus of zG2A-a to the alanine residue also attenuated its high and the proton-induced CRE and NFAT activities. On the contrary, the substitution did not attenuate SRE activity. The substitution of the arginine residue at the 10th position from the N-terminus of zG2A-b to the alanine residue also did not attenuate its high or the proton-induced SRE activity. These results indicate that zebrafish G2A homologs were activated by protons but not by LPC and 9-HODE, and the activation mechanisms of the homologs were similar to those of human G2A.

リンク情報
DOI
https://doi.org/10.1016/j.bbrc.2015.11.075
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26614909
ID情報
  • DOI : 10.1016/j.bbrc.2015.11.075
  • PubMed ID : 26614909

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