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Blood, 15 May 2006, Vol. 107, No. 10, pp. 3959-3966.
Prepublished online as a Blood First Edition Paper on February 2, 2006; DOI 10.1182/blood-2005-08-3334.
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Submitted August 17, 2005
Accepted January 7, 2006
Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter
Yvonne Helmus, Jonas Denecke, Sviatlana Yakubenia, Peter Robinson, Kerstin Luhn, Diana L Watson, Paraic J McGrogan, Dietmar Vestweber, Thorsten Marquardt, and Martin K Wild*
Max Planck Institute of Molecular Biomedicine and Institute of Cell Biology, ZMBE, University of Munster, Munster, Germany
Department of Pediatrics, University Hospital of Munster, Munster, Germany
Yorkhill NHS Trust, Royal Hospital for Sick Children, Glasgow, United Kingdom
* Corresponding author; email: wildm{at}uni-muenster.de.
Leukocyte adhesion deficiency II (LAD II, CDG IIc) is a rare congenital disease which is caused by defective fucosylation leading to immunodeficiency and psychomotor retardation. We have previously identified the genetic defect of LAD II in a patient whose Golgi GDP-fucose transporter (GFTP) bears a single amino acid exchange that renders this protein non-functional but correctly localized to the Golgi. We now report a novel dual defect by which a truncated GFTP causes the disease in a new LAD II patient. We show that the truncation renders this GFTP unable to localize to the Golgi, the compartment where it is required. Furthermore, the missing part of the GFTP can be dissected into two regions, one that is needed for Golgi localisation and one that is additionally required for the function of the GFTP. We investigated the subcellular localisation of all known defective GFTPs allowing us to divide all genetically analysed LAD II patients into two groups, one in which single amino acid exchanges in the GFTP impair its function but not its subcellular localisation, and another group with a dual defect in function and Golgi expression of the GFTP due to the absence of two important molecular regions.
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