Linked Life Data

2897363

Source:http://linkedlifedata.com/resource/pubmed/id/2897363

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1988-6-29
pubmed:abstractText
Skin fibroblasts from two affected members of a family with an autosomal dominant form of mild-moderate osteogenesis imperfecta produced two populations of type I collagen molecules. One population was normal and the other population contained alpha 2(I) chains which had a basic charge shift localized to a peptide from the carboxyl-terminal end of the triple-helical domain. The alpha chains in the abnormal molecules had increased post-translational modification along the entire triple-helical domain but the thermal stability was normal. We isolated a 28-kb BamHI fragment from the normal and mutant COL1A2 alleles from an affected family member. DNA sequence determination demonstrated that a single nucleotide change resulted in an arginine for glycine substitution at triple-helical position 1012, the last triple-helical glycine. These data demonstrate the stringent requirement for maintenance of the Gly-X-Y triplet sequence in type I collagen and suggest that point mutations which disrupt Gly-X-Y in alpha 2(I) produce milder clinical effects than similar mutations in alpha 1(I).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7734-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype.
pubmed:affiliation
Department of Pediatrics, University of Washington, Seattle 98195.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't