Mutations in fibrillar collagens (types I, II, III, and XI), fibril‐associated collagen (type IX), and network‐forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels

@article{Kuivaniemi1997MutationsIF,
  title={Mutations in fibrillar collagens (types I, II, III, and XI), fibril‐associated collagen (type IX), and network‐forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels},
  author={Helena Kuivaniemi and Gerard Tromp and D. J. Prockop},
  journal={Human Mutation},
  year={1997},
  volume={9},
  url={https://api.semanticscholar.org/CorpusID:6890740}
}
The mutations in types I, II, III, IX, X, and XI collagens cause a wide spectrum of diseases of bone, cartilage, and blood vessels, including osteogenesis imperfecta, a variety of chondrodysplasias, types IV and VII of the Ehlers‐Danlos syndrome, and, rarely, some forms of osteoporosis, osteoarthritis, and familial aneurysms.
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Folding defects in fibrillar collagens.

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disorder correlation in patients with a lethal type II collagen mutations with analysis of genotype-phenotype COL 2 A 1 Report of five novel and one recurrent

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Type IV collagen : characterization of the COL4A5 gene, mutations in Alport syndrome, and autoantibodies in Alport and Goodpasture syndromes

The results of this work have a significant clinical value by providing for the first time complete, effective DNA-based analysis of all exon/intron and promoter regions of the COL4A5 gene in Alport syndrome and Goodpasture syndrome.

Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases.

Molecular mechanisms of junctional epidermolysis bullosa: Col 15 domain mutations decrease the thermal stability of collagen XVII.

Two novel glycine substitutions, G609D and G612R, and a splice site mutation resulting in a deletion of three Gly-X-Y amino acid triplets are described here to investigate the molecular pathomechanisms of non-PTC mutations in recombinant collagen XVII.

G76E substitution in type I collagen is the first nonlethal glutamic acid substitution in the alpha1(I) chain and alters folding of the N-terminal end of the helix.

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69 References

Mutations in collagen genes: causes of rare and some common diseases in humans

The results suggest that mutations in procollagen genes may cause a wide spectrum of both rare and common human diseases.

Osteogenesis imperfecta type III: mutations in the type I collagen structural genes, COL1A1 and COL1A2, are not necessarily responsible.

Results suggest that mutations within or near the type I collagen structural genes are not responsible for this form of OI, which is recognised in the black populations of southern Africa.

Exclusion of mutations in the gene for type III collagen (COL3A1) as a common cause of intracranial aneurysms or cervical artery dissections

The results indicated that mutations in the gene for type III procollagen (COL3A1) are not a common cause of either intracranial artery aneurysms or cervical artery dissections.

Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta.

The results suggest that there may be phenotypic and genotypic overlap between mild osteogenesis imperfecta and postmenopausal osteoporosis, and that a subset of women with post menopausal osteopsorosis may have mutations in the genes for type I procollagen.

Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II

It is reported here that cells cultured from 15 infants with OI type II synthesized both normal type I procollagen and a form that was unstable, poorly secreted and excessively modified.

Type X Collagen Multimer Assembly in Vitro Is Prevented by a Gly618 to Val Mutation in the α1(X) NC1 Domain Resulting in Schmid Metaphyseal Chondrodysplasia (*)

These studies provide the first evidence of the effect of a type X collagen mutation on protein structure and function and directly demonstrate the critical role of interactions between NC1 domains in the formation of typeX collagen multimeric structures in vitro.

Reduced amounts of cartilage collagen fibrils and growth plate anomalies in transgenic mice harboring a glycine-to-cysteine mutation in the mouse type II procollagen alpha 1-chain gene.

It is proposed that the principal consequence of the mutation is a considerable reduction in density of the typical thin cartilage collagen fibrils and that this phenomenon causes the severe disorganization of the growth plate.

Mutations that alter the primary structure of type I collagen. The perils of a system for generating large structures by the principle of nucleated growth.

It is demonstrated that the geneprotein systems for fibril-forming collagens may be the most vulnerable systems in nature to mutations that change primary structure to nucleated growth.

Osteogenesis imperfecta type I: molecular heterogeneity for COL1A1 null alleles of type I collagen.

Seven different COL1A1 gene mutations in eight unrelated families with OI type I are identified and it is demonstrated that different molecular mechanisms that have the same effect on type I collagen production result in the same clinical phenotype.

Mice lacking alpha 1 (IX) collagen develop noninflammatory degenerative joint disease.

A mouse strain lacking both isoforms of the alpha 1(IX) chain is generated and Homozygous mutant mice are viable and show no detectable abnormalities at birth but develop a severe degenerative joint disease resembling human osteoarthritis.
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