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Molecular and Cellular Biology, April 2003, p. 2564-2576, Vol. 23, No. 7
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.7.2564-2576.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Myeloid Cell Function in MRP-14 (S100A9) Null Mice

Josie A. R. Hobbs, Richard May,{dagger} Kiki Tanousis, Eileen McNeill, Margaret Mathies,{ddagger} Christoffer Gebhardt,§ Robert Henderson, Matthew J. Robinson, and Nancy Hogg*

Leukocyte Adhesion Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, London WC2A 3PX, United Kingdom,

Received 3 June 2002/ Returned for modification 31 July 2002/ Accepted 7 January 2003

Myeloid-related protein 14 (MRP-14) and its heterodimeric partner, MRP-8, are cytosolic calcium-binding proteins, highly expressed in neutrophils and monocytes. To understand the function of MRP-14, we performed targeted disruption of the MRP-14 gene in mice. MRP-14-/- mice showed no obvious phenotype and were fertile. MRP-8 mRNA but not protein is present in the myeloid cells of these mice, suggesting that the stability of MRP-8 protein is dependent on MRP-14 expression. A compensatory increase in other proteins was not detected in cells lacking MRP-8 and MRP-14. Although the morphology of MRP-14-/- myeloid cells was not altered, they were significantly less dense. When Ca2+ responses were investigated, there was no change in the maximal response to the chemokine MIP-2. At lower concentrations, however, there was reduced responsiveness in MRP-14-/- compared with MRP-14+/+ neutrophils. This alteration in the ability to flux Ca2+ did not impair the ability of the MRP-14-/- neutrophils to respond chemotactically to MIP-2. In addition, the myeloid cell functions of phagocytosis, superoxide burst, and apoptosis were unaffected in MRP-14-/- cells. In an in vivo model of peritonitis, MRP-14-/- mice showed no difference from wild-type mice in induced inflammatory response. The data indicate that MRP-14 and MRP-8 are dispensable for many myeloid cell functions.

* Corresponding author. Mailing address: Leukocyte Adhesion Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, London WC2A 3PX, United Kingdom. Phone: 44 20 7269 3255. Fax: 44 20 7269 3093. E-mail: nancy.hogg{at}cancer.org.uk.

{dagger} Present address: Cambridge Antibody Technology, Melbourn SG8 6JJ, United Kingdom.

{ddagger} Present address: W. M. Keck Science Center, The Claremont Colleges, Claremont, CA 91711.

§ Present address: Division of Signal Transduction and Growth Control, German Cancer Research Centre, 69120 Heidelberg, Germany.

Present address: Immune Cell Biology, National Institute of Medical Research, Mill Hill, London NW7 1AA, United Kingdom

Molecular and Cellular Biology, April 2003, p. 2564-2576, Vol. 23, No. 7
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.7.2564-2576.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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