Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-181 |
Sentence |
denotes |
COL5A1 exon 14 splice acceptor mutation causes a functional null allele, haploinsufficiency of alpha 1(V) and abnormal heterotypic interstitial fibrils in Ehlers-Danlos syndrome II. |
TextSentencer_T2 |
182-285 |
Sentence |
denotes |
We studied four affected individuals from a family of three generations with Ehlers-Danlos Syndrome II. |
TextSentencer_T3 |
286-403 |
Sentence |
denotes |
Type V collagen transcripts of affected individuals were screened by reverse transcriptase-polymerase chain reaction. |
TextSentencer_T4 |
404-507 |
Sentence |
denotes |
Amplification of the exon 9-28 region of alpha1(V) yielded normal and larger products from the proband. |
TextSentencer_T5 |
508-629 |
Sentence |
denotes |
Sequencing of cDNA revealed a 100-base pair insertion from the 3'-end of intron 13 between exons 13 and 14 in one allele. |
TextSentencer_T6 |
630-730 |
Sentence |
denotes |
The genomic defect was identified as an A(-2)--> G substitution at the exon 14 splice acceptor site. |
TextSentencer_T7 |
731-830 |
Sentence |
denotes |
A cryptic acceptor site -100 nucleotide within intron 13 is used instead of the mutant splice site. |
TextSentencer_T8 |
831-916 |
Sentence |
denotes |
The insertion shifts the reading frame +1 and results in a stop codon within exon 17. |
TextSentencer_T9 |
917-1155 |
Sentence |
denotes |
The mutant transcript was much less abundant than normal allele product in untreated cultured fibroblasts but was approximately equimolar in cycloheximide-treated cells, suggesting that the mutation causes nonsense-mediated decay of mRNA. |
TextSentencer_T10 |
1156-1307 |
Sentence |
denotes |
By RNase protection experiments, the level of mutant transcript was determined to be 8% that of the normal transcript in untreated proband fibroblasts. |
TextSentencer_T11 |
1308-1436 |
Sentence |
denotes |
Relative to type I collagen, proband fibroblasts secreted only 65% of the amount of type V collagen secreted by normal controls. |
TextSentencer_T12 |
1437-1658 |
Sentence |
denotes |
Selective salt precipitation of proband secreted collagen provided supportive evidence that the alpha chain composition of type V collagen remains alpha1(V)(2)alpha2(V) even in the context of alpha1(V) haploinsufficiency. |
TextSentencer_T13 |
1659-1788 |
Sentence |
denotes |
Type V collagen incorporates into type I collagen fibrils in the extracellular matrix and is thought to regulate fibril diameter. |
TextSentencer_T14 |
1789-1951 |
Sentence |
denotes |
Transmission electron micrographs of type I collagen fibrils in a proband dermal biopsy showed greater heterogeneity in fibril diameter than in a matched control. |
TextSentencer_T15 |
1952-2080 |
Sentence |
denotes |
The proband had a greater proportion of both larger and smaller fibrils and occasional fibrils with a cauliflower configuration. |
TextSentencer_T16 |
2081-2330 |
Sentence |
denotes |
Unlike the genotype/phenotype relationship seen for type I collagen defects and osteogenesis imperfecta, the null allele in this family appears to cause clinical features similar to those seen in cases with structural alterations in type V collagen. |
T1 |
0-181 |
Sentence |
denotes |
COL5A1 exon 14 splice acceptor mutation causes a functional null allele, haploinsufficiency of alpha 1(V) and abnormal heterotypic interstitial fibrils in Ehlers-Danlos syndrome II. |
T2 |
182-285 |
Sentence |
denotes |
We studied four affected individuals from a family of three generations with Ehlers-Danlos Syndrome II. |
T3 |
286-403 |
Sentence |
denotes |
Type V collagen transcripts of affected individuals were screened by reverse transcriptase-polymerase chain reaction. |
T4 |
404-507 |
Sentence |
denotes |
Amplification of the exon 9-28 region of alpha1(V) yielded normal and larger products from the proband. |
T5 |
508-629 |
Sentence |
denotes |
Sequencing of cDNA revealed a 100-base pair insertion from the 3'-end of intron 13 between exons 13 and 14 in one allele. |
T6 |
630-730 |
Sentence |
denotes |
The genomic defect was identified as an A(-2)--> G substitution at the exon 14 splice acceptor site. |
T7 |
731-830 |
Sentence |
denotes |
A cryptic acceptor site -100 nucleotide within intron 13 is used instead of the mutant splice site. |
T8 |
831-916 |
Sentence |
denotes |
The insertion shifts the reading frame +1 and results in a stop codon within exon 17. |
T9 |
917-1155 |
Sentence |
denotes |
The mutant transcript was much less abundant than normal allele product in untreated cultured fibroblasts but was approximately equimolar in cycloheximide-treated cells, suggesting that the mutation causes nonsense-mediated decay of mRNA. |
T10 |
1156-1307 |
Sentence |
denotes |
By RNase protection experiments, the level of mutant transcript was determined to be 8% that of the normal transcript in untreated proband fibroblasts. |
T11 |
1308-1436 |
Sentence |
denotes |
Relative to type I collagen, proband fibroblasts secreted only 65% of the amount of type V collagen secreted by normal controls. |
T12 |
1437-1658 |
Sentence |
denotes |
Selective salt precipitation of proband secreted collagen provided supportive evidence that the alpha chain composition of type V collagen remains alpha1(V)(2)alpha2(V) even in the context of alpha1(V) haploinsufficiency. |
T13 |
1659-1788 |
Sentence |
denotes |
Type V collagen incorporates into type I collagen fibrils in the extracellular matrix and is thought to regulate fibril diameter. |
T14 |
1789-1951 |
Sentence |
denotes |
Transmission electron micrographs of type I collagen fibrils in a proband dermal biopsy showed greater heterogeneity in fibril diameter than in a matched control. |
T15 |
1952-2080 |
Sentence |
denotes |
The proband had a greater proportion of both larger and smaller fibrils and occasional fibrils with a cauliflower configuration. |
T16 |
2081-2330 |
Sentence |
denotes |
Unlike the genotype/phenotype relationship seen for type I collagen defects and osteogenesis imperfecta, the null allele in this family appears to cause clinical features similar to those seen in cases with structural alterations in type V collagen. |