Browsing by Subject "procollagen"

Article

The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutations

Constantinou-Deltas, Constantinos D.; VOGEL, B. E.; JEFFREY, J. J.; PROCKOP, D. J. (1987)

Previous studies demonstrated that the thermal stability of the procollagen triple helix can be assayed by digesting the protein for short periods with high concentrations of trypsin and chymotrypsin. Here we cleaved human ...

Article

Expression of type I procollagen genes.

Prockop, D. J.; Kadler, K. E.; Hojima, Y.; Constantinou-Deltas, Constantinos D.; Dombrowski, K. E.; Kuivaniemi, H.; Tromp, G.; Vogel, B. (1988)

All of the type I collagen in connective tissue is the product of one structural gene for the pro alpha 1(I) chain and another for the pro alpha 2(I) chain of type I procollagen. An intriguing question therefore is how the ...

Article

G to A polymorphism in exon 45 of the COL1A1 gene

Sokolov, B. P.; Constantinou-Deltas, Constantinos D.; Tsuneyoshi, T.; Zhuang, J.; Prockop, D. J. (1991)

Article

A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen

Constantinou-Deltas, Constantinos D.; Nielsen, K. B.; Prockop, D. J. (1989)

A fraction of the proα1(I) and proα2(I) chains in type I procollagen synthesized by the fibroblasts from a proband with a lethal variant of osteogenesis imperfecta were overmodified by posttranslational reactions. After ...

Article

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

Spotila, L. D.; Constantinou-Deltas, Constantinos D.; Sereda, L.; Ganguly, A.; Riggs, B. L.; Prockop, D. J. (1991)

Mutations in the two genes for type I collagen (COL1A1 or COL1A2) cause osteogenesis imperfecta (OI), a heritable disease characterized by moderate to extreme brittleness of bone early in life. Here we show that a 52-year-old ...

Article

Pvull polymorphism at the COL1A2 locus

Constantinou-Deltas, Constantinos D.; Spotila, L. D.; Zhuang, J.; Sereda, L.; Hanning, C.; Prockop, D. J. (1990)

Article

A sequence polymorphism in the 3′-nontranslated region of the proα1 chain of type I procollagen

Westerhausen, A. I.; Constantinou-Deltas, Constantinos D.; Prockop, D. J. (1990)

Article

A single base mutation in type I procollagen (COL1A1) that converts glycine α1-541 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

Zhuang, J.; Constantinou-Deltas, Constantinos D.; Ganguly, A.; Prockop, D. J. (1991)

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 ...

Article

A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix

Baldwin, C. T.; Constantinou-Deltas, Constantinos D.; Dumars, K. W.; Prockop, D. J. (1989)

Type I procollagen was examined in cultured skin fibroblasts from a patient with a lethal variant of osteogenesis imperfecta. About half of the pro-α chains were post-translationally overmodified and had a decreased thermal ...

Article

Somatic cell mosaicism: Another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfecta

Constantinou-Deltas, Constantinos D.; Ladda, R. L.; Prockop, D. J. (1993)

Mutations in the genes coding for the proα1 and proα2 chains of type I procollagen have been found in many patients with osteogenesis imperfecta (OI), a heritable disorder of connective tissue. The severity of the disease ...

Article

The substitution of arginine for glycine 85 of the α1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen

Deak, S. B.; Scholz, P. M.; Amenta, P. S.; Constantinou-Deltas, Constantinos D.; Levi-Minzi, S. A.; Gonzalez-Lavin, L.; Mackenzie, J. W. (1991)

We report a case of mild osteogenesis imperfecta in a 56-year-old male undergoing aortic valve replacement surgery. The primary defect in this patient was the substitution of arginine for glycine 85 in one of the two chains ...

Article

Substitution of serine for α1(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 or amino acid specific

Pack, M. A.; Constantinou-Deltas, Constantinos D.; Kalia, K.; Nielsen, K. B.; Prockop, D. J. (1989)

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 ...

Article

Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta: The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix

Tsuneyoshi, T.; Westerhausen, A.; Constantinou-Deltas, Constantinos D.; Prockop, D. J. (1991)

Two substitutions for glycine in the triple-helical domain were found in type I procollagen synthesized by skin fibroblasts from two probands with lethal osteogenesis imperfecta. One was a substitution of valine for glycine ...

Article

Type I procollagen: The gene-protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissue

Prockop, D. J.; Constantinou-Deltas, Constantinos D.; Dombrowski, K. E.; Hojima, Y.; Kadler, K. E.; Kuivaniemi, H.; Tromp, G.; Vogel, B. E. (1989)

Recent data from several laboratories have established that most variants of osteogenesis imperfecta (OI) are caused by mutations in the 2 structural genes for type I procollagen. There are 2 general reasons for the large ...