Source:http://linkedlifedata.com/resource/pubmed/id/16358725
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2005-12-19
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| pubmed:abstractText |
A collection of DNA samples obtained from primary open-angle glaucoma (POAG) patients from St. Petersburg was analyzed for single-strand conformation polymorphism (SSCP) to reveal sequence variants in exon 3 of the myocilin gene (MYOC/TIGR) and in exons 4 and 5 of the optineurin gene (OPTN), where most of the mutations revealed worldwide are located. The Q368X mutation (c. 1102 C --> T) in exon 3 of MYOC/TIGR was detected in 1.2% (2/170) of the POAG patients from St. Petersburg, i.e., with the frequency close to that observed in other world populations. Three known polymorphisms in exon 3 of MYOC/TIGR, Y347Y (c. 1041 T --> C) (12.4%), T325T (c. 975 G --> A) (0.6%), and K398R (c. 1193 A --> G) (0.6%) were also detected. No statistically significant differences in frequencies of these polymorphisms were revealed between the POAG patient and control groups. The L41L polymorphism (c. 433 G --> A) in exon 4 of OPTN was detected in 2.9% of probands and in 1% of controls. The frequency of heterozygotes for the M98K polymorphism (c. 603 T --> A) in the OPTN exon 5 was statistically significantly higher (P = 0.036; Fisher's exact test) among the POAG patients (6.5%) than among the controls (1%). In the sample examined the E50K mutation, typical of the patients with pseudonormal intraocular pressure glaucoma, was not found.
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| pubmed:language |
rus
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/OPTN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIIA,
http://linkedlifedata.com/resource/pubmed/chemical/trabecular meshwork-induced...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0016-6758
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
41
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1567-74
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16358725-Amino Acid Substitution,
pubmed-meshheading:16358725-Case-Control Studies,
pubmed-meshheading:16358725-Cytoskeletal Proteins,
pubmed-meshheading:16358725-DNA Mutational Analysis,
pubmed-meshheading:16358725-Exons,
pubmed-meshheading:16358725-Eye Proteins,
pubmed-meshheading:16358725-Female,
pubmed-meshheading:16358725-Gene Frequency,
pubmed-meshheading:16358725-Glaucoma, Open-Angle,
pubmed-meshheading:16358725-Glycoproteins,
pubmed-meshheading:16358725-Heterozygote,
pubmed-meshheading:16358725-Humans,
pubmed-meshheading:16358725-Male,
pubmed-meshheading:16358725-Pedigree,
pubmed-meshheading:16358725-Point Mutation,
pubmed-meshheading:16358725-Polymorphism, Single-Stranded Conformational,
pubmed-meshheading:16358725-Risk Factors,
pubmed-meshheading:16358725-Transcription Factor TFIIIA
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| pubmed:year |
2005
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| pubmed:articleTitle |
[Mutations and polymorphisms in the genes for myocilin and optineur in as the risk factors of primary open-angle glaucoma].
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| pubmed:publicationType |
Journal Article,
English Abstract
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