Recurrent substitutions of arginine 789 by cysteine in pro-alpha 1 (II) collagen chains produce spondyloepiphyseal dysplasia congenita

D Chan; J F Rogers; J F Bateman; W G Cole

Recurrent substitutions of arginine 789 by cysteine in pro-alpha 1 (II) collagen chains produce spondyloepiphyseal dysplasia congenita

J Rheumatol Suppl. 1995 Feb:43:37-8.

Authors

D Chan¹, J F Rogers, J F Bateman, W G Cole

Affiliation

¹ Department of Pediatrics, Royal Children's Hospital, Parkville, Victoria, Australia.

PMID: 7752132

Abstract

A child with typical spondyloepiphyseal dysplasia congenita had a recurrent, heterozygous substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine in exon 41 of the COL2A1 gene. The amino acid substitution involved the Y position of a Gly-X-Y triplet.

Publication types

Case Reports
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Arginine / genetics
Base Sequence
Child, Preschool
Collagen / genetics
Cysteine / genetics
Humans
Molecular Sequence Data
Mutation* / genetics
Osteochondrodysplasias / congenital
Osteochondrodysplasias / genetics*
Polymerase Chain Reaction
Procollagen / genetics*
Restriction Mapping

Substances

Procollagen
Collagen
Arginine
Cysteine