Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature.

作者: M. E. Akerman , J. Pilch , D. Peters , E. Ruoslahti

DOI: 10.1073/PNAS.0409844102

关键词:

摘要: A group of angiogenesis inhibitors are derived from fragments extracellular matrix or blood proteins. Endostatin, antithrombin, and anastellin members this substances. The plasma adhesion proteins fibronectin vitronectin serve as cofactors for these three antiangiogenic Anginex is a synthetic 33-amino acid peptide that was originally modeled to reproduce the β-sheet structure Here, we show anginex initiates polymerization inactive in mice lack fibronectin. shares characteristics with anastellin. Fluorescein-labeled specifically localized angiogenic vessels vivo. This localization dependent on inhibited by an Arg-Gly-Asp peptide. Thus, several physiological dependence role protein interaction apparently form integrin-binding complexes deliver sites angiogenesis. functional convergence factors has important implications therapies.

参考文章(32)
C R Ill, E Ruoslahti, Association of thrombin-antithrombin III complex with vitronectin in serum. Journal of Biological Chemistry. ,vol. 260, pp. 15610- 15615 ,(1985) , 10.1016/S0021-9258(17)36302-0
A Stockmann, S Hess, P Declerck, R Timpl, K.T. Preissner, Multimeric vitronectin. Identification and characterization of conformation-dependent self-association of the adhesive protein Journal of Biological Chemistry. ,vol. 268, pp. 22874- 22882 ,(1993) , 10.1016/S0021-9258(18)41608-0
Christopher D. Buckley, Darrell Pilling, Nick V. Henriquez, Greg Parsonage, Katy Threlfall, Dagmar Scheel-Toellner, David L. Simmons, Arne N. Akbar, Janet M. Lord, Mike Salmon, RGD peptides induce apoptosis by direct caspase-3 activation Nature. ,vol. 397, pp. 534- 539 ,(1999) , 10.1038/17409
Takao Sakai, Kamin J. Johnson, Michihiro Murozono, Keiko Sakai, Marc A. Magnuson, Tadeuz Wieloch, Tobias Cronberg, Atsushi Isshiki, Harold P. Erickson, Reinhard Fässler, Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis. Nature Medicine. ,vol. 7, pp. 324- 330 ,(2001) , 10.1038/85471
Erkki Ruoslahti, Specialization of tumour vasculature Nature Reviews Cancer. ,vol. 2, pp. 83- 90 ,(2002) , 10.1038/NRC724
Judah Folkman, Angiogenesis in cancer, vascular, rheumatoid and other disease Nature Medicine. ,vol. 1, pp. 27- 31 ,(1995) , 10.1038/NM0195-27
P. Laakkonen, M. E. Akerman, H. Biliran, M. Yang, F. Ferrer, T. Karpanen, R. M. Hoffman, E. Ruoslahti, Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 9381- 9386 ,(2004) , 10.1073/PNAS.0403317101
Alex Morla, Zhuohua Zhang, Erkki Ruoslahti, Superfibronectin is a functionally distinct form of fibronectin Nature. ,vol. 367, pp. 193- 196 ,(1994) , 10.1038/367193A0
Sharon R. Adderley, Desmond J. Fitzgerald, Glycoprotein IIb/IIIa Antagonists Induce Apoptosis in Rat Cardiomyocytes by Caspase-3 Activation * Journal of Biological Chemistry. ,vol. 275, pp. 5760- 5766 ,(2000) , 10.1074/JBC.275.8.5760
H. P. Erickson, Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin Proceedings of the National Academy of Sciences of the United States of America. ,vol. 91, pp. 10114- 10118 ,(1994) , 10.1073/PNAS.91.21.10114