Genetic Disorders of Collagen Metabolism

Hollister, David W.; Byers, Peter H.; Holbrook, Karen A.

doi:10.1007/978-1-4615-8315-8_1

Cited by 45 publications

(24 citation statements)

References 220 publications

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“…All the fragments detected with the genomic probe were accounted for by the linear map developed from overlapping phage clones of the human proa2(I) gene (19). Since the intervening and flanking sequences of highly homologous genes, such as the two a-globin genes (27) (28)(29)(30). However, it has been difficult to generate definitive data about the molecular defects, because of the large size of both the genes and the proteins.…”

Section: Introductionmentioning

confidence: 99%

Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta.

Tsipouras¹,

Myers²,

Ramirez³

et al. 1983

J. Clin. Invest.

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A B S T R A C T One cloned complementary DNA and one genomnic subclone were used to detect restriction fragment length polymorphism associated with the proa2(I) gene for human type I procollagen. The restriction fragments obtained from examination of 30-122 chromosomes confirmed previous indications that the proa2(I) gene is found in a single copy in the human haploid genome. One highly polymorphic site was detected with EcoRI in the 5'-half of the gene. The restriction site polymorphism at the site had an allelic frequency of 0.38, and it generated two fragments of 10.5 and 3.5 kilobase in homozygous individuals. The restriction fragment length polymorphism generated at the EcoRI site was used to study affected and nonaffected individuals in four generations of a family with an autosomal dominant form of osteogenesis imperfecta. The data demonstrated a linkage of the phenotype to a proa2(I) allele with a lod score of 2.41 at a recombination fraction (0) of 0. The data therefore provided presumptive evidence that osteogenesis imperfecta in this family is caused by a mutation in the proa2(I) gene or some contiguous region of the genome. The relatively high frequency of polymorphism at the EcoRI site makes it useful for studying a broad range of genetic disorders in which mutations in type I procollagen are suspected. In addition, the polymorphic site should provide useful markers for linkage

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Section: Introductionmentioning

confidence: 99%

Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta.

Tsipouras¹,

Myers²,

Ramirez³

et al. 1983

J. Clin. Invest.

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“…Most forms of osteogenesis imperfecta (OI)' are due to structural abnormalities in or decreased production of type I collagen (1)(2)(3). Studies of collagens synthesized by cultured fibroblasts from different patients with 01 type I (4-6), 01 type 11 (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17), and 01 type III (18)(19)(20)(21)(22) have demonstrated evidence of mutations in the proal(I) and proa2(I) genes of type I collagen.…”

Section: Introductionmentioning

confidence: 99%

Osteogenesis imperfecta type IV. Biochemical confirmation of genetic linkage to the pro alpha 2(I) gene of type I collagen.

Wenstrup¹,

Tsipouras²,

Byers³

1986

J. Clin. Invest.

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Fibroblasts from two affected members of a large pedigree in which osteogenesis imperfecta (01) type IV is genetically linked to the proa2(I) gene of type I collagen synthesize two populations of proa2(I) chains. One population is normal; the second population appears to have a deletion of about 10 amino acid residues from the middle of the triple helical domain. The mutation in proa2(I) causes increased posttranslational modification in the amino-terminal half of some proal(I) chains, lowers the melting temperature of type I collagen molecules that incorporate a mutant proa2(I) chain, and prevents or delays the secretion of those molecules from fibroblasts in cell culture. On the basis of this study and linkage studies in additional families, it appears that the 01 type IV phenotype is often the result of heterozygosity for mutations in proa2(I) that alter the triple helical structure of type I collagen.

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“…However, several general features of the diseases are beginning to emerge. One, stressed above, is that similar mutations which alter the (2)(3)(4)(5). The same observations begin to establish a "functional topology" (Fig.…”

Section: Discussionmentioning

confidence: 67%

“…In many instances the discoveries have provided the basis for new DNA tests for the early, prenatal diagnosis of serious forms of the diseases. Recent work on human genes for collagen is proceeding along a similar path and has now defined the molecular basis for a number of heritable disorders of connective tissue (for reviews, see references [1][2][3][4][5]. It is very likely that DNA tests for the prenatal diagnosis of a few of these conditions will soon be available.…”

Section: Introductionmentioning

confidence: 99%

Mutations in collagen genes. Consequences for rare and common diseases.

Prockop¹

1985

J. Clin. Invest.

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Genetic Disorders of Collagen Metabolism

Cited by 45 publications

References 220 publications

Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta.

Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta.

Osteogenesis imperfecta type IV. Biochemical confirmation of genetic linkage to the pro alpha 2(I) gene of type I collagen.

Mutations in collagen genes. Consequences for rare and common diseases.

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