SEARCH:   Advanced

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. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: 2005-08-3334v1 107/10/3959    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Helmus, Y. Articles by Wild, M. K. Search for Related Content PubMed PubMed Citation Articles by Helmus, Y. Articles by Wild, M. K. Related Collections Cell Adhesion and Motility Clinical Trials and Observations Immunobiology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter Yvonne Helmus, Jonas Denecke, Sviatlana Yakubenia, Peter Robinson, Kerstin Lühn, Diana L. Watson, Paraic J. McGrogan, Dietmar Vestweber, Thorsten Marquardt, and Martin K. Wild From the Max Planck Institute of Molecular Biomedicine and Institute of Cell Biology, Zentrum für Molekularbiologie der Entzündung (ZMBE), University of Münster, Münster, Germany; Department of Pediatrics, University Hospital of Münster, Münster, Germany; and Yorkhill National Health Service (NHS) Trust, Royal Hospital for Sick Children, Glasgow, United Kingdom. Leukocyte adhesion deficiency II (LAD II) is a rare congenital disease caused by defective fucosylation leading to immuno-deficiency 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 nonfunctional 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 2 regions, one that is needed for Golgi localization and one that is additionally required for the function of the GFTP. We investigated the subcellular localization of all known defective GFTPs allowing us to divide all genetically analyzed LAD II patients into 2 groups, one in which single amino acid exchanges in the GFTP impair its function but not its subcellular localization, and another group with a dual defect in function and Golgi expression of the GFTP due to the absence of 2 important molecular regions. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. C. Hellbusch, M. Sperandio, D. Frommhold, S. Yakubenia, M. K. Wild, D. Popovici, D. Vestweber, H.-J. Grone, K. von Figura, T. Lubke, et al. Golgi GDP-fucose Transporter-deficient Mice Mimic Congenital Disorder of Glycosylation IIc/Leukocyte Adhesion Deficiency II J. Biol. Chem., April 6, 2007; 282(14): 10762 - 10772. [Abstract] [Full Text] [PDF] B. Ma, J. L. Simala-Grant, and D. E. Taylor Fucosylation in prokaryotes and eukaryotes Glycobiology, December 1, 2006; 16(12): 158R - 184R. [Abstract] [Full Text] [PDF] W. Zhao, T.-L. L. Chen, B. M. Vertel, and K. J. Colley The CMP-sialic Acid Transporter Is Localized in the Medial-Trans Golgi and Possesses Two Specific Endoplasmic Reticulum Export Motifs in Its Carboxyl-terminal Cytoplasmic Tail J. Biol. Chem., October 13, 2006; 281(41): 31106 - 31118. [Abstract] [Full Text] [PDF]

	Blood Online is supported in part by Genentech BioOncology and Biogen Idec
	Copyright © 2006 by American Society of Hematology         Online ISSN: 1528-0020