HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) 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 ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (29) Citing Articles via Google Scholar Google Scholar Articles by WINTERPACHT, A. Articles by ZABEL, B. Search for Related Content PubMed PubMed Citation Articles by WINTERPACHT, A. Articles by ZABEL, B.

A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia

¹ Children's Hospital, University of Mainz, D-55101 Mainz
² Institute of Human Genetics, University of Hamburg, D-22529 Hamburg
³ Institute for Molecular Biophysics, University of Mainz, D-55128 Mainz
⁴ St. Hedwig Hospital, D-93006 Regensburg, Germany

Winterpacht, Andreas, Katja Hilbert, Christiane Stelzer, Thorsten Schweikardt, Heinz Decker, Hugo Segerer, Jürgen Spranger, and Bernhard Zabel. A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia. Physiol. Genomics 2: 9–12, 2000.—Fibroblast growth factor receptor 3 (FGFR3) is a glycoprotein that belongs to the family of tyrosine kinase receptors. Specific mutations in the FGFR3 gene are associated with autosomal dominant human skeletal disorders such as hypochondroplasia, achondroplasia, and thanatophoric dysplasia. Hypochondroplasia (HCH), the mildest form of this group of short-limbed dwarfism disorders, results in ~60% of cases from a mutation in the intracellular FGFR3-tyrosine kinase domain. The remaining cases may either be caused by defects in other FGFR gene regions or other yet unidentified genes. We describe a novel HCH mutation, the first found outside the common mutation hot spot of this condition. This point mutation, an N328I exchange in the extracellular Ig domain III of the receptor, seems to be unique as it affects a putative N-glycosylation site that is conserved between different FGFRs and species. The amino acid exchange itself most probably has no impact on the three-dimensional structure of the receptor domain, suggesting that the phenotype is the result of altered receptor glycosylation and its pathophysiological consequences.

glycosylation; tyrosine kinase receptor; chondrodysplasia; glycoprotein

This article has been cited by other articles:

				L. Castro-Feijoo, L. Loidi, A. Vidal, S. Parajes, E. Roson, A. Alvarez, P. Cabanas, J. Barreiro, A. Alonso, F. Dominguez, et al. Hypochondroplasia and acanthosis nigricans: a new syndrome due to the p.Lys650Thr mutation in the fibroblast growth factor receptor 3 gene? Eur. J. Endocrinol., September 1, 2008; 159(3): 243 - 249. [Abstract] [Full Text] [PDF]

				L. Duchesne, B. Tissot, T. R. Rudd, A. Dell, and D. G. Fernig N-Glycosylation of Fibroblast Growth Factor Receptor 1 Regulates Ligand and Heparan Sulfate Co-receptor Binding J. Biol. Chem., September 15, 2006; 281(37): 27178 - 27189. [Abstract] [Full Text] [PDF]

				C. J. Robinson, N. J. Harmer, S. J. Goodger, T. L. Blundell, and J. T. Gallagher Cooperative Dimerization of Fibroblast Growth Factor 1 (FGF1) upon a Single Heparin Saccharide May Drive the Formation of 2:2:1 FGF1{middle dot}FGFR2c{middle dot}Heparin Ternary Complexes J. Biol. Chem., December 23, 2005; 280(51): 42274 - 42282. [Abstract] [Full Text] [PDF]