메뉴 건너뛰기




Volumn 63, Issue 1, 2006, Pages 142-152

Molecular cloning of disintegrin-like transcript BA-5A from a Bitis arietans venom gland cDNA library: A putative intermediate in the evolution of the long-chain disintegrin bitistatin

Author keywords

Bitis arietans; cDNA cloning; Disintegrin evolution; Snake venomics; Venom proteome

Indexed keywords

ADAM PROTEIN; BA 5A PROTEIN; BITIS ARIETANS VENOM; BITISTATIN; C TYPE LECTIN LIKE PROTEIN; CYSTATIN; CYSTEINE; DISINTEGRIN; METALLOPROTEINASE; PROTEIN; PROTEOME; SERINE PROTEINASE; UNCLASSIFIED DRUG; VENOM; ZINC METALLOPROTEINASE;

EID: 33745600373     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-005-0268-z     Document Type: Article
Times cited : (47)

References (47)
  • 2
    • 27744533208 scopus 로고    scopus 로고
    • Snake venomics: Comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina
    • Bazaa A, Marrakchi N, El Ayeb M, Sanz L, Calvete JJ (2005) Snake venomics: comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina. Proteomics 5:4223-4235
    • (2005) Proteomics , vol.5 , pp. 4223-4235
    • Bazaa, A.1    Marrakchi, N.2    El Ayeb, M.3    Sanz, L.4    Calvete, J.J.5
  • 3
    • 4344607978 scopus 로고    scopus 로고
    • Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution
    • Bilgrami S, Tomar S, Yadav S, Kaur P, Kumar J, Jabeen T, Sharma S, Sinhg TP (2004) Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution. J Mol Biol 341:829-837
    • (2004) J Mol Biol , vol.341 , pp. 829-837
    • Bilgrami, S.1    Tomar, S.2    Yadav, S.3    Kaur, P.4    Kumar, J.5    Jabeen, T.6    Sharma, S.7    Sinhg, T.P.8
  • 4
    • 23944518374 scopus 로고    scopus 로고
    • Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 Å resolution
    • Bilgrami S, Yadav S, Sharma S, Perbandt M, Betzel C, Singh TP (2005) Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 Å resolution. Biochemistry 44:11058-11066
    • (2005) Biochemistry , vol.44 , pp. 11058-11066
    • Bilgrami, S.1    Yadav, S.2    Sharma, S.3    Perbandt, M.4    Betzel, C.5    Singh, T.P.6
  • 5
    • 14744294145 scopus 로고    scopus 로고
    • Structure-function correlations of snake venom disintegrins
    • Calvete JJ (2005) Structure-function correlations of snake venom disintegrins. Curr Pharm Des 11:829-835
    • (2005) Curr Pharm des , vol.11 , pp. 829-835
    • Calvete, J.J.1
  • 6
    • 0030786687 scopus 로고    scopus 로고
    • The disulfide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bilis arietans
    • Calvete JJ, Schrader M, Raida M, McLane MA, Romero A, Niewiarowski S (1997) The disulfide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bilis arietans. FEBS Lett 416:197-202
    • (1997) FEBS Lett , vol.416 , pp. 197-202
    • Calvete, J.J.1    Schrader, M.2    Raida, M.3    McLane, M.A.4    Romero, A.5    Niewiarowski, S.6
  • 8
    • 0038385565 scopus 로고    scopus 로고
    • Disulfide bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin α5β1 antagonist from Eristocophis macmahoni venom
    • Calvete JJ, Jürgens M, Marcinkiewicz C, Romero A, Schrader M, Niewiarowski S (2000b) Disulfide bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin α5β1 antagonist from Eristocophis macmahoni venom. Biochem J 345:573-581
    • (2000) Biochem J , vol.345 , pp. 573-581
    • Calvete, J.J.1    Jürgens, M.2    Marcinkiewicz, C.3    Romero, A.4    Schrader, M.5    Niewiarowski, S.6
  • 9
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulfide bond engineering
    • Calvete JJ, Moreno-Murciano MP, Theakston RDG, Kisiel DG, Marcinkiewicz C (2003) Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulfide bond engineering. Biochem J 372:725-734
    • (2003) Biochem J , vol.372 , pp. 725-734
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Theakston, R.D.G.3    Kisiel, D.G.4    Marcinkiewicz, C.5
  • 11
  • 12
    • 13044316548 scopus 로고    scopus 로고
    • Developmental shifts and species selection in gastropods
    • USA
    • Duda TF Jr, Palumbi SR (1999) Developmental shifts and species selection in gastropods. Proc Natl Acad Sci USA 96:6820-6823
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6820-6823
    • Duda Jr., T.F.1    Palumbi, S.R.2
  • 13
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox JW, Serrano SMT (2005) Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 45:969-985
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.T.2
  • 14
    • 15544369378 scopus 로고    scopus 로고
    • From genome to "venome": Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • Fry BG (2005) From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res 15:403-420
    • (2005) Genome Res , vol.15 , pp. 403-420
    • Fry, B.G.1
  • 15
    • 1942533494 scopus 로고    scopus 로고
    • Assembling an arsenal: Origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences
    • Fry BG, Wüster W (2004) Assembling an arsenal: origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences. Mol Biol Evol 21:870-883
    • (2004) Mol Biol Evol , vol.21 , pp. 870-883
    • Fry, B.G.1    Wüster, W.2
  • 17
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the Metzincin clan of metalloendopeptidases
    • Gomis-Rüth FX (2003) Structural aspects of the Metzincin clan of metalloendopeptidases. Mol Biotechnol 24:157-202
    • (2003) Mol Biotechnol , vol.24 , pp. 157-202
    • Gomis-Rüth, F.X.1
  • 18
    • 0141594743 scopus 로고    scopus 로고
    • Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species
    • Harrison RA, Oliver J, Hasson SS, Bharati K, Theakston RDG (2003) Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species. Gene 315:95-102
    • (2003) Gene , vol.315 , pp. 95-102
    • Harrison, R.A.1    Oliver, J.2    Hasson, S.S.3    Bharati, K.4    Theakston, R.D.G.5
  • 19
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists
    • Jia L-G, Wang X-M, Shannon JD, Bjarnason JB, Fox JW (1997) Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists. J Biol Chem 272:13094-13102
    • (1997) J Biol Chem , vol.272 , pp. 13094-13102
    • Jia, L.-G.1    Wang, X.-M.2    Shannon, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 20
    • 1242316947 scopus 로고    scopus 로고
    • Snake venomics: Characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and tandem mass spectrometry analysis
    • Juárez P, Sanz L, Calvete JJ (2004) Snake venomics: characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and tandem mass spectrometry analysis. Proteomics 4:327-338
    • (2004) Proteomics , vol.4 , pp. 327-338
    • Juárez, P.1    Sanz, L.2    Calvete, J.J.3
  • 21
    • 33745601887 scopus 로고    scopus 로고
    • Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin
    • Companion paper DOI: 10.1007/s00239-005-0269-y
    • Juárez P, Wagstaff SC, Sanz L, Harrison RA, Calvete JJ (2006) Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin. J Mol Evol. Companion paper DOI: 10.1007/s00239-005-0269-y
    • (2006) J Mol Evol
    • Juárez, P.1    Wagstaff, S.C.2    Sanz, L.3    Harrison, R.A.4    Calvete, J.J.5
  • 22
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • Kini R, Evans HJ (1992) Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon 30:265-293
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.1    Evans, H.J.2
  • 23
    • 0038770146 scopus 로고    scopus 로고
    • Functional diversification of animal toxins by adaptative evolution
    • Ménez A (ed) John Wiley & Sons, Chichester, UK
    • Kordis D, Krizaj I, Gubensek F (2002) Functional diversification of animal toxins by adaptative evolution. In: Ménez A (ed) Perspectives in molecular toxinology. John Wiley & Sons, Chichester, UK, pp 401-419
    • (2002) Perspectives in Molecular Toxinology , pp. 401-419
    • Kordis, D.1    Krizaj, I.2    Gubensek, F.3
  • 24
    • 0036139211 scopus 로고    scopus 로고
    • Mega2: Molecular Evolutionary Genetics Analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M (2001) Mega2: Molecular Evolutionary Genetics Analysis software. Bioinformatics 17:1244-1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 25
    • 19544368798 scopus 로고    scopus 로고
    • Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on hemostasis
    • Lu Q, Navdaev A, Clemetson JM, Clemetson KJ (2005a) Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on hemostasis. Toxicon 45:1089-1098
    • (2005) Toxicon , vol.45 , pp. 1089-1098
    • Lu, Q.1    Navdaev, A.2    Clemetson, J.M.3    Clemetson, K.J.4
  • 26
    • 22144440164 scopus 로고    scopus 로고
    • Snake venom metalloproteinase containing a disintegrin-like domain, its structure-activity relationships at interacting with integrins
    • Lu X, Lu D, Scully MF, Kakkar VV (2005b) Snake venom metalloproteinase containing a disintegrin-like domain, its structure-activity relationships at interacting with integrins. Curr Med Chem Cardiovasc Hematol Agents 3:249-260
    • (2005) Curr Med Chem Cardiovasc Hematol Agents , vol.3 , pp. 249-260
    • Lu, X.1    Lu, D.2    Scully, M.F.3    Kakkar, V.V.4
  • 27
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland FS (1998) Snake venoms and the hemostatic system. Toxicon 36:1749-1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 29
    • 17144392170 scopus 로고    scopus 로고
    • Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR
    • Monleón D, Esteve V, Kovacs H, Calvete JJ, Celda B (2005) Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR. Biochem J 387:57-66
    • (2005) Biochem J , vol.387 , pp. 57-66
    • Monleón, D.1    Esteve, V.2    Kovacs, H.3    Calvete, J.J.4    Celda, B.5
  • 31
    • 0029814973 scopus 로고    scopus 로고
    • Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: Gene duplication and divergence of a common ancestor rather than convergent evolution
    • Moura da Silva AM, Theakston RDG, Crampton JM (1996) Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution. J Mol Evol 43:263-269
    • (1996) J Mol Evol , vol.43 , pp. 263-269
    • Moura Da Silva, A.M.1    Theakston, R.D.G.2    Crampton, J.M.3
  • 32
    • 0035870095 scopus 로고    scopus 로고
    • Selective recognition of α2β1 integrin by jararhagin, a metalloproteinase/disintegrin from Bothrops jararaca venom
    • Moura da Silva AM, Marcinkiewicz C, Marcinkiewicz M, Niewiarowski S (2001) Selective recognition of α2β1 integrin by jararhagin, a metalloproteinase/disintegrin from Bothrops jararaca venom. Thromb Res 102:153-159
    • (2001) Thromb Res , vol.102 , pp. 153-159
    • Moura Da Silva, A.M.1    Marcinkiewicz, C.2    Marcinkiewicz, M.3    Niewiarowski, S.4
  • 33
    • 0034213348 scopus 로고    scopus 로고
    • Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
    • Nikai T, Taniguchi K, Komori Y, Masuda K, Fox JW, Sugihara H (2000) Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch Biochem Biophys 378:6-15
    • (2000) Arch Biochem Biophys , vol.378 , pp. 6-15
    • Nikai, T.1    Taniguchi, K.2    Komori, Y.3    Masuda, K.4    Fox, J.W.5    Sugihara, H.6
  • 34
    • 0242265472 scopus 로고    scopus 로고
    • Accelerated and regional evolution of snake venom gland isozymes
    • Ménez A (ed) John Wiley & Sons, Chichester, UK
    • Ohno M, Ogawa T, Oda-Ueda N, Chijiwa T, Hattori S (2002) Accelerated and regional evolution of snake venom gland isozymes. In: Ménez A (ed) Perspectives in molecular toxinology. John Wiley & Sons, Chichester, UK, pp 387-401
    • (2002) Perspectives in Molecular Toxinology , pp. 387-401
    • Ohno, M.1    Ogawa, T.2    Oda-Ueda, N.3    Chijiwa, T.4    Hattori, S.5
  • 35
    • 0035049724 scopus 로고    scopus 로고
    • Comparative biochemistry of disintegrins isolated from snake venoms: Consideration of the taxonomy and geographical distribution of snakes in the genus Echis
    • Okuda D, Nozaki C, Sekiya F, Morita T (2001) Comparative biochemistry of disintegrins isolated from snake venoms: consideration of the taxonomy and geographical distribution of snakes in the genus Echis. J Biochem 129:615-620
    • (2001) J Biochem , vol.129 , pp. 615-620
    • Okuda, D.1    Nozaki, C.2    Sekiya, F.3    Morita, T.4
  • 36
    • 0037016015 scopus 로고    scopus 로고
    • A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region
    • Okuda D, Koike H, Morita T (2002) A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region. Biochemistry 41:14248-14254
    • (2002) Biochemistry , vol.41 , pp. 14248-14254
    • Okuda, D.1    Koike, H.2    Morita, T.3
  • 37
    • 0026495409 scopus 로고
    • Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family
    • Paine MJ, Desmond HP, Theakston RD, Crampton JM (1992) Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. J Biol Chem 267:22869-22876
    • (1992) J Biol Chem , vol.267 , pp. 22869-22876
    • Paine, M.J.1    Desmond, H.P.2    Theakston, R.D.3    Crampton, J.M.4
  • 38
    • 0032585108 scopus 로고    scopus 로고
    • Cloning and characterization of novel disintegrins from Agkistrodon halys venom
    • Park D, Kang I, Kim H, Chung K, Kim DS, Yun Y (1998) Cloning and characterization of novel disintegrins from Agkistrodon halys venom. Mol Cells 8:578-584
    • (1998) Mol Cells , vol.8 , pp. 578-584
    • Park, D.1    Kang, I.2    Kim, H.3    Chung, K.4    Kim, D.S.5    Yun, Y.6
  • 39
    • 0024852988 scopus 로고
    • Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans
    • Shebuski RJ, Ramjit DR, Bencen GH, Polokoff MA (1989) Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine- aspartic acid-containing peptide from the venom of the viper Bitis arietans. J Biol Chem 264:21550-21556
    • (1989) J Biol Chem , vol.264 , pp. 21550-21556
    • Shebuski, R.J.1    Ramjit, D.R.2    Bencen, G.H.3    Polokoff, M.A.4
  • 40
    • 0031195282 scopus 로고    scopus 로고
    • Sequence and biological activity of catrocollastatin-C: A disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom
    • Shimokawa K-I, Shannon JD, Jia L-G, Fox JW (1997) Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom. Arch Biochem Biophys 343:35-43
    • (1997) Arch Biochem Biophys , vol.343 , pp. 35-43
    • Shimokawa, K.-I.1    Shannon, J.D.2    Jia, L.-G.3    Fox, J.W.4
  • 41
    • 33645789298 scopus 로고    scopus 로고
    • Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries. Insight into the evolution of the snake venom's integrin inhibition system
    • Sanz L, Bazaa A, Marrakchi N, Pérez A, Chenik M, Bel Lasfer Z, El Ayeb M, Calvete JJ (2006) Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries. Insight into the evolution of the snake venom's integrin inhibition system. Biochem J 395:385-392
    • (2006) Biochem J , vol.395 , pp. 385-392
    • Sanz, L.1    Bazaa, A.2    Marrakchi, N.3    Pérez, A.4    Chenik, M.5    Bel Lasfer, Z.6    El Ayeb, M.7    Calvete, J.J.8
  • 44
    • 0034053413 scopus 로고    scopus 로고
    • Purification, cloning and sequence analyses for pro-metalloprotease- disintegrin variants from Deinagkistrodon acutus venom and subclassification of the small venom metalloproteases
    • Tsai IH, Wang YM, Chiang TY, Chen YL, Huang RJ (2000) Purification, cloning and sequence analyses for pro-metalloprotease-disintegrin variants from Deinagkistrodon acutus venom and subclassification of the small venom metalloproteases. Eur J Biochem 267:1359-1367
    • (2000) Eur J Biochem , vol.267 , pp. 1359-1367
    • Tsai, I.H.1    Wang, Y.M.2    Chiang, T.Y.3    Chen, Y.L.4    Huang, R.J.5
  • 45
    • 4644310821 scopus 로고    scopus 로고
    • Comparative proteomics and subtyping of venom phospholipases A2 and disintegrins of Protobothrops pit vipers
    • Tsai I-H, Chen Y-H, Wang Y-M (2004) Comparative proteomics and subtyping of venom phospholipases A2 and disintegrins of Protobothrops pit vipers. Biochim Biophys Acta 1702:111-119
    • (2004) Biochim Biophys Acta , vol.1702 , pp. 111-119
    • Tsai, I.-H.1    Chen, Y.-H.2    Wang, Y.-M.3
  • 46
    • 0029105096 scopus 로고
    • Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen
    • Zhou Q, Smith JB, Grossman MH (1995) Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem J 307:411-417
    • (1995) Biochem J , vol.307 , pp. 411-417
    • Zhou, Q.1    Smith, J.B.2    Grossman, M.H.3
  • 47
    • 0037174925 scopus 로고    scopus 로고
    • The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling
    • Zigrino P, Kamiguti AS, Eble J, Drescher C, Nischt R, Fox JW, Mauch C (2002) The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling. J Biol Chem 277:40528-40535
    • (2002) J Biol Chem , vol.277 , pp. 40528-40535
    • Zigrino, P.1    Kamiguti, A.S.2    Eble, J.3    Drescher, C.4    Nischt, R.5    Fox, J.W.6    Mauch, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.