메뉴 건너뛰기




Volumn 29, Issue 12, 2008, Pages 2188-2195

Peptidomic analysis of blood plasma after in vivo treatment with protease inhibitors-A proof of concept study

Author keywords

Dipetidylpeptidase IV; DPPIV; Factor Xa; FONDAPARINUX; Peptidomics; Protease inhibition

Indexed keywords

BLOOD CLOTTING FACTOR 10A; DIPEPTIDYL PEPTIDASE IV INHIBITOR; FONDAPARINUX; PROTEINASE; PROTEINASE INHIBITOR;

EID: 56149103751     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2008.08.016     Document Type: Article
Times cited : (18)

References (24)
  • 2
    • 0000135759 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats
    • Balkan B., Kwasnik L., Miserendino R., Holst J.J., and Li X. Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia 42 (1999) 1324-1331
    • (1999) Diabetologia , vol.42 , pp. 1324-1331
    • Balkan, B.1    Kwasnik, L.2    Miserendino, R.3    Holst, J.J.4    Li, X.5
  • 3
    • 0033602521 scopus 로고    scopus 로고
    • Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors
    • Belyaev A., Zhang X., Augustyns K., Lambeir A.M., De M., Vedernikova I., et al. Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors. J Med Chem 42 (1999) 52-1041
    • (1999) J Med Chem , vol.42 , pp. 52-1041
    • Belyaev, A.1    Zhang, X.2    Augustyns, K.3    Lambeir, A.M.4    De, M.5    Vedernikova, I.6
  • 4
    • 0029822179 scopus 로고    scopus 로고
    • Biosynthesis of prothrombin: intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation
    • Bristol J.A., Ratcliffe J.V., Roth D.A., Jacobs M.A., Furie B.C., and Furie B. Biosynthesis of prothrombin: intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation. Blood 88 (1996) 2585-2593
    • (1996) Blood , vol.88 , pp. 2585-2593
    • Bristol, J.A.1    Ratcliffe, J.V.2    Roth, D.A.3    Jacobs, M.A.4    Furie, B.C.5    Furie, B.6
  • 7
    • 0038363953 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV substrates. An update on in vitro peptide hydrolysis by human DPPIV
    • De Meester I., Lambeir A.M., Proost P., and Scharpe S. Dipeptidyl peptidase IV substrates. An update on in vitro peptide hydrolysis by human DPPIV. Adv Exp Med Biol 524 (2003) 3-17
    • (2003) Adv Exp Med Biol , vol.524 , pp. 3-17
    • De Meester, I.1    Lambeir, A.M.2    Proost, P.3    Scharpe, S.4
  • 8
    • 0036356840 scopus 로고    scopus 로고
    • The fibrinolysis system: regulation of activity and physiologic functions of its main components
    • Dobrovolsky A.B., and Titaeva E.V. The fibrinolysis system: regulation of activity and physiologic functions of its main components. Biochemistry (Mosc.) 67 (2002) 99-108
    • (2002) Biochemistry (Mosc.) , vol.67 , pp. 99-108
    • Dobrovolsky, A.B.1    Titaeva, E.V.2
  • 9
    • 10444267279 scopus 로고    scopus 로고
    • In vitro comparison of the effect of fondaparinux and enoxaparin on whole blood tissue factor-triggered thromboelastography profile
    • Gerotziafas G.T., Chakroun T., Samama M.M., and Elalamy I. In vitro comparison of the effect of fondaparinux and enoxaparin on whole blood tissue factor-triggered thromboelastography profile. Thromb Haemost 92 (2004) 1296-1302
    • (2004) Thromb Haemost , vol.92 , pp. 1296-1302
    • Gerotziafas, G.T.1    Chakroun, T.2    Samama, M.M.3    Elalamy, I.4
  • 10
    • 1642417831 scopus 로고    scopus 로고
    • Comparison of the effect of fondaparinux and enoxaparin on thrombin generation during in-vitro clotting of whole blood and platelet-rich plasma
    • Gerotziafas G.T., Depasse F., Chakroun T., Van Dreden P., Samama M.M., and Elalamy I. Comparison of the effect of fondaparinux and enoxaparin on thrombin generation during in-vitro clotting of whole blood and platelet-rich plasma. Blood Coagul Fibrin 15 (2004) 149-156
    • (2004) Blood Coagul Fibrin , vol.15 , pp. 149-156
    • Gerotziafas, G.T.1    Depasse, F.2    Chakroun, T.3    Van Dreden, P.4    Samama, M.M.5    Elalamy, I.6
  • 11
    • 84890798379 scopus 로고    scopus 로고
    • Surrogate end points: how well do they represent patient-relevant end points?
    • Jost M.M. Surrogate end points: how well do they represent patient-relevant end points?. Biomarkers Med 1 (2007) 1-15
    • (2007) Biomarkers Med , vol.1 , pp. 1-15
    • Jost, M.M.1
  • 12
    • 20844448187 scopus 로고    scopus 로고
    • Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery
    • Koomen J.M., Li D., Xiao L.C., Liu T.C., Coombes K.R., Abbruzzese J., et al. Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery. J Proteome Res 4 (2005) 972-981
    • (2005) J Proteome Res , vol.4 , pp. 972-981
    • Koomen, J.M.1    Li, D.2    Xiao, L.C.3    Liu, T.C.4    Coombes, K.R.5    Abbruzzese, J.6
  • 13
    • 0037787851 scopus 로고    scopus 로고
    • I. Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV
    • Lambeir A.M., Durinx C., Scharpe S., and De M. I. Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Crit Rev Clin Lab Sci 40 (2003) 209-294
    • (2003) Crit Rev Clin Lab Sci , vol.40 , pp. 209-294
    • Lambeir, A.M.1    Durinx, C.2    Scharpe, S.3    De, M.4
  • 16
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn G.S., States D.J., Adamski M., Blackwell T.W., Menon R., Hermjakob H., et al. Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 5 (2005) 3226-3245
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 17
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: linking extracellular proteases to substrates
    • Overall C.M., and Blobel C.P. In search of partners: linking extracellular proteases to substrates. Nat Rev Mol Cell Biol 8 (2007) 245-257
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 18
    • 23944520883 scopus 로고    scopus 로고
    • HUPO Plasma Proteome Project specimen collection and handling: towards the standardization of parameters for plasma proteome samples
    • Rai A.J., Gelfand C.A., Haywood B.C., Warunek D.J., Yi J., Schuchard M.D., et al. HUPO Plasma Proteome Project specimen collection and handling: towards the standardization of parameters for plasma proteome samples. Proteomics 5 (2005) 3262-3277
    • (2005) Proteomics , vol.5 , pp. 3262-3277
    • Rai, A.J.1    Gelfand, C.A.2    Haywood, B.C.3    Warunek, D.J.4    Yi, J.5    Schuchard, M.D.6
  • 20
    • 34250679321 scopus 로고    scopus 로고
    • Factor XIII activation peptide is released into plasma upon cleavage by thrombin and shows a different structure compared to its bound form
    • Schroeder V., Vuissoz J.M., Caflisch A., and Kohler H.P. Factor XIII activation peptide is released into plasma upon cleavage by thrombin and shows a different structure compared to its bound form. Thromb Haemost 97 (2007) 890-898
    • (2007) Thromb Haemost , vol.97 , pp. 890-898
    • Schroeder, V.1    Vuissoz, J.M.2    Caflisch, A.3    Kohler, H.P.4
  • 21
    • 35148870759 scopus 로고    scopus 로고
    • Clinical peptidomics: peptide-biomarker discovery in blood
    • Marko-Varga G. (Ed), Elsevier Science, Amsterdam
    • Schulte I., Tammen H., Selle H., Zucht H.D., and Schulz-Knappe P. Clinical peptidomics: peptide-biomarker discovery in blood. In: Marko-Varga G. (Ed). Proteomics & Peptidomics (2005), Elsevier Science, Amsterdam
    • (2005) Proteomics & Peptidomics
    • Schulte, I.1    Tammen, H.2    Selle, H.3    Zucht, H.D.4    Schulz-Knappe, P.5
  • 22
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display
    • Tammen H., Schulte I., Hess R., Menzel C., Kellmann M., Mohring T., et al. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 5 (2005) 3414-3422
    • (2005) Proteomics , vol.5 , pp. 3414-3422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 23
    • 3042857728 scopus 로고    scopus 로고
    • Fondaparinux: a Factor Xa inhibitor for antithrombotic therapy
    • Turpie A.G. Fondaparinux: a Factor Xa inhibitor for antithrombotic therapy. Expert Opin Pharmacother 5 (2004) 1373-1384
    • (2004) Expert Opin Pharmacother , vol.5 , pp. 1373-1384
    • Turpie, A.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.