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Biochemical and Biophysical Research Communications Volume 255, Issue 3, 24 February 1999, Pages 657-662
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A Cellulose-Binding Domain-Fused Recombinant Human T Cell Connective Tissue-Activating Peptide-III Manifests Heparanase Activity Meirav Rechter a, Ofer Lider a, 1, Liora Cahalon a, Ehud Baharav a, Mara Dekel b, Daniel Seigel b, Israel Vlodavsky c , Helena Aingorn c , Irun R. Cohen a, Oded Shoseyov b Show more https://doi.org/10.1006/bbrc.1999.0181
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Abstract The chemokine connective tissue-activating peptide (CTAP)-III, which belongs to the leukocyte-derived growth factor family of mediators, was previously shown to be mitogenic for fibroblasts. However, it has recently been shown that CTAP-III, released from platelets, can act like a heparanase enzyme and degrade heparan sulfate. This suggests that CTAP-III may also function as a proinflammatory mediator. We have successfully cloned CTAP-III from a gt11 cDNA library of PHA-activated human CD4+T cells and produced recombinant CTAP-III as a fusion protein with a cellulose-binding domain moiety. This recombinant CTAP-III exhibited heparanase activity and released degradation products from metabolically labeled, naturally produced extracellular matrix. We have also developed polyclonal and monoclonal antibodies, and these antibodies against the recombinant CTAP-III detected the CTAP-III molecule in human T cells, polymorphonuclear leukocytes, and placental extracts. Thus, our study provides tools to examine further immune cell behavior in inflamed sites rich with extracellular moieties and proinflammatory mediators.
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Abbreviations used: CTAP-III, connective tissue activating peptide-III; LDGF, leukocyte derived growth factor; NAP-2, neutrophil activating peptide-2; HSPG, heparan sulfate proteoglycans; ECM, extracellular matrix; CBD, cellulose binding domain T. A. Springer 1
To whom correspondence should be addressed at Department of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel. Fax: 792-8-9343657. Email:
[email protected].
Copyright © 1999 Academic Press. All rights reserved.
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