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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.
Submitted August 20, 2003
Accepted September 29, 2003
Differential processing of stromal-derived factor-1  and  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*
Experimental Transplantation and Immunology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA
HIV and AIDS Malignancy Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA
Laboratory of Biophysical Chemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA
Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA
* Corresponding author; email: tosatog{at}mail.nih.gov.
The chemokine SDF-1, which is constitutively expressed in most tissues as SDF-1  and  resulting from alternative gene splicing, regulates hematopoiesis, lymphocyte homing, B-lineage cell growth and angiogenesis. Since SDF-1 and are constitutively and ubiquitously expressed, their degradation must serve an important regulatory role. Here we show that SDF-1 and 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. Dipeptidyl-peptidase/CD26 is responsible for serum cleavage of SDF-1 and 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 pre-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 provides biological significance to the existence of two splice forms of the chemokine, and adds a tool to precisely regulate SDF-1 biological activity by changes in specific activity.
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