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Originally published In Press as doi:10.1074/jbc.M103106200 on June 4, 2001

J. Biol. Chem., Vol. 276, Issue 32, 29839-29845, August 10, 2001
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Kinetic Investigation of Chemokine Truncation by CD26/Dipeptidyl Peptidase IV Reveals a Striking Selectivity within the Chemokine Family*

Anne-Marie LambeirDagger §, Paul Proost, Christine DurinxDagger , Gunther Bal||, Kristel Senten||, Koen Augustyns||, Simon ScharpéDagger , Jo Van Damme, and Ingrid De MeesterDagger

From the Dagger  Laboratory of Medical Biochemistry, Department of Pharmaceutical Sciences, University of Antwerp, Universiteitsplein 1 S6, B-2610 Antwerp, Belgium,  Laboratory of Molecular Immunology, Rega Institute for Medical Research, K.U. Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium, || Laboratory of Medicinal Chemistry, Department of Pharmaceutical Sciences, University of Antwerp, Universiteitsplein 1 S4, B-2610 Antwerp, Belgium

Chemokines coordinate many aspects of leukocyte migration. As chemoattractants they play an important role in the innate and acquired immune response. There is good experimental evidence that N-terminal truncation by secreted or cell surface proteases is a way of modulating chemokine action. The localization of CD26/dipeptidyl peptidase IV on cell surfaces and in biological fluids, its primary specificity, and the type of naturally occurring truncated chemokines are consistent with such a function.

We determined the steady-state catalytic parameters for a relevant selection of chemokines (CCL3b, CCL5, CCL11, CCL22, CXCL9, CXCL10, CXCL11, and CXCL12) previously reported to alter their chemotactic behavior due to CD26/dipeptidyl peptidase IV-catalyzed truncation. The results reveal a striking selectivity for stromal cell-derived factor-1alpha (CXCL12) and macrophage-derived chemokine (CCL22). The kinetic parameters support the hypothesis that CD26/dipeptidyl peptidase IV contributes to the degradation of certain chemokines in vivo. The data not only provide insight into the selectivity of the enzyme for specific chemokines, but they also contribute to the general understanding of CD26/dipeptidyl peptidase IV secondary substrate specificity.

* This work was supported by a Byzonder Onderzoeks Fonds Project from the University of Antwerp and by Flemish Fund for Scientific Research grants (to P. P., C. D., G. B., and I. D. M.) and project G0039.01.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The amino acid sequence of this protein can be accessed through NCBI Protein Database under NCBI accession numbers P27487 (DPP IV/CD26), A28815 (RANTES), O00626 (MDC), P16619 (LD78beta ), P48061 SDF-1alpha ), P51671 (eotaxin), O14625 (I-TAC), P02778 (IP-10), and Q07325 (Mig).

§ To whom correspondence should be addressed. Tel.: 32-3-8202727; Fax: 31-3-8202745; E-mail: anne-marie.lambeir@ua.ac.be.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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