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Rheumatology Advance Access originally published online on September 11, 2009
Rheumatology 2009 48(12):1614-1615; doi:10.1093/rheumatology/kep254
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© The Author 2009. Published by Oxford University Press on behalf of the British Society for Rheumatology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Letters to the Editor

No evidence for association of the systemic lupus erythematosus-associated ITGAM variant, R77H, with rheumatoid arthritis in the Caucasian population

Amanda J. Phipps-Green1, Ruth K. G. Topless1, Marilyn E. Merriman1, Nicola Dalbeth2, Peter J. Gow3, Andrew A. Harrison4, John Highton5, Peter B. B. Jones2, Lisa K. Stamp6, Pille Harrison7, Bryan P. Wordsworth7 and Tony R. Merriman1

1Department of Biochemistry, University of Otago, Dunedin, 2Department of Medicine, University of Auckland, 3Department of Rheumatology, Middlemore Hospital, Auckland, 4Department of Medicine, University of Otago, Wellington, 5Department of Medicine, University of Otago, Dunedin, 6Department of Medicine, University of Otago, Christchurch, New Zealand and 7Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, Nuffield Orthopaedic Centre, Oxford, UK

Correspondence to: Tony R. Merriman, Department of Biochemistry, University of Otago, PO Box 56, Dunedin 9054, New Zealand. E-mail: tony.merriman@otago.ac.nz

The first 10% of the full text of this article appears below.

SIR, A non-synonymous integrin-{alpha}-M (ITGAM) variant (R77H) confers a strong risk for SLE in Caucasian, African and Hispanic populations [odds ratio (OR)meta = 1.83] [1, 2]. ITGAM encodes the {alpha}-chain subunit of integrin-{alpha}Mβ2, a cell surface receptor expressed predominantly on monocytes and neutrophils, which mediates activation, adhesion and migration of leucocytes through the endothelium, as well as phagocytosis of complement-coated particles, and neutrophil apoptosis [3]. Interaction of integrin-{alpha}Mβ2 with intercellular adhesion molecules (ICAMs) mobilizes leucocytes to sites . . . [Full Text of this Article]


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