메뉴 건너뛰기




Volumn 395, Issue 1, 2006, Pages 165-172

Structure-activity relationships of the human prothrombin kringle-2 peptide derivative NSA9: Anti-proliferative activity and cellular internalization

Author keywords

Anti angiogenesis; Derivative; Endothelial cell proliferation; Flow cytometry; NSA9; Structure activity relationship (SAR)

Indexed keywords

BIOASSAY; BIOLOGICAL ORGANS; CELL CULTURE; ENZYME INHIBITION; PROTEINS; TUMORS;

EID: 33645564863     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051300     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. (1995) Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat. Med. 1, 27-31
    • (1995) Nat. Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 2
    • 0034695685 scopus 로고    scopus 로고
    • The hemostatic system as a regulator of angiogenesis
    • Browder, T., Folkman, J. and Pirie-Shepherd, S. (2000) The hemostatic system as a regulator of angiogenesis. J. Biol. Chem. 275, 1521-1524
    • (2000) J. Biol. Chem. , vol.275 , pp. 1521-1524
    • Browder, T.1    Folkman, J.2    Pirie-Shepherd, S.3
  • 3
  • 5
    • 0025147371 scopus 로고
    • A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin
    • Good, D. J., Polverini, P. J., Rastinejad, F., Le Beau, M. M., Lemons, R. S., Frazier, W. A. and Bouck, N. P. (1990) A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin. Proc. Natl. Acad. Sci. U.S.A. 87, 6624-6628
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6624-6628
    • Good, D.J.1    Polverini, P.J.2    Rastinejad, F.3    Le Beau, M.M.4    Lemons, R.S.5    Frazier, W.A.6    Bouck, N.P.7
  • 7
    • 4143051554 scopus 로고    scopus 로고
    • Recent developments in the inhibition of angiogenesis: Examples from studies on platelet factor-4 and the VEGF/VEGER system
    • Bikfalvi, A. (2004) Recent developments in the inhibition of angiogenesis: examples from studies on platelet factor-4 and the VEGF/VEGER system. Biochem. Pharmcol. 68, 1017-1021
    • (2004) Biochem. Pharmcol. , vol.68 , pp. 1017-1021
    • Bikfalvi, A.1
  • 8
    • 0032582635 scopus 로고    scopus 로고
    • Prothrombin kringle-2 domain has a growth inhibitory activity against basic fibroblast growth factor-stimulated capillary endothelial cells
    • Lee, T. H., Rhim, T. and Kim, S. S. (1998) Prothrombin kringle-2 domain has a growth inhibitory activity against basic fibroblast growth factor-stimulated capillary endothelial cells. J. Biol. Chem. 273, 28805-28812
    • (1998) J. Biol. Chem. , vol.273 , pp. 28805-28812
    • Lee, T.H.1    Rhim, T.2    Kim, S.S.3
  • 9
    • 0034979273 scopus 로고    scopus 로고
    • Role of vascular endothelial growth factor in regulation of physiological angiogenesis
    • Ferrara, N. (2001) Role of vascular endothelial growth factor in regulation of physiological angiogenesis. Am. J. Physiol. Cell Physiol. 280, C1358-C1366
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Ferrara, N.1
  • 10
    • 13844319702 scopus 로고    scopus 로고
    • Molecular imaging of antiangiogenic agents
    • Rehman, S. and Jayson, G. C. (2005) Molecular imaging of antiangiogenic agents. Oncologist 10, 92-103
    • (2005) Oncologist , vol.10 , pp. 92-103
    • Rehman, S.1    Jayson, G.C.2
  • 11
    • 20144379162 scopus 로고    scopus 로고
    • Endogenous inhibitors of angiogenesis
    • Nyberg, P., Xie, L. and Kalluri, R. (2005) Endogenous inhibitors of angiogenesis. Cancer Res. 65, 3967-3979
    • (2005) Cancer Res. , vol.65 , pp. 3967-3979
    • Nyberg, P.1    Xie, L.2    Kalluri, R.3
  • 12
    • 0842311707 scopus 로고    scopus 로고
    • Discovery and development of anti-angiogenic peptides: A structural link
    • Dings, R. P. M., Nesmelova, I., Griffioen, A. W. and Mayo, K. H. (2003) Discovery and development of anti-angiogenic peptides: a structural link. Angiogenesis 6, 83-91
    • (2003) Angiogenesis , vol.6 , pp. 83-91
    • Dings, R.P.M.1    Nesmelova, I.2    Griffioen, A.W.3    Mayo, K.H.4
  • 13
    • 0030948209 scopus 로고    scopus 로고
    • Structure-internalization relationship for adsorptive-mediated endocytosis of basic peptides at the blood-brain barrier
    • Tamai, I., Sai, Y., Kobayashi, H., Kamata, M., Wakamiya, T. and Tsuji, A. (1997) Structure-internalization relationship for adsorptive-mediated endocytosis of basic peptides at the blood-brain barrier. J. Pharmacol. Exp. Ther. 280, 410-415
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 410-415
    • Tamai, I.1    Sai, Y.2    Kobayashi, H.3    Kamata, M.4    Wakamiya, T.5    Tsuji, A.6
  • 14
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L. and Rothbard, J. B. (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 15
    • 0036794256 scopus 로고    scopus 로고
    • Sequence requirements for the activity of membrane-active peptides
    • Werkmeister, J. A., Hewish, D. R., Kirkpatrick, A. and Rivett, D. E. (2002) Sequence requirements for the activity of membrane-active peptides. J. Pept. Res. 60, 232-238
    • (2002) J. Pept. Res. , vol.60 , pp. 232-238
    • Werkmeister, J.A.1    Hewish, D.R.2    Kirkpatrick, A.3    Rivett, D.E.4
  • 20
    • 2442555007 scopus 로고    scopus 로고
    • An endostatin-derived peptide interacts with integrins and regulates actin cytoskeleton and migration of endothelial cells
    • Wickström, S. A., Alitalo, K. and Keski-Oja, J. (2004) An endostatin-derived peptide interacts with integrins and regulates actin cytoskeleton and migration of endothelial cells. J. Biol. Chem. 279, 20178-20185
    • (2004) J. Biol. Chem. , vol.279 , pp. 20178-20185
    • Wickström, S.A.1    Alitalo, K.2    Keski-Oja, J.3
  • 21
    • 0141809387 scopus 로고    scopus 로고
    • Angiosuppressive and angiostimulatory effects exerted by synthetic partial sequences of endostatin
    • Morbidelli, L., Donnini, S., Chillemi, F., Giachetti, A. and Ziehe, M. (2003) Angiosuppressive and angiostimulatory effects exerted by synthetic partial sequences of endostatin. Clin. Cancer Res. 9, 5358-5369
    • (2003) Clin. Cancer Res. , vol.9 , pp. 5358-5369
    • Morbidelli, L.1    Donnini, S.2    Chillemi, F.3    Giachetti, A.4    Ziehe, M.5
  • 22
    • 0037442551 scopus 로고    scopus 로고
    • Human endostatin-derived synthetic peptides possess potent antiangiogenic properties in vitro and in vivo
    • Cattaneo, M. G., Pola, S., Francescato, P., Chillemi, F. and Vicentini, L. M. (2003) Human endostatin-derived synthetic peptides possess potent antiangiogenic properties in vitro and in vivo. Exp. Cell. Res. 283, 230-236
    • (2003) Exp. Cell. Res. , vol.283 , pp. 230-236
    • Cattaneo, M.G.1    Pola, S.2    Francescato, P.3    Chillemi, F.4    Vicentini, L.M.5
  • 23
    • 0141455068 scopus 로고    scopus 로고
    • Studies on the structure-activity relationship of endostatin: Synthesis of human endostatin peptides exhibiting potent antiangiogenic activities
    • Chillemi, F., Francescato, P., Ragg, E., Cattaneo, M. G., Pola, S. and Vicentini, L. (2003) Studies on the structure-activity relationship of endostatin: synthesis of human endostatin peptides exhibiting potent antiangiogenic activities. J. Med. Chem. 46, 4165-4172
    • (2003) J. Med. Chem. , vol.46 , pp. 4165-4172
    • Chillemi, F.1    Francescato, P.2    Ragg, E.3    Cattaneo, M.G.4    Pola, S.5    Vicentini, L.6
  • 24
    • 3543075257 scopus 로고    scopus 로고
    • N-/C-terminal deleted mutant of human endostatin efficiently acts as an anti-angiogenic and anti-tumorigenic agent
    • Cho, H., Kim, W. J., Lee, Y. M., Kim, Y. M., Kwon, Y. G., Park, Y. S., Choi, E. Y. and Kim, K. W. (2004) N-/C-terminal deleted mutant of human endostatin efficiently acts as an anti-angiogenic and anti-tumorigenic agent. Onco. Rep. 11, 191-195
    • (2004) Onco. Rep. , vol.11 , pp. 191-195
    • Cho, H.1    Kim, W.J.2    Lee, Y.M.3    Kim, Y.M.4    Kwon, Y.G.5    Park, Y.S.6    Choi, E.Y.7    Kim, K.W.8
  • 26
    • 0027290714 scopus 로고
    • Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity
    • Tolsma, S. S., Volpert, O. V., Good, D. J., Frazier, W. A., Polverini, P. J. and Bouck, N. (1993) Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity. J. Cell. Biol. 122, 497-511
    • (1993) J. Cell. Biol. , vol.122 , pp. 497-511
    • Tolsma, S.S.1    Volpert, O.V.2    Good, D.J.3    Frazier, W.A.4    Polverini, P.J.5    Bouck, N.6
  • 27
    • 0033027727 scopus 로고    scopus 로고
    • Three distinct D-amino acid substitutions confer potent antiangiogenic activity on an inactive peptide derived from a thrombospondin-1 type 1 repeat
    • Dawson, D. W., Volpert, O. V., Pearce, S. F. A., Schneider, A. J., Silverstein, R. L., Henkin, J. and Bouck, N. P. (1999) Three distinct D-amino acid substitutions confer potent antiangiogenic activity on an inactive peptide derived from a thrombospondin-1 type 1 repeat. Mol. Pharmacol. 55, 332-338
    • (1999) Mol. Pharmacol. , vol.55 , pp. 332-338
    • Dawson, D.W.1    Volpert, O.V.2    Pearce, S.F.A.3    Schneider, A.J.4    Silverstein, R.L.5    Henkin, J.6    Bouck, N.P.7
  • 30
    • 0036734144 scopus 로고    scopus 로고
    • Parathyroid hormone-related peptide is a naturally occurring, protein kinase A-dependent angiogenesis inhibitor
    • Bakre, M. M., Zhu, Y., Yin, H., Burton, D. W., Terkeltaub, R., Deftos, L. J. and Varner, J. A. (2002) Parathyroid hormone-related peptide is a naturally occurring, protein kinase A-dependent angiogenesis inhibitor. Nat. Med. 8, 995-1003
    • (2002) Nat. Med. , vol.8 , pp. 995-1003
    • Bakre, M.M.1    Zhu, Y.2    Yin, H.3    Burton, D.W.4    Terkeltaub, R.5    Deftos, L.J.6    Varner, J.A.7
  • 31
    • 0035853460 scopus 로고    scopus 로고
    • A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor
    • Tan, D. C. W., Kini, R. M., Jois, S. D. S., Lim, D. K. F., Xin, L. and Ge, R. (2001) A small peptide derived from Flt-1 (VEGFR-1) functions as an angiogenic inhibitor. FEBS Lett. 494, 150-156
    • (2001) FEBS Lett. , vol.494 , pp. 150-156
    • Tan, D.C.W.1    Kini, R.M.2    Jois, S.D.S.3    Lim, D.K.F.4    Xin, L.5    Ge, R.6
  • 32
    • 0038516807 scopus 로고    scopus 로고
    • Recombinant human prothrombin kringles have potent anti-angiogenic activities and inhibit Lewis lung carcinoma tumor growth and metastases
    • Kim, T. H., Kim, E., Yoon, D., Kim, J., Rhim, T. Y. and Kim, S. S. (2002) Recombinant human prothrombin kringles have potent anti-angiogenic activities and inhibit Lewis lung carcinoma tumor growth and metastases. Angiogenesis 5, 191-201
    • (2002) Angiogenesis , vol.5 , pp. 191-201
    • Kim, T.H.1    Kim, E.2    Yoon, D.3    Kim, J.4    Rhim, T.Y.5    Kim, S.S.6
  • 33
    • 0036544676 scopus 로고    scopus 로고
    • A peptide derived from human prothrombin fragment 2 inhibits prothrombinase and angiogenesis
    • Kim, B. J., Koo, S. Y. and Kim, S. S. (2002) A peptide derived from human prothrombin fragment 2 inhibits prothrombinase and angiogenesis. Thromb. Res. 106, 81-87
    • (2002) Thromb. Res. , vol.106 , pp. 81-87
    • Kim, B.J.1    Koo, S.Y.2    Kim, S.S.3
  • 34
    • 0018085515 scopus 로고
    • Solid-phase peptide synthesis using mild base cleavage of N α-fluorenylmethyloxycarbonylamino acids, exemplified by a synthesis of dihydrosomatostatin
    • Chang, C. D. and Meienhofer, J. (1978) Solid-phase peptide synthesis using mild base cleavage of N α-fluorenylmethyloxycarbonylamino acids, exemplified by a synthesis of dihydrosomatostatin. Int. J. Pept. Protein Res. 11, 246-249
    • (1978) Int. J. Pept. Protein Res. , vol.11 , pp. 246-249
    • Chang, C.D.1    Meienhofer, J.2
  • 35
    • 0025738516 scopus 로고
    • Tetrazolium-based assays for cellular viability: A critical examination of selected parameters affecting formazan production
    • Vistica, D. T., Skehan, P., Scudiero, D., Monks, A., Pittman, A. and Boyd, M. R. (1991) Tetrazolium-based assays for cellular viability: a critical examination of selected parameters affecting formazan production. Cancer Res. 51, 2515-2520
    • (1991) Cancer Res. , vol.51 , pp. 2515-2520
    • Vistica, D.T.1    Skehan, P.2    Scudiero, D.3    Monks, A.4    Pittman, A.5    Boyd, M.R.6
  • 37
    • 13444291499 scopus 로고    scopus 로고
    • Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin
    • John, H., Radtke, K., Ständker, L. and Forssmann, W. G. (2005) Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin. Biochim. Biopnys. Acta 1747, 161-170
    • (2005) Biochim. Biopnys. Acta , vol.1747 , pp. 161-170
    • John, H.1    Radtke, K.2    Ständker, L.3    Forssmann, W.G.4
  • 38
    • 23744487017 scopus 로고    scopus 로고
    • The human prothrombin kringle-2 derived peptide, NSA9, is internalized into bovine capillary endothelial cells through endocytosis and energy-dependent pathways
    • Hwang, H. S. and Kim, S. S. (2005) The human prothrombin kringle-2 derived peptide, NSA9, is internalized into bovine capillary endothelial cells through endocytosis and energy-dependent pathways. Biochem. Biophys. Res. Commun. 335, 469-476
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 469-476
    • Hwang, H.S.1    Kim, S.S.2
  • 40
    • 0037061669 scopus 로고    scopus 로고
    • Bioactive pseudopeptidic analogues and cyclostereoisomers of osteogenic growth peptide C-terminal pentapeptide, OGP (10-14)
    • Chen, Y., Muhlrad, A., Shteyer, A., Vidson, M., Bab, I. and Chorev, M. (2002) Bioactive pseudopeptidic analogues and cyclostereoisomers of osteogenic growth peptide C-terminal pentapeptide, OGP (10-14). J. Med. Chem. 45, 1624-1632
    • (2002) J. Med. Chem. , vol.45 , pp. 1624-1632
    • Chen, Y.1    Muhlrad, A.2    Shteyer, A.3    Vidson, M.4    Bab, I.5    Chorev, M.6
  • 41
    • 0029030898 scopus 로고
    • Structure-activity study of a laminin α1 chain active peptide segment Ile-Lys-Val-Ala-Val (IKVAN)
    • Nomizu, M., Weeks, B. S., Weston, C. A., Kim, W. H., Kleinman, H. K. and Yamada, Y. (1995) Structure-activity study of a laminin α1 chain active peptide segment Ile-Lys-Val-Ala-Val (IKVAN). FEBS Lett. 365, 227-231
    • (1995) FEBS Lett. , vol.365 , pp. 227-231
    • Nomizu, M.1    Weeks, B.S.2    Weston, C.A.3    Kim, W.H.4    Kleinman, H.K.5    Yamada, Y.6
  • 44
    • 0036391162 scopus 로고    scopus 로고
    • Osteogenic growth peptide: From concept to drug design
    • Bab, I. and Chorev, M. (2002) Osteogenic growth peptide: from concept to drug design. Biopolymer 66, 33-48
    • (2002) Biopolymer , vol.66 , pp. 33-48
    • Bab, I.1    Chorev, M.2
  • 45
    • 0032946965 scopus 로고    scopus 로고
    • Structure-activity studies of normal and retro pig cecropin-melittin hybrids
    • Juvvadi, P., Vunnaam, S., Yoo, B. and Merrifield, R. B. (1999) Structure-activity studies of normal and retro pig cecropin-melittin hybrids. J. Peptide Res. 53, 244-251
    • (1999) J. Peptide Res. , vol.53 , pp. 244-251
    • Juvvadi, P.1    Vunnaam, S.2    Yoo, B.3    Merrifield, R.B.4
  • 46
    • 0025001650 scopus 로고
    • AII-D-magainin: Chirality, antimicrobial activity and proteolytic resistance
    • Bessalle, R., Kapitkovsky, A., Gorea, A., Shalit, I. and Fridkin, M. (1990) AII-D-magainin: chirality, antimicrobial activity and proteolytic resistance. FEBS Lett. 274, 151-155
    • (1990) FEBS Lett. , vol.274 , pp. 151-155
    • Bessalle, R.1    Kapitkovsky, A.2    Gorea, A.3    Shalit, I.4    Fridkin, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.