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Blood, 1 April 2004, Vol. 103, No. 7, pp. 2452-2459. Prepublished online as a Blood First Edition Paper on October 2, 2003; DOI 10.1182/blood-2003-08-2857. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-08-2857v1 103/7/2452    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 De La Luz Sierra, M. Articles by Tosato, G. Search for Related Content PubMed PubMed Citation Articles by De La Luz Sierra, M. Articles by Tosato, G. Related Collections Hematopoiesis and Stem Cells Immunobiology Neoplasia Cell Adhesion and Motility Chemokines, Cytokines, and Interleukins Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  CHEMOKINES Differential processing of stromal-derived factor-1 and stromal-derived factor-1 explains functional diversity Maria De La Luz Sierra, Fuquan Yang, Masashi Narazaki, Ombretta Salvucci, David Davis, Robert Yarchoan, Hongwei H. Zhang, Henry Fales, and Giovanna Tosato From the Experimental Transplantation and Immunology Branch and the HIV and AIDS Malignancy Branch, National Cancer Institute, National Institutes of Health (NIH); the Laboratory of Biophysical Chemistry, National Heart, Lung, and Blood Institute, NIH; and the Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD. The chemokine stromal-derived factor-1 (SDF-1), which is constitutively expressed in most tissues as SDF-1 and SDF-1 resulting from alternative gene splicing, regulates hematopoiesis, lymphocyte homing, B-lineage cell growth, and angiogenesis. Because SDF-1 and SDF-1 are constitutively and ubiquitously expressed, their degradation must serve an important regulatory role. Here we show that SDF-1 and SDF-1 are secreted as full-length molecules. When exposed to human serum, full-length SDF-1 (1-68) undergoes processing first at the COOH terminus to produce SDF-1 1-67 and then at the NH2 terminus to produce SDF-1 3-67. By contrast, full-length SDF-1 (1-72) is processed only at the NH2 terminus to produce SDF-1 3-72. CD26/dipeptidyl peptidase is responsible for serum cleavage of SDF-1 and SDF-1 at the NH2 terminus. Serum processing of SDF-1 at the COOH terminus, which has not been previously reported, reduces the ability of the polypeptide to bind to heparin and to cells and to stimulate B-cell proliferation and chemotaxis. The additional processing at the NH2 terminus renders both forms of SDF-1 unable to bind to heparin and to activate cells. The differential processing of SDF-1 and SDF-1 provides biologic significance to the existence of 2 splice forms of the chemokine and adds a tool to precisely regulate SDF-1's biologic activity by changes in specific activity. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: X.-Y. Du and L. L.K. Leung Proteolytic regulatory mechanism of chemerin bioactivity Acta Biochim Biophys Sin, November 12, 2009; (2009) gmp091v1. [Abstract] [Full Text] [PDF] S. L. Mueller-Ortiz, D. Wang, J. E. Morales, L. Li, J.-Y. Chang, and R. A. 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