메뉴 건너뛰기




Volumn 10, Issue 20, 2010, Pages 3712-3722

In vitro effects of Echis carinatus venom on the human plasma proteome

Author keywords

2 D PAGE; Animal proteomics; Plasma proteome; Proteases; Protein fragmentation; Snake venom

Indexed keywords

ALPHA 1 ANTITRYPSIN; APOLIPOPROTEIN A1; COMPLEMENT COMPONENT C4A; ECARIN; ECHIS VENOM; FIBRINOGEN; HAPTOGLOBIN; HEMOGLOBIN; HEMOPEXIN; PREALBUMIN; PROTEINASE; PROTEINASE INHIBITOR; PROTEOME; PROTHROMBIN; RETINOL BINDING PROTEIN 4; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 78649413567     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000055     Document Type: Article
Times cited : (9)

References (38)
  • 2
    • 58149156563 scopus 로고    scopus 로고
    • Proteome analysis of snake venom toxins: pharmacological insights
    • Georgieva, D., Arni, R. K., Betzel, C., Proteome analysis of snake venom toxins: pharmacological insights. Expert Rev. Proteomics 2008, 5, 787-797.
    • (2008) Expert Rev. Proteomics , vol.5 , pp. 787-797
    • Georgieva, D.1    Arni, R.K.2    Betzel, C.3
  • 3
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • Matsui, T., Fujimura, Y., Titani, K., Snake venom proteases affecting hemostasis and thrombosis. Biochim. Biophys. Acta 2000, 1477, 146-156.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 4
    • 33846105870 scopus 로고    scopus 로고
    • Snake venom components and their application in biomedicine
    • Koh, D. C., Arumugam, A., Jeyaseelan, K., Snake venom components and their application in biomedicine. Cell. Mol. Life Sci. 2006, 63, 3030-3041.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 3030-3041
    • Koh, D.C.1    Arumugam, A.2    Jeyaseelan, K.3
  • 6
    • 0028902904 scopus 로고
    • cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom
    • Nishida, S., Fujita, T., Kohno, N., Atoda, H. et al., cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom. Biochemistry 1995, 34, 1771-1778.
    • (1995) Biochemistry , vol.34 , pp. 1771-1778
    • Nishida, S.1    Fujita, T.2    Kohno, N.3    Atoda, H.4
  • 7
    • 0029939421 scopus 로고    scopus 로고
    • Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism
    • Yamada, D., Sekiya, F., Morita, T., Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J. Biol. Chem. 1996, 271, 5200-5207.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5200-5207
    • Yamada, D.1    Sekiya, F.2    Morita, T.3
  • 10
    • 67649617069 scopus 로고    scopus 로고
    • Subsite cooperativity in protease specificity
    • Ng, N. M., Pike, R. N., Boyd, S. E., Subsite cooperativity in protease specificity. Biol. Chem. 2009, 390, 401-407.
    • (2009) Biol. Chem. , vol.390 , pp. 401-407
    • Ng, N.M.1    Pike, R.N.2    Boyd, S.E.3
  • 11
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: history, character and diagnostic prospects
    • Anderson, N. L., Anderson, N. G., The human plasma proteome: history, character and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 12
    • 0242653640 scopus 로고    scopus 로고
    • Clinical proteomics: written in blood
    • Liotta, L. A., Ferrari, M., Petricoin, E., Clinical proteomics: written in blood. Nature 2003, 425, 905.
    • (2003) Nature , vol.425 , pp. 905
    • Liotta, L.A.1    Ferrari, M.2    Petricoin, E.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg, A., Obermaier, C., Boguth, G., Harder, A. et al., The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 2000, 21, 1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0035525595 scopus 로고    scopus 로고
    • Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis
    • Mortz, E., Krogh, T. N., Vorum, H., Görg, A., Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 2001, 1, 1359-1363.
    • (2001) Proteomics , vol.1 , pp. 1359-1363
    • Mortz, E.1    Krogh, T.N.2    Vorum, H.3    Görg, A.4
  • 17
    • 0028983813 scopus 로고
    • Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Góñez, J., Heldin, C. H., Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 1995, 224, 451-455.
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Góñez, J.3    Heldin, C.H.4
  • 18
    • 34249315396 scopus 로고    scopus 로고
    • Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma
    • Yi, J., Kim, C., Gelfand, C. A., Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma. J. Proteome Res. 2007, 6, 1768-1781.
    • (2007) J. Proteome Res. , vol.6 , pp. 1768-1781
    • Yi, J.1    Kim, C.2    Gelfand, C.A.3
  • 19
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: linking extracellular proteases to substrates
    • Overall, C. M., Blobel, C. P., In search of partners: linking extracellular proteases to substrates. Nat. Rev. Mol. Cell Biol. 2007, 8, 245-257.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 20
    • 0035423930 scopus 로고    scopus 로고
    • Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells
    • Wu, W. B., Chang, S. C., Liau, M. Y., Huang, T. F., Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells. Biochem. J. 2001, 357, 719-728.
    • (2001) Biochem. J. , vol.357 , pp. 719-728
    • Wu, W.B.1    Chang, S.C.2    Liau, M.Y.3    Huang, T.F.4
  • 21
    • 33644535491 scopus 로고    scopus 로고
    • Molecular cloning of novel serine proteases and phospholipases A2 from green pit viper (Trimeresurus albolabris) venom gland cDNA library
    • Rojnuckarin, P., Muanpasitporn, C., Chanhome, L., Arpijuntarangkoon, J., Intragumtornchai, T., Molecular cloning of novel serine proteases and phospholipases A2 from green pit viper (Trimeresurus albolabris) venom gland cDNA library. Toxicon 2006, 47, 279-287.
    • (2006) Toxicon , vol.47 , pp. 279-287
    • Rojnuckarin, P.1    Muanpasitporn, C.2    Chanhome, L.3    Arpijuntarangkoon, J.4    Intragumtornchai, T.5
  • 22
    • 0035742922 scopus 로고    scopus 로고
    • Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis
    • Siigur, J., Aaspõllu, A., Tõnism. agi, K., Trummal, K. et al., Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis. Haemostasis 2001, 31, 123-132.
    • (2001) Haemostasis , vol.31 , pp. 123-132
    • Siigur, J.1    Aaspõllu, A.2    Tõnism. agi, K.3    Trummal, K.4
  • 23
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • Matsui, T., Fujimura, Y., Titani, K., Snake venom proteases affecting hemostasis and thrombosis. Biochim. Biophys. Acta 2000, 1477, 146-156.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 24
    • 0018801061 scopus 로고
    • Characterization of the inactive fragment resulting from limited proteolysis of human alpha1-proteinase inhibitor by Crotalus adamanteus proteinase II
    • Kress, L. F., Kurecki, T., Chan, S. K., Laskowski, M., Sr., Characterization of the inactive fragment resulting from limited proteolysis of human alpha1-proteinase inhibitor by Crotalus adamanteus proteinase II. J. Biol. Chem. 1979, 254, 5317-5320.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5317-5320
    • Kress, L.F.1    Kurecki, T.2    Chan, S.K.3    Laskowski M., Sr.4
  • 25
    • 0014106895 scopus 로고
    • Alpha-1-antitrypsin, an inhibitor for thrombin and plasmin
    • Gans, H., Tan, B. H., Alpha-1-antitrypsin, an inhibitor for thrombin and plasmin. Clin. Chim. Acta 1967, 17, 111-117.
    • (1967) Clin. Chim. Acta , vol.17 , pp. 111-117
    • Gans, H.1    Tan, B.H.2
  • 26
    • 0030955961 scopus 로고    scopus 로고
    • Inhibition of human serine proteases by SPAAT, the C-terminal 44-residue peptide from alpha1-antitrypsin
    • Niemann, M. A., Baggott, J. E., Miller, E. J., Inhibition of human serine proteases by SPAAT, the C-terminal 44-residue peptide from alpha1-antitrypsin. Biochim. Biophys. Acta 1997, 1340, 123-130.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 123-130
    • Niemann, M.A.1    Baggott, J.E.2    Miller, E.J.3
  • 27
    • 34447503617 scopus 로고    scopus 로고
    • Antithrombotic activity of kininogen is mediated by inhibitory effects of domain 3 during arterial injury in vivo
    • Hassan, S., Sainz, I. M., Khan, M. M., Bradford, H. N. et al., Antithrombotic activity of kininogen is mediated by inhibitory effects of domain 3 during arterial injury in vivo. Am. J. Physiol. Heart Circ. Physiol. 2007, 292, 2959-2965.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292 , pp. 2959-2965
    • Hassan, S.1    Sainz, I.M.2    Khan, M.M.3    Bradford, H.N.4
  • 29
    • 0034234396 scopus 로고    scopus 로고
    • Involvement of bradykinin in acute exercise-induced increase of glucose uptake and GLUT-4 translocation in skeletal muscle: studies in normal and diabetic humans and rats
    • Taguchi, T., Kishikawa, H., Motoshima, H., Sakai, K. et al., Involvement of bradykinin in acute exercise-induced increase of glucose uptake and GLUT-4 translocation in skeletal muscle: studies in normal and diabetic humans and rats. Metabolism 2000, 49, 920-930.
    • (2000) Metabolism , vol.49 , pp. 920-930
    • Taguchi, T.1    Kishikawa, H.2    Motoshima, H.3    Sakai, K.4
  • 30
    • 0036657222 scopus 로고    scopus 로고
    • Alpha2-HS glycoprotein: a protein in search of a function
    • Arnaud, P., Kalabay, L., Alpha2-HS glycoprotein: a protein in search of a function. Diabetes Metab. Res. Rev. 2002, 18, 311-314.
    • (2002) Diabetes Metab. Res. Rev. , vol.18 , pp. 311-314
    • Arnaud, P.1    Kalabay, L.2
  • 31
    • 0027434926 scopus 로고
    • Alpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon model
    • De Boer, J. P., Creasey, A. A., Chang, A., Abbink, J. J. et al., Alpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon model. Infect. Immun. 1993, 61, 5035-5043.
    • (1993) Infect. Immun. , vol.61 , pp. 5035-5043
    • De Boer, J.P.1    Creasey, A.A.2    Chang, A.3    Abbink, J.J.4
  • 32
    • 0028219635 scopus 로고
    • Purification from Vipera lebetina (desert adder) venom of a protein that depletes human complement
    • Gasmi, A., Louzir, H., Karoui, H., el Ayeb, M., Dellagi, K., Purification from Vipera lebetina (desert adder) venom of a protein that depletes human complement. Nat. Toxins 1994, 2, 44-48.
    • (1994) Nat. Toxins , vol.2 , pp. 44-48
    • Gasmi, A.1    Louzir, H.2    Karoui, H.3    el Ayeb, M.4    Dellagi, K.5
  • 33
    • 0037606194 scopus 로고    scopus 로고
    • Apolipoprotein composition and particle size affect HDL degradation by chymase: effect on cellular cholesterol efflux
    • Lee, M., Kovanen, P. T., Tedeschi, G., Oungre, E. et al., Apolipoprotein composition and particle size affect HDL degradation by chymase: effect on cellular cholesterol efflux. J. Lipid Res. 2003, 44, 539-546.
    • (2003) J. Lipid Res. , vol.44 , pp. 539-546
    • Lee, M.1    Kovanen, P.T.2    Tedeschi, G.3    Oungre, E.4
  • 34
    • 0346847766 scopus 로고    scopus 로고
    • Albumin is substrate of human chymase. Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site
    • Raymond, W. W., Ruggles, S. W., Craik, C. S., Caughey, G. H., Albumin is substrate of human chymase. Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site. J. Biol. Chem. 2003, 278, 34517-34524.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34517-34524
    • Raymond, W.W.1    Ruggles, S.W.2    Craik, C.S.3    Caughey, G.H.4
  • 36
    • 54849423259 scopus 로고    scopus 로고
    • Human haptoglobin structure and function-a molecular modelling study
    • Polticelli, F., Bocedi, A., Minervini, G., Ascenzi, P., Human haptoglobin structure and function-a molecular modelling study. FEBS J. 2008, 275, 5648-5656.
    • (2008) FEBS J , vol.275 , pp. 5648-5656
    • Polticelli, F.1    Bocedi, A.2    Minervini, G.3    Ascenzi, P.4
  • 37
    • 43749090222 scopus 로고    scopus 로고
    • Iron and anemia in human biology: a review of mechanisms
    • Handelman, G. J., Levin, N. W., Iron and anemia in human biology: a review of mechanisms. Heart Fail. Rev. 2008, 13, 393-404.
    • (2008) Heart Fail. Rev. , vol.13 , pp. 393-404
    • Handelman, G.J.1    Levin, N.W.2
  • 38
    • 0034684193 scopus 로고    scopus 로고
    • The transthyretin-retinol-binding protein complex
    • Monaco, H. L., The transthyretin-retinol-binding protein complex. Biochim. Biophys Acta 2000, 1482, 65-72.
    • (2000) Biochim. Biophys Acta , vol.1482 , pp. 65-72
    • Monaco, H.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.