1984
DOI: 10.1073/pnas.81.14.4524
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Nuclease S1 mapping of a homozygous mutation in the carboxyl-propeptide-coding region of the pro alpha 2(I) collagen gene in a patient with osteogenesis imperfecta.

Abstract: The molecular defect in a patient with a moderately severe form of osteogenesis imperfecta was characterized by nuclease S1 mapping. Single-stranded 5' and 3' endlabeled DNA probes coding for 80% of the carboxyl-propeptide of the proa2(I) collagen gene were hybridized to mRNA isolated from cultured fibroblasts of the patient and his parents. Nuclease S1 digestion revealed a homozygous mutation in the patient and a heterozygous pattern in the consanguineous parents. As a result of the defect in the gene, none o… Show more

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Cited by 67 publications
(25 citation statements)
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“…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. There is less information regarding the biochemical basis of 01 type IV, which differs clinically from the other relatively mild autosomal dominant OI phenotype, 01 type I.…”
Section: Introductionmentioning
confidence: 99%
“…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. There is less information regarding the biochemical basis of 01 type IV, which differs clinically from the other relatively mild autosomal dominant OI phenotype, 01 type I.…”
Section: Introductionmentioning
confidence: 99%
“…The data on these two patients (28)(29)(30), both with the clinical symptoms of osteogenesis imperfecta, indicate that structural changes of the carboxyl-terminal propeptides can change either processing of the protein or association of the proa-chains. In one incompletely studied variant (28), an alteration of the carboxylpropeptides apparently led to increased addition of a mannoserich carbohydrate to the carboxyl-terminal propeptide and decreased the solubility of the protein.…”
Section: Genes For Procollagensmentioning
confidence: 99%
“…In one incompletely studied variant (28), an alteration of the carboxylpropeptides apparently led to increased addition of a mannoserich carbohydrate to the carboxyl-terminal propeptide and decreased the solubility of the protein. In a much more fully defined variant (29)(30)(31), a mutation that altered the structure of the carboxy-terminal propeptides was shown to prevent association of proa2 chains with proal chains (31). The mutation was shown to be a deletion of four base pairs which changed the reading frame of the carboxyl-propeptide of the proa2 chain (29,30).…”
Section: Genes For Procollagensmentioning
confidence: 99%
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“…For example, dentinogenesis imperfecta was seen in two thirds of families with type IV osteogenesis imperfecta,'2 and more than 10 wormian bones arranged in a mosaic pattern were found in all patients with osteogenesis imperfecta after the neonatal period.' 3 In doubtful cases of suspected non-accidental fractures careful radiological examination of the skull with both lateral and Townes views may be advisable with repeat examination of neonates in later infancy. The absence of wormian bones is strong evidence against osteogenesis imperfecta.…”
Section: B L Hallidaymentioning
confidence: 99%