생명과학회지 (Journal of Life Science)

  • 제8권3호
  • /
  • Pages.235-240
  • /
  • 1998
  • /
  • 1225-9918(pISSN)
  • /
  • 2287-3406(eISSN)
한국생명과학회 (Korean Society of Life Science)
권호 표지

두툽상어 matrix metalloproteinase 유전자 cDNA의 클로닝

Cloning of a matrix metalloproteinase cDNA from Scylliorhinus torazame

  • 김종원 (부산대학교 자연과학대학 분자생물학과) ;
  • 조원진 (부산대학교 자연과학대학 분자생물학과) ;
  • 천광호 (부산대학교 자연과학대학 분자생물학과) ;
  • 김규원 (부산대학교 자연과학대학 분자생물학과) ;
  • 김영진 (부산대학교 자연과학대학 분자생물학과) ;
  • 이상준 (국립수산진흥원 생물공학과) ;
  • 신혜자 (동서대학교 환경공학과) ;
  • 임운기 (부산대학교 자연과학대학 분자생물학과)
  • 발행 : 1998.06.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Matrix metalloproteinases(MMP)는 배발생 및 재조직화 등의 정상적인 생체형성과 관절염, 암전이, 치근막염, 골조송증 등의 질병과정에서 collagen이나 proteoglycan과 같은 세포외기질의 구성성분을 분해하는 아연(zinc)효소군이다. 지금까지 다양한 종에서 mmp의 유전자가 클로닝되고 그 기능이 연구되어 왔지만 아직 어류에서는 연구결과가 보고된 바가 없다. 본 연구에서는 한국의 부산연안에 많은 연골어유 투툽상어(Scylliorhinus toraxzame)로부터 RT-PCR(reverse transcriptase dependent polymerase chain reaction)의방법으로 mmp cDNA의 일부를 클로닝하였다. 이것은 염기서열에서 인간, 쥐 및 닭의 membrane type matrix matalloproteinase-3(mt3-mmps)의 염기서열과 74% 동일성을 보이며, 아미노산서열에서는 90%이상의 동일성을 갖고 있다. 또한 MMP에 나타나는 cysteine switch domain, zinc binding domain(HExGH motif), propeptide cleavage site, and RRKR motif등을 가지고 있다. 이러한 결과로부터 본 연구에서 클로닝된 RT-PCR단편은 두툽상어의 mt3-mmp 또는 이와 유사한 유전자의 cDNA이라 믿어진다.

Matrix metalloproteinases(MMPs) are a group of zinc enzymes responsible for degradation of the matrix components such as collagen and proteoglycans in normal embryogenesis and remodeling and in many disease processes such as arthritis, cancer, periodontitis, and osteprocess. Genetically distince MMPs have been characterized and their genes have been cloned thus far from a variaty of species but not from fishes. In this stydy, a mmp cDNA was cloned by using RT-PCR(reverse transcriptase dependent polymerase chain reaction) from Scylliorhinus toraxzame(shark), agroup of cartilaginous fish, abundant in the coast of Pusan, Korea. It has 74% base homologue with membrane type matrix matalloproteinase-3 genes(mt3-mmps) from human, rat and chick, and also shows more than 90% residue homologue with them. In addition, it has cysteine switch domain, zinc binding domain(HExGH motif), propeptide cleavage site, and RRKR motif, which are present in MMPs. This result indicates that cDNA fragment cloned here may be mt3-mmp or its analogous gejne cDNA fragment of Scylliorhinus torzame.

키워드

참고문헌

  1. J. Biol. Chem. v.272 Expression of three membrane-Type matrix metalloproteinases(MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain Shofuda, K.;Yasumitsu, H.;Nishihashi, A.;Miki, K.;Miyazaki, K.
  2. J. Biol. Chem. v.271 Cloning and developmental expression of a membrane type-matrix metalloproteinase from chicken Yang, M.;Hayashi, K.;Hayashi, M.;Fujii, J. T.;Kurkinen, M.
  3. Biochem. Biophys.Acta v.948 Membrane and matrix localization of proteinases : a common theme in tumor cell invasion and angiogenesis Moscatelli, D.;Rifkin, D. B.
  4. FASEB J. v.5 Matrix metalloproteinases and their inhibitors in connective tissue remodeling f Woessner, J. F. Jr.
  5. Cell. Mol. Biol. v.36 Matrix metalloproteinases Emonard, H.;Grim, J.-A.
  6. J. Oral. Pathol. v.17 From tadpole collagenase to a family of matrix metalloproteinase Birkedal-Hansen, H.
  7. Ann. Rheum. Dis. v.49 The tissue metalloproteinase family and the inhibitor TIMP : a study using cDNAs and recombinant proteins Docherty, A. J. P.;Murphy, G.
  8. Triends Genet. v.6 Metalloproteinases and their inhibitors in matrix remodeling Matrisian, L. M.
  9. Collagen : molecular biology v.Ⅳ Molecular biology of collagen degradation Frisch, S. M.;Werb, Z.;Olsen, B. R.(ed.);Mimni, M. E.(ed.)
  10. Textbook o Rheumtology(3rd, ed.) Proteinases and matrix degradation Werb. Z.;Kelly, W. N.(ed.);Harris, E. D. Jr.(ed.);Ruddy, S.(ed.);Sledge(ed.)
  11. Proteinase Inhibitors Serpins : the super-family of plasa serine proteinase inhibitors Carrel, R. W.;Bosewll, D. R.;Barrett, A. J.(ed.);Salvesen, G.(ed.)
  12. Proteinase Inhibitros Protein inhibitors of metalloproteinases Cawston, T. E.;Barrett A. J.(ed.);Salvesen, G.(ed.)
  13. Biochemistry v.29 Zinc coordination, function, and structure of zinc enzymes and other proteins Valee, B. L.;Auld, D.S.
  14. Proc. Natl. Acad. Sci. v.87 Multiple modes of activation of latent human fibroblast collagenase : evidence for the role of a Cys73 active site zinc complex in latency and a cysteine switch mechanism for activation Springman, E. B.;Angleton, E. L.;Birkedal-Hansen, H.;Van Wart, H. E.
  15. New Engl. J. Med. v.320 Tissue destruction by neutrophils Weise, S. J.
  16. Biochemistry v.29 The mechanism of activation of tissue procollagenase by matrix metalloproteinase-3(stromelysin) Suzuki, K.;Enghild, J. J.;Morodomi, T.;Salvesen, G.;Nagase, H.
  17. Anal. Biochem. v.161 Singlee-step mehod of RNA isolation by acid guanidium thiocyanate-phenol-chlorofrom extraction Chomczynski, P.;Sacchi, N.
  18. Methods in Enzymology v.218 Rapid amplification of complementary DNa ends for generation of full-length complementary DNAs : thermal RACE Frohman, M. A.
  19. Current Opinion in Biotechnology v.6 Novel methods for cloning and engineerings genes using the polymerase chain raction Rashtchian, A.
  20. Gene v.155 Random rapid amplification of cDNA ends(RRACE) allows for cloning of multiple novel human cDNA fragements containing(GAG)n repeats Garney, J. P.;McKnight, C.;Van Epps, S.;Kelly, M. R.