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J. Biol. Chem., Vol. 278, Issue 28, 25499-25508, July 11, 2003

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Changing the Conformation State of Cytochrome b₅₅₈ Initiates NADPH Oxidase Activation

MRP8/MRP14 REGULATION^*

Sylvie Berthier  , Marie-Hélène Paclet  , Sandra Lerouge , Florence Roux ¶, Sabrina Vergnaud , Anthony W. Coleman || and Françoise Morel  **

From the Groupe de Recherche et d'Etude du Processus Inflammatoire, Laboratoire d'Enzymologie, Centre Hospitalier Universitaire de Grenoble, BP 217, 38043 Grenoble, ^¶Laboratoire de Chimie des Protéines, Commissariat à l'Energie Atomique de Grenoble, 38054 Grenoble, and ^||Institut de Biologie et Chimie des Protéines, 69367 Lyon, France

Phagocyte NADPH oxidase generates for defense mechanisms and cellular signaling. Myeloid-related proteins MRP8 and MRP14 of the S100 family are EF-hand calcium-binding proteins. MRP8 and MRP14 were co-isolated from neutrophils on an anti-p47^phox matrix with oxidase cytosolic factors and identified by mass spectrometry. MRP8 and MRP14 are absent from Epstein-Barr virus-immortalized B lymphocytes, and, coincidentally, these cells display weak oxidase activity compared with neutrophils. MRP8/MRP14 that was purified from neutrophils enhanced oxidase turnover of B cells in vitro, suggesting that MRP8/MRP14 is involved in the activation process. This was confirmed ex vivo by co-transfection of Epstein-Barr virus-transformed B lymphocytes with genes encoding MRP8 and MRP14. In a semi-recombinant cell-free assay, recombinant MRP8/MRP14 increased the affinity of p67^phox for cytochrome b₅₅₈ synergistically with p47^phox. Moreover, MRP8/MRP14 initiated oxidase activation on its own, through a calcium-dependent specific interaction with cytochrome b₅₅₈ as shown by atomic force microscopy and a structure-function relationship investigation. The data suggest that the change of conformation in cytochrome b₅₅₈, which initiates the electron transfer, can be mediated by effectors other than oxidase cytosolic factors p67^phox and p47^phox. Moreover, MRP8/MRP14 dimer behaves as a positive mediator of phagocyte NADPH oxidase regulation.

Received for publication, September 23, 2002 , and in revised form, April 15, 2003.

^* This work was supported by grants from the Ministère de l'Enseignement supérieur de la Recherche et Technologie, Paris, the Région Rhône Alpes, programme Mobilité Internationale Rhône-Alpes 2001, the Groupement des Entreprises Françaises dans la lutte contre le Cancer, délégation de Grenoble, the Fondation pour la Recherche Médicale, Isère, the Direction Régionale de la Recherche Clinique, and the Association Française, la Ligue Nationale contre le Cancer. We acknowledge the financial support of Mission Physique et Chimie du Vivant (CNRS) and la Fondation pour la Recherche Médicale for atomic force microscopy. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

^** To whom correspondence should be addressed: GREPI EA 2938, Lab. Enzymologie, CHU Grenoble BP 217, 38043 Grenoble, cedex 9, France. Tel.: 33-4-76-76-54-83; Fax: 33-4-76-76-56-08; E-mail: frmorel.enzymo{at}chu-grenoble.fr.

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