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Volumn 577, Issue 3, 2004, Pages 478-482

Structural determinants of the selectivity of KTS-disintegrins for the α1β1 integrin

Author keywords

BSA, bovine serum albumin; CMFDA, 5 chloromethylfluorescein diacetate; HPLC, high performance liquid chromatography; MALDI TOF, matrix assisted laser desorption ionization time of flight mass spectrometry; TFA, trifluoroacetic acid

Indexed keywords

ARGININE; COLLAGEN TYPE 4; CORE PROTEIN; DISINTEGRIN; ECHISTATIN; LEUCINE; MONOMER; OBTUSTATIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 1; VIPERISTATIN;

EID: 8844224111     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.10.050     Document Type: Article
Times cited : (62)

References (33)
  • 1
    • 0028979497 scopus 로고
    • The alpha 2 beta 1 integrin: A collagen receptor on platelets and other cells
    • Santoro S.A., Zutter M.M. The alpha 2 beta 1 integrin: a collagen receptor on platelets and other cells. Thromb. Haemost. 74:1995;813-821
    • (1995) Thromb. Haemost. , vol.74 , pp. 813-821
    • Santoro, S.A.1    Zutter, M.M.2
  • 2
    • 0036734093 scopus 로고    scopus 로고
    • A reevaluation of integrins as regulators of angiogenesis
    • Hynes R.O. A reevaluation of integrins as regulators of angiogenesis. Nat. Med. 8:2002;918-921
    • (2002) Nat. Med. , vol.8 , pp. 918-921
    • Hynes, R.O.1
  • 3
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson S.K., Santoro S.A. Ligand recognition by the I domain-containing integrins. Cell Mol. Life Sci. 54:1998;556-566
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 4
    • 0033402950 scopus 로고    scopus 로고
    • Integrin I domains and their function
    • Leitinger B., Hogg N. Integrin I domains and their function. Biochem. Soc. Transact. 27:1999;826-832
    • (1999) Biochem. Soc. Transact. , vol.27 , pp. 826-832
    • Leitinger, B.1    Hogg, N.2
  • 5
    • 0031459892 scopus 로고    scopus 로고
    • Angiogenesis promoted by vascular endothelial growth factor: Regulation through alpha1beta1 and alpha2beta1 integrins
    • Senger D.R., Claffey K.P., Benes J.E., Perruzzi C.A., Sergiou A.P., Detmar M. Angiogenesis promoted by vascular endothelial growth factor: regulation through alpha1beta1 and alpha2beta1 integrins. Proc. Natl. Acad. Sci. USA. 94:1997;13612-13617
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13612-13617
    • Senger, D.R.1    Claffey, K.P.2    Benes, J.E.3    Perruzzi, C.A.4    Sergiou, A.P.5    Detmar, M.6
  • 6
    • 0036142782 scopus 로고    scopus 로고
    • The alpha(1)beta(1) and alpha(2)beta(1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis
    • Senger D.R., Perruzzi C.A., Streit M., Koteliansky V.E., de Fougerolles A.R., Detmar M. The alpha(1)beta(1) and alpha(2)beta(1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis. Am. J. Pathol. 160:2002;195-204
    • (2002) Am. J. Pathol. , vol.160 , pp. 195-204
    • Senger, D.R.1    Perruzzi, C.A.2    Streit, M.3    Koteliansky, V.E.4    De Fougerolles, A.R.5    Detmar, M.6
  • 8
    • 0034007381 scopus 로고    scopus 로고
    • Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization
    • Pozzi A., Moberg P.E., Miles L.A., Wagner S., Soloway P., Gardner H.A. Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization. Proc. Natl. Acad. Sci. USA. 97:2000;2202-2207
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2202-2207
    • Pozzi, A.1    Moberg, P.E.2    Miles, L.A.3    Wagner, S.4    Soloway, P.5    Gardner, H.A.6
  • 9
    • 0035984171 scopus 로고    scopus 로고
    • Lessons from the alpha2 integrin knockout mouse
    • Mercurio A.M. Lessons from the alpha2 integrin knockout mouse. Am. J. Pathol. 161:2002;3-6
    • (2002) Am. J. Pathol. , vol.161 , pp. 3-6
    • Mercurio, A.M.1
  • 11
    • 0034849664 scopus 로고    scopus 로고
    • Mammary epithelial cell-cycle progression via the alpha(2)beta(1) integrin: Unique and synergistic roles of the alpha(2) cytoplasmic domain
    • Klekotka P.A., Santoro S.A., Ho A., Dowdy S.F., Zutter M. Mammary epithelial cell-cycle progression via the alpha(2)beta(1) integrin: unique and synergistic roles of the alpha(2) cytoplasmic domain. Am. J. Pathol. 159:2001;983-992
    • (2001) Am. J. Pathol. , vol.159 , pp. 983-992
    • Klekotka, P.A.1    Santoro, S.A.2    Ho, A.3    Dowdy, S.F.4    Zutter, M.5
  • 12
    • 0037301510 scopus 로고    scopus 로고
    • Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa
    • Moreno-Murciano P., Daniel Monleón D., Calvete J.J., Celda B., Marcinkiewicz C. Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa. Protein Sci. 12:2003;366-371
    • (2003) Protein Sci. , vol.12 , pp. 366-371
    • Moreno-Murciano, P.1    Daniel Monleón, D.2    Calvete, J.J.3    Celda, B.4    Marcinkiewicz, C.5
  • 14
    • 0033535986 scopus 로고    scopus 로고
    • Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): Synergistic and noncovalent interaction between its subunits
    • Wang R., Kini R.M., Chung M.C.M. Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits. Biochemistry. 38:1999;7584-7595
    • (1999) Biochemistry , vol.38 , pp. 7584-7595
    • Wang, R.1    Kini, R.M.2    Chung, M.C.M.3
  • 15
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski S., McLane M.A., Kloczewiak M., Stewart G.J. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol. 31:1994;289-300
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 18
    • 0032884927 scopus 로고    scopus 로고
    • Structural and functional characterization of EMF10, a heterodimeric disintegrin from Eristocophis macmahoni venom that selectively inhibits alpha 5 beta 1 integrin
    • Marcinkiewicz C., Calvete J.J., Senadhi V.K., Marcinkiewicz M.M., Raida M., Schick P., Lobb R.R., Niewiarowski S. Structural and functional characterization of EMF10, a heterodimeric disintegrin from Eristocophis macmahoni venom that selectively inhibits alpha 5 beta 1 integrin. Biochemistry. 38:1999;13302-13309
    • (1999) Biochemistry , vol.38 , pp. 13302-13309
    • Marcinkiewicz, C.1    Calvete, J.J.2    Senadhi, V.K.3    Marcinkiewicz, M.M.4    Raida, M.5    Schick, P.6    Lobb, R.R.7    Niewiarowski, S.8
  • 19
    • 0037065736 scopus 로고    scopus 로고
    • The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3, and alpha5beta1 integrin
    • Calvete J.J., Fox J.W., Agelan A., Niewiarowski S., Marcinkiewicz C. The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3, and alpha5beta1 integrin. Biochemistry. 41:2002;2014-2021
    • (2002) Biochemistry , vol.41 , pp. 2014-2021
    • Calvete, J.J.1    Fox, J.W.2    Agelan, A.3    Niewiarowski, S.4    Marcinkiewicz, C.5
  • 21
    • 1042265198 scopus 로고    scopus 로고
    • Structural requirements of MLD-containing disintegrins for functional interaction with alpha 4 beta 1 and alpha 9 beta1 integrins
    • Bazan-Socha S., Kisiel D.G., Young B.R., Theakston R.D.G., Calvete J.J., Sheppard D., Marcinkiewicz C. Structural requirements of MLD-containing disintegrins for functional interaction with alpha 4 beta 1 and alpha 9 beta1 integrins. Biochemistry. 43:2004;1639-1647
    • (2004) Biochemistry , vol.43 , pp. 1639-1647
    • Bazan-Socha, S.1    Kisiel, D.G.2    Young, B.R.3    Theakston, R.D.G.4    Calvete, J.J.5    Sheppard, D.6    Marcinkiewicz, C.7
  • 23
    • 0025519981 scopus 로고
    • Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor
    • O'Toole T.E., Loftus J.C., Du X., Glass A., Ruggeri Z.M., Shattil S.J., Plow E.F., Ginsberg M.H. Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor. Cell Regul. 1:1990;883-893
    • (1990) Cell Regul. , vol.1 , pp. 883-893
    • O'Toole, T.E.1    Loftus, J.C.2    Du, X.3    Glass, A.4    Ruggeri, Z.M.5    Shattil, S.J.6    Plow, E.F.7    Ginsberg, M.H.8
  • 24
    • 0037070206 scopus 로고    scopus 로고
    • Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus
    • Smith J.B., Theackston R.D.G., Coelho A.L., Barja-Fidalgo C., Calvete J.J., Marcinkiewicz C. Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus. FEBS Lett. 512:2002;111-115
    • (2002) FEBS Lett. , vol.512 , pp. 111-115
    • Smith, J.B.1    Theackston, R.D.G.2    Coelho, A.L.3    Barja-Fidalgo, C.4    Calvete, J.J.5    Marcinkiewicz, C.6
  • 25
    • 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 J.J. Snake venomics: characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and tandem mass spectrometry analysis. Proteomics. 4:2004;327-338
    • (2004) Proteomics , vol.4 , pp. 327-338
    • Juárez, P.1    Sanz, L.2    Calvete, J.J.3
  • 26
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulphide bond engineering
    • Calvete J.J., Moreno-Murciano M.P., Theakston R.D.G., Kisiel D.G., Marcinkiewicz C. Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering. Biochem. J. 372:2003;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
  • 27
    • 0030750415 scopus 로고    scopus 로고
    • Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site
    • Marcinkiewicz C., Senadhi V.K., McLane M.A., Niewiarowski S. Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site. Blood. 90:1997;1565-1575
    • (1997) Blood , vol.90 , pp. 1565-1575
    • Marcinkiewicz, C.1    Senadhi, V.K.2    McLane, M.A.3    Niewiarowski, S.4
  • 29
    • 0242664789 scopus 로고    scopus 로고
    • Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin
    • Monleon D., Moreno-Murciano M.P., Kovacs H., Marcinkiewicz C., Calvete J.J., Celda B. Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin. J. Biol. Chem. 278:2003;45570-45576
    • (2003) J. Biol. Chem. , vol.278 , pp. 45570-45576
    • Monleon, D.1    Moreno-Murciano, M.P.2    Kovacs, H.3    Marcinkiewicz, C.4    Calvete, J.J.5    Celda, B.6
  • 30
    • 0024206252 scopus 로고
    • Echistatin. a potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus
    • Gan Z.R., Gould R.J., Jacobs J.W., Friedman P.A., Polokoff M.A. Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus. J. Biol. Chem. 263:1988;19827-19832
    • (1988) J. Biol. Chem. , vol.263 , pp. 19827-19832
    • Gan, Z.R.1    Gould, R.J.2    Jacobs, J.W.3    Friedman, P.A.4    Polokoff, M.A.5
  • 31
    • 0028168017 scopus 로고
    • Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets
    • McLane M.A., Kowalska M.A., Silver L., Shattil S.J., Niewiarowski S. Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets. Biochem. J. 301:1994;429-436
    • (1994) Biochem. J. , vol.301 , pp. 429-436
    • McLane, M.A.1    Kowalska, M.A.2    Silver, L.3    Shattil, S.J.4    Niewiarowski, S.5
  • 32
    • 0035049724 scopus 로고    scopus 로고
    • Comparative biochemistry of disintegrins isolated from snake venom: Consideration of the taxonomy and geographical distribution of snakes in the genus Echis
    • Okuda D., Nozaki C., Sekiya F., Morita T. Comparative biochemistry of disintegrins isolated from snake venom: consideration of the taxonomy and geographical distribution of snakes in the genus Echis. J. Biochem. (Tokyo). 129:2001;615-620
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 615-620
    • Okuda, D.1    Nozaki, C.2    Sekiya, F.3    Morita, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.