Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Structure and Arterial Relaxing Activity of Substance P-related Peptides and Substance P analogs

Substance P-related peptide들과 유도체의 구조 및 혈관이완 활성

  • KIM Eun Jung (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • KIM Chan-Hee (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • GO Hye-Jin (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • KIM In Hae (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • AN Sang Hyun (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • SOHN Hee-Young (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • PARK Hee Yeon (Biotechnology Research, National Fisheries Research & Development Institute) ;
  • YOON Ho Dong (Biotechnology Research, National Fisheries Research & Development Institute) ;
  • CHANG Young-Chae (Department of Pathology, School of Medicine, Catholic University of Daegu) ;
  • HONG Yong-Ki (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • PARK Nam Gyu (Department of Biotechnology and Bioengineering, Faculty of Food Science and Biotechnology, Pukyong National University)
  • 김은정 (부경대학교 수산과학대학 생물공학과) ;
  • 김찬희 (부경대학교 수산과학대학 생물공학과) ;
  • 고혜진 (부경대학교 수산과학대학 생물공학과) ;
  • 김인혜 (부경대학교 수산과학대학 생물공학과) ;
  • 안상현 (부경대학교 수산과학대학 생물공학과) ;
  • 손희영 (부경대학교 수산과학대학 생물공학과) ;
  • 박희연 (국립수산과학원 생명공학연구단) ;
  • 윤호동 (국립수산과학원 생명공학연구단) ;
  • 장영채 (대구가톨릭대학교 의과대학) ;
  • 홍용기 (부경대학교 수산과학대학 생물공학과) ;
  • 박남규 (부경대학교 수산과학대학 생물공학과)
  • Published : 2005.06.01
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Abstract

Relationship between structure and biological activity was performed using the five substance P-related peptides (SPRPs) [mammalian-SP (M-SP), cod-SP (C-SP), trout-SP (T-SP), lungfish-SP (L-SP) and Ranakinin] and four SP analogs [[$His^5$]-SP (5H-SP), [$Gly^5$]-SP (5G-SP), ($Ile^8$)-SP (8I-SP) and ($Trp^8$)-Ranakinin (8W-Ranakinin)]. The circular dichroism (CD) spectra showed that all of the peptides took an unordered structure in buffer solution and artificial liposomes. However, 8W-Ranakinin undergoes conformational changes by being transferred into neutral and acidic liposomes from an unordered structure to more ordered structure. The arterial relaxing effect of the peptides was also studied with guinea-pig aorta (GPA), As a result of the studies, L-SP was about 14-fold more potant than M-SP. The order of potency compared to $EC_{50}$ value was $L-SP{\gg}M-SP>5G-SP{\ge}8I-SP>5H-SP>T-SP$, C-SP, Ranakinin, 8W-Ranakinin.

Keywords

References

  1. Auge, S., B. Bersch, M. Tropis and A. Milon. 2000. Characterization of substance P-membrane interaction by transferred nuclear overhauser effect. Biopolymers, 54, 297-306 https://doi.org/10.1002/1097-0282(20001015)54:5<297::AID-BIP10>3.0.CO;2-9
  2. Chang, M.M., S.E. Leeman and H.D. Niall. 1971. Aminoacid sequence of substance P. Nat. New Biol., 232, 86-87
  3. Comis, A. and E. Burcher. 1999. Structure activity studies at the rat tachykinin NK2 receptor: effect of substitution at position 5 of neurokinin A. J. Pepet. Res., 53, 337-342 https://doi.org/10.1034/j.1399-3011.1999.00038.x
  4. Helke, C.J., J.E. Kraause, P.W. Mantyh, R. Couture and M.J. Bannon. 1990. Diversity in mammalian tachykinin peptidergic neurons: multiple peptides, receptor and regulatory mechanisms. FASEB J., 4, 1606-1615 https://doi.org/10.1096/fasebj.4.6.1969374
  5. Jensen, J. and J. M. Conlon. 1992. Substance P-related and neurokinin-A-related peptides from the brain of the cod and trout. Eur. J. Biochem., 206, 659-664 https://doi.org/10.1111/j.1432-1033.1992.tb16971.x
  6. Keire, D.A. and T.G. Fletcher. 1996. The conformation of substance P in lipid environments. Biophys. J., 70, 1716-1727 https://doi.org/10.1016/S0006-3495(96)79734-5
  7. Liu, L., J.M. Conlon, J.M.P. Joss and E. Burcher. 2002. Purification, characterization, and biological activity of a substance P-related peptide from the gut of the Australian lungfish, Neoceratodus forsteri. Gen. Comp. Endocrinol., 125, 104-112 https://doi.org/10.1006/gcen.2001.7732
  8. O'Harte, F., E. Burcher, S. Lovas, D.D. Smith, H. Vaudry and J.M. Conlon. 1991. Ranakinin: a novel NK1 tachykinin receptor agonist isolated with neurokinin B from the brain of the frog Rana ridibunda. J. Neurochem., 57, 2086-2091 https://doi.org/10.1111/j.1471-4159.1991.tb06426.x
  9. Otsuka, M. and K. Yoshioka. 1993. Neurotransmitter functions of mammalian tachykinins. Physiol. Rev., 73, 229-308 https://doi.org/10.1152/physrev.1993.73.2.229
  10. Patacchini, R. and C.A. Maggi. 1995. Tachykinin receptors and receptor subtypes. Arch. Int. Pharmacodyn., 329, 161-184
  11. Park, N.G., J.K. Seo, H.J. Ku, S. Lee, G. Sugihara, K.H. Kim, J.S. Park and S.W. Kang. 1997. Conformation and biological activity of mastoparan B and its analogs I. Bull. Kor. Chem. Soc., 18, 50-56
  12. Rouissi, N., A. Claing, M. Nicolau, D. Jukic, P. D'Orleans-Juste and D. Regoli, 1993. Substance P (NK1-receptor) antagonists: in vivo and in vitro activities in rats and guinea-pigs. Life Sci., 52, 1141-1147 https://doi.org/10.1016/0024-3205(93)90436-7
  13. Saito, R., H. Konishi, Y. Takano, S. Nonaka, K. Sakaguchi, Y. Shimohigashi and H. Kamiya. 1990. Characterization of tachykinin receptors in endothelial cells of porcine artery. Neurosci. Lett., 110, 337-342 https://doi.org/10.1016/0304-3940(90)90870-F
  14. Schwyzer, R. 1987. Membrane-assisted molecular mechanism of neurokinin receptor subtype selection. EMBO J., 6, 2255-2259
  15. von Euler, U.S. and J.H. Gaddum. 1931. An unidentified depressor substance in certain tissue extracts. J. Physiol., 72, 74-87 https://doi.org/10.1113/jphysiol.1931.sp002763