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Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene detects a mutation that results in the substitution of glycine 1009 to valine and causes severe Ehlers-Danlos syndrome type IV

1994; Wiley; Volume: 3; Issue: 3 Linguagem: Inglês

10.1002/humu.1380030315

1098-1004

Lieve Nuytinck, Anne De Paepe, Jean‐Pierre Renard, Filip Adriaens, Jules G. Leroy,

Wnt/β-catenin signaling in development and cancer

Human MutationVolume 3, Issue 3 p. 268-274 Research Article Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene detects a mutation that results in the substitution of glycine 1009 to valine and causes severe Ehlers–Danlos syndrome type IV Lieve Nuytinck, Lieve Nuytinck Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorAnne De Paepe, Corresponding Author Anne De Paepe Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorJean-Pierre Renard, Jean-Pierre Renard Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorFilip Adriaens, Filip Adriaens Maria Hospital Popering, Belgium; Fax: 32-9-240-4970Search for more papers by this authorJules Leroy, Jules Leroy Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this author Lieve Nuytinck, Lieve Nuytinck Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorAnne De Paepe, Corresponding Author Anne De Paepe Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorJean-Pierre Renard, Jean-Pierre Renard Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this authorFilip Adriaens, Filip Adriaens Maria Hospital Popering, Belgium; Fax: 32-9-240-4970Search for more papers by this authorJules Leroy, Jules Leroy Centre for Medical Genetics, University Hospital Gent, B-9000 Gent, Belgium; Fax: 32-9-240-4970Search for more papers by this author First published: 1994 https://doi.org/10.1002/humu.1380030315Citations: 5AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract A single base mismatch was detected by single-strand conformation polymorphism (SSCP) of the collagen type III gene in a patient with Ehlers-Danlos syndrome type IV. The patient's fibroblasts secreted both normal and slowly migrating type III procollagen molecules. Two-dimensional CNBr peptide mapping suggested that the defect was localised in the CB9 peptide or the C-propeptide region of the α1(III)-chain. Analysis of a set of restriction-endonuclease-digested fragments of an amplified cDNA sequence encoding CB9, identified a single-strand conformation polymorphism and localized it within a region of 79 bp corresponding to the carboxyl-terminal end of the CB9 peptide of the α1(III)-chain. DNA sequence analysis demonstrated that the patient was heterozygous for a point mutation converting G to T at base pair 3440 of the collagen α1,(III) cDNA resulting in the substitution of glycine with valine at amino acid position 1009 of the α1(III)-chain. The mutation in this patient lies within a region of mutations at the carboxyl-terminal end of the type III collagen α-helix which all produce a severe "acrogeric" form of EDS IV. © 1994 Wiley-Liss, Inc. Citing Literature Volume3, Issue31994Pages 268-274 RelatedInformation