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osteogenesis imperfecta/protease
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Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion.
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In this paper we describe a mild moderate form of osteogenesis imperfecta caused by a point mutation in COL1A1 which converted glycine 85 to valine. The valine substitution introduced into the triple-helical domain of type-I collagen a conformational perturbation causing susceptibility to digestive
Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific.
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Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier side chains for glycine residues and decreased the melting temperature of the
A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR.
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Skin fibroblasts from a proband with a lethal variant of osteogenesis imperfecta synthesized both apparently normal type I procollagen and a type I procollagen that had slow electrophoretic mobility because of posttranslational overmodifications. The thermal unfolding of the collagen molecules as
Concepts in collagen biochemistry: evidence that collagenopathies underlie osteogenesis imperfecta.
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Collagen, the principal structural macromolecule of the body, is expressed as a family of genetically distinct protein molecules. Two main subfamilies are emerging, the interstitial, fibrillar collagens (Types I, II and III) and the cell-associated or basement membrane collagens (Types IV and V).
A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta.
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A proband with lethal osteogenesis imperfecta has been investigated for the causative defect at the levels of collagen protein, mRNA, and DNA. Analysis of type I collagen synthesized by the proband's fibroblasts showed excessive post-translational modification of alpha 1(I) chains along the entire
Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.
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The clinical severity of Osteogenesis Imperfecta (OI), also known as the brittle bone disease, relates to the extent of conformational changes in the collagen triple helix induced by Gly substitution mutations. The lingering question is why Gly substitutions at different locations of collagen cause
Incorporation of type I collagen molecules that contain a mutant alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis imperfecta.
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To understand more directly the tissue defect in osteogenesis imperfecta (OI), bone matrix was analyzed from an infant with lethal OI (type II) of defined mutation (collagen alpha 2(I)Gly580-->Asp). Pepsin-solubilized alpha 1(I) and alpha 2(I) chains and derived CNBr-peptides migrated more slowly on
Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta.
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Herein, we have studied a consanguineous Egyptian family with two children diagnosed with severe autosomal recessive osteogenesis imperfecta (AR-OI) and a large umbilical hernia. Homozygosity mapping in this family showed lack of linkage to any of the previously known AR-OI genes, but revealed a
Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta.
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The kinetics of triple helix formation of procollagen I were measured in normal human fibroblast cultures and cell strains from six patients with osteogenesis imperfecta (OI), a heritable connective tissue disorder. After a 4-minute pulse-labelling with [35S]methionine, the appearance of
Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta.
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Osteogenesis imperfecta (OI) is characterized by bone fragility and fractures that may be accompanied by bone deformity, dentinogenesis imperfecta, short stature, and shortened life span. About 90% of individuals with OI have dominant mutations in the type I collagen genes COL1A1 and COL1A2.
Hsp47 as a collagen-specific molecular chaperone.
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Heat shock protein (HSP) 47 is a 47 kDa collagen-binding glycoprotein localized in the endoplasmic reticulum (ER). It belongs to the serpin family and contains a serpin loop, although it does not have serine protease inhibitory activity. The induction of Hsp47 by heat shock is regulated by a heat
Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.
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Cultured skin fibroblasts from two probands with lethal variants of osteogenesis imperfecta synthesized type I procollagen that was posttranslationally over-modified. Analysis of cDNAs and genomic DNAs from the two probands demonstrated that proband I had a single-base mutation that converted the
Inherited disorders of collagen gene structure and expression.
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As a result of investigations completed during the last 15 years, the molecular bases of most form of osteogenesis imperfecta (OI) and of some forms of the Ehlers-Danlos syndrome (EDS) are now known. Most forms of OI result from point mutations in the genes (COL1A1 and COL1A2) that encode the chains
A 5' splice site mutation affecting the pre-mRNA splicing of two upstream exons in the collagen COL1A1 gene. Exon 8 skipping and altered definition of exon 7 generates truncated pro alpha 1(I) chains with a non-collagenous insertion destabilizing the triple helix.
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A heterozygous de novo G to A point mutation in intron 8 at the +5 position of the splice donor site of the gene for the pro alpha 1(I) chain of type I procollagen, COL1A1, was defined in a patient with type IV osteogenesis imperfecta. The splice donor site mutation resulted not only in the skipping
Potential modifier role of the R618Q variant of proalpha2(I)collagen in type I collagen fibrillogenesis: in vitro assembly analysis.
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An arginine to glutamine substitution in the triple helix of proalpha2(I)collagen (R618Q) was first reported in a patient with a variant of Marfan syndrome and later identified in conjunction with a second mutation in a patient with osteogenesis imperfecta (OI). The presence of the R618Q
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