J Med Genet

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS REGISTER


[Advanced]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this link to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Add article to my folders
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by NICHOLLS, A C
Right arrow Articles by POPE, F M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by NICHOLLS, A C
Right arrow Articles by POPE, F M
J Med Genet 2001;38:132-136 ( February )

Letters to the editor

Homozygosity for a splice site mutation of the COL1A2 gene yields a non-functional proalpha 2(I) chain and an EDS/OI clinical phenotype

The first 150 words of the full text of this article appear below.

EDITOR---Type I collagen is the major structural protein of skin, bone, tendon, ligaments, and cornea. It is a heterotrimer of two alpha 1(I) chains and one alpha 2(I) chain. Mutations in one of its two structural genes (COL1A1, COL1A2) underlie the inherited disorders osteogenesis imperfecta (OI) and Ehlers-Danlos syndrome types VIIA and B (EDS VIIA, EDS VIIB).1 Mutations which inhibit the processing of the protein precursor, procollagen, cause the ligamentous laxity and extreme joint hypermobility of EDS VII. Structural abnormalities and/or reduced production of type I collagen lead to the increased bone fragility, thin skin, blue sclerae, dentinogenesis imperfecta, and presenile deafness of osteogenesis imperfecta. The OI phenotype can vary from perinatally lethal to mild disease depending upon the nature of the mutation. Among the mild group are patients who are heterozygous for a non-functional COL1A1 allele.2-5 Homozygosity for a non-functional COL1A1 allele appears to be incompatible . . . [Full text of this article]


This article has been cited by other articles:


Home page
 J. Med. Genet.Home page
F Malfait, S Symoens, P Coucke, L Nunes, S De Almeida, and A De Paepe
Total absence of the alpha2(I) chain of collagen type I causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems.
J. Med. Genet., July 1, 2006; 43(7): e36 - e36.
[Abstract] [Full Text] [PDF]

Home page
 Rheumatology (Oxford)Home page
F. Malfait, A. J. Hakim, A. De Paepe, and R. Grahame
The genetic basis of the joint hypermobility syndromes
Rheumatology, May 1, 2006; 45(5): 502 - 507.
[Full Text] [PDF]

Home page
 J. Med. Genet.Home page
S Symoens, L Nuytinck, E Legius, F Malfait, P J Coucke, and A De Paepe
Met>Val substitution in a highly conserved region of the pro-{alpha}1(I) collagen C-propeptide domain causes alternative splicing and a mild EDS/OI phenotype
J. Med. Genet., July 1, 2004; 41(7): e96 - e96.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS REGISTER
Terms and conditions relating to subscriptions purchased online  ¦  Website terms and conditions  ¦  Privacy policy
Copyright © 2001 by the BMJ Publishing Group Ltd.