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Prepublished online as a Blood First Edition Paper on December 12, 2002; DOI 10.1182/blood-2002-07-2315. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-07-2315v1 101/8/3014    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Liu, J.-M. Articles by Wdzieczak-Bakala, J. Search for Related Content PubMed PubMed Citation Articles by Liu, J.-M. Articles by Wdzieczak-Bakala, J. Related Collections Hematopoiesis and Stem Cells Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 April 2003, Vol. 101, No. 8, pp. 3014-3020 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The tetrapeptide AcSDKP, an inhibitor of primitive hematopoietic cell proliferation, induces angiogenesis in vitro and in vivo Jian-Miao Liu, Françoise Lawrence, Milica Kovacevic, Jérôme Bignon, Evangelia Papadimitriou, Jean-Yves Lallemand, Panagiotis Katsoris, Pierre Potier, Yves Fromes, and Joanna Wdzieczak-Bakala From the Institut de Chimie des Substances Naturelles, Centre National de la Recherche Scientifique (CNRS), Gif-sur-Yvette, France; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, Greece; Division of Genetics, Cell and Developmental Biology, Department of Biology, University of Patras, Patras, Greece; and Institut de Myologie, INSERM U523, Paris, France. The tetrapeptide acetyl-Ser-Asp-Lys-Pro (AcSDKP), purified from bone marrow and constitutively synthesized in vivo, belongs to the family of negative regulators of hematopoiesis. It protects the stem cell compartment from the toxicity of anticancer drugs and irradiation and consequently contributes to a reduction in marrow failure. This current work provides experimental evidence for another novel biologic function of AcSDKP. We report that AcSDKP is a mediator of angiogenesis, as measured by its ability to modulate endothelial cell function in vitro and angiogenesis in vivo. AcSDKP at nanomolar concentrations stimulates in vitro endothelial cell migration and differentiation into capillary-like structures on Matrigel as well as enhances the secretion of an active form of matrix metalloproteinase-1 (MMP-1). In vivo, AcSDKP promotes a significant angiogenic response in the chicken embryo chorioallantoic membrane (CAM) and in the abdominal muscle of the rat. Moreover, it induces the formation of blood vessels in Matrigel plugs implanted subcutaneously in the rat. This is the first report demonstrating the ability of AcSDKP to interact directly with endothelial cells and to elicit an angiogenic response in vitro and in vivo. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y.-H. Liu, M. D'Ambrosio, T.-d. Liao, H. Peng, N.-E. Rhaleb, U. Sharma, S. Andre, H.-J. Gabius, and O. A. Carretero N-acetyl-seryl-aspartyl-lysyl-proline prevents cardiac remodeling and dysfunction induced by galectin-3, a mammalian adhesion/growth-regulatory lectin Am J Physiol Heart Circ Physiol, February 1, 2009; 296(2): H404 - H412. [Abstract] [Full Text] [PDF] L. Waeckel, J. Bignon, J.-M. Liu, D. Markovits, T. G. Ebrahimian, J. Vilar, B. Mees, O. Blanc-Brude, V. Barateau, S. Le ricousse-Roussanne, et al. Tetrapeptide AcSDKP Induces Postischemic Neovascularization Through Monocyte Chemoattractant Protein-1 Signaling Arterioscler Thromb Vasc Biol, April 1, 2006; 26(4): 773 - 779. [Abstract] [Full Text] [PDF] D. Wang, O. A. Carretero, X.-Y. Yang, N.-E. Rhaleb, Y.-H. Liu, T.-D. Liao, and X.-P. Yang N-acetyl-seryl-aspartyl-lysyl-proline stimulates angiogenesis in vitro and in vivo Am J Physiol Heart Circ Physiol, November 1, 2004; 287(5): H2099 - H2105. [Abstract] [Full Text] [PDF] Y. Nakayama, N. Nara, Y. Kawakita, Y. Takeshima, M. Arakawa, M. Katoh, S. Morita, K. Iwatsuki, K. Tanaka, S. Okamoto, et al. Cloning of cDNA Encoding a Regeneration-Associated Muscle Protease Whose Expression Is Attenuated in Cell Lines Derived from Duchenne Muscular Dystrophy Patients Am. J. Pathol., May 1, 2004; 164(5): 1773 - 1782. [Abstract] [Full Text] [PDF] S. Fuchs, H. D. Xiao, J. M. Cole, J. W. Adams, K. Frenzel, A. Michaud, H. Zhao, G. Keshelava, M. R. Capecchi, P. Corvol, et al. Role of the N-terminal Catalytic Domain of Angiotensin-converting Enzyme Investigated by Targeted Inactivation in Mice J. Biol. Chem., April 16, 2004; 279(16): 15946 - 15953. [Abstract] [Full Text] [PDF]

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