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The Journal of Immunology, Vol 156, Issue 5 1954-1962, Copyright © 1996 by American Association of Immunologists
ARTICLES |
F Petersen, A Ludwig, HD Flad and E Brandt
Department of Immunology and Cell Biology, Research Institute, Borstel,Germany.
Platelet factor 4 (PF-4), like IL-8, is a member of the chemokine superfamily of proinflammatory cytokines. However, although the capacity of IL-8 to stimulate functions in neutrophils is well established, reports on PF-4 are still contradictory. In the present study, we have prepared highly purified PF-4 and examined its ability to induce chemotaxis, degranulation, adhesion to gelatin and plasma proteins, and changes in intracellular calcium levels. Even over a broad range of concentrations, PF-4 alone was unable to induce functional changes in PMN. However, neutrophils pre- or co-incubated with physiologically relevant concentrations of TNF-alpha responded to PF-4 by the selective mobilization of the secondary granule marker lactoferrin but not of the primary granule marker elastase. Contrary to IL-8, PMN did not require pretreatment with cytochalasin B for PF-4- induced exocytosis of lactoferrin. The synergistic effect of PF-4 with TNF-alpha was not a priming phenomenon because the cooperative response remained unchanged even when TNF-alpha was added 5 min after the chemokine. In contrast, TNF-alpha-treated PMN did not respond to PF-4 by chemotaxis or by an increase of intracellular calcium levels, and no competition of PF-4 for IL-8 receptors was observed. Our results suggest a mechanism as well as a biologic role of PF-4 in the regulation of neutrophil function, which is different from that of IL-8 and other alpha-chemokines.
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B. I. Schenk, F. Petersen, H.-D. Flad, and E. Brandt Platelet-Derived Chemokines CXC Chemokine Ligand (CXCL)7, Connective Tissue-Activating Peptide III, and CXCL4 Differentially Affect and Cross-Regulate Neutrophil Adhesion and Transendothelial Migration J. Immunol., September 1, 2002; 169(5): 2602 - 2610. [Abstract] [Full Text] [PDF]
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P. E. Van den Steen, P. Proost, A. Wuyts, J. Van Damme, and G. Opdenakker Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact Blood, October 15, 2000; 96(8): 2673 - 2681. [Abstract] [Full Text] [PDF]
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B. Scheuerer, M. Ernst, I. Durrbaum-Landmann, J. Fleischer, E. Grage-Griebenow, E. Brandt, H.-D. Flad, and F. Petersen The CXC-chemokine platelet factor 4 promotes monocyte survival and induces monocyte differentiation into macrophages Blood, February 15, 2000; 95(4): 1158 - 1166. [Abstract] [Full Text] [PDF]
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F. Petersen, E. Brandt, U. Lindahl, and D. Spillmann Characterization of a Neutrophil Cell Surface Glycosaminoglycan That Mediates Binding of Platelet Factor 4 J. Biol. Chem., April 30, 1999; 274(18): 12376 - 12382. [Abstract] [Full Text] [PDF]
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F. Petersen, L. Bock, H.-D. Flad, and E. Brandt A Chondroitin Sulfate Proteoglycan on Human Neutrophils Specifically Binds Platelet Factor 4 and Is Involved in Cell Activation J. Immunol., October 15, 1998; 161(8): 4347 - 4355. [Abstract] [Full Text] [PDF]
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A. Ludwig, F. Petersen, S. Zahn, O. Gotze, J.-M. Schroder, H.-D. Flad, and E. Brandt The CXC-Chemokine Neutrophil-Activating Peptide-2 Induces Two Distinct Optima of Neutrophil Chemotaxis by Differential Interaction With Interleukin-8 Receptors CXCR-1 and CXCR-2 Blood, December 1, 1997; 90(11): 4588 - 4597. [Abstract] [Full Text] [PDF]
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Z. C. Han, M. Lu, J. Li, M. Defard, B. Boval, N. Schlegel, and J. P. Caen Platelet Factor 4 and Other CXC Chemokines Support the Survival of Normal Hematopoietic Cells and Reduce the Chemosensitivity of Cells to Cytotoxic Agents Blood, April 1, 1997; 89(7): 2328 - 2335. [Abstract] [Full Text] [PDF]
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