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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1991-2-14
|
| pubmed:abstractText |
Two different mutations in the c-erbA beta thyroid hormone receptor have recently been reported as genetic abnormalities responsible for the syndrome of generalized thyroid hormone resistance (GTHR). We have now found in a third kindred, D, in which GTHR is inherited as a dominant disease, a new point mutation in the T3-binding domain of c-erbA beta. A guanine to cytosine base substitution at nucleotide position 1305, which altered codon-335 from glutamine (CAG) to histidine (CAC), was found in one allele of 10 affected members and was not found in 6 unaffected members. This C-1305 sequence was not present in 106 random alleles, indicating that it was a mutation in c-erbA beta, and it was tightly linked to GTHR in kindred D, with a maximum logarithm of the odds score of 4.19 at a recombination fraction of 0. The tight linkage result confirms that GTHR maps to the c-erbA beta locus in multiple kindreds. In view of the tight linkage between the C-1305 mutation and GTHR, and that this mutation is a nonconservative alteration in a crucial region of the T3-binding domain, it is probably the genetic defect in kindred D responsible for GTHR. The kindred D receptor appears to result in a different phenotype of tissue resistance compared to the previously reported kindred. A receptor with a mutation in the carboxy-terminus of c-erbA beta.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CAGCTG-specific type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Cytosine,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, Type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Thyrotropin-Releasing Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Triiodothyronine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-972X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
72
|
| pubmed:geneSymbol |
c-erbA&bgr;
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
32-8
|
| pubmed:dateRevised |
2008-8-19
|
| pubmed:meshHeading |
pubmed-meshheading:1846005-Base Sequence,
pubmed-meshheading:1846005-Binding Sites,
pubmed-meshheading:1846005-Cytosine,
pubmed-meshheading:1846005-Deoxyribonucleases, Type II Site-Specific,
pubmed-meshheading:1846005-Drug Resistance,
pubmed-meshheading:1846005-Endocrine System Diseases,
pubmed-meshheading:1846005-Female,
pubmed-meshheading:1846005-Humans,
pubmed-meshheading:1846005-Lod Score,
pubmed-meshheading:1846005-Male,
pubmed-meshheading:1846005-Molecular Sequence Data,
pubmed-meshheading:1846005-Mutation,
pubmed-meshheading:1846005-Pedigree,
pubmed-meshheading:1846005-Pituitary Gland,
pubmed-meshheading:1846005-Proto-Oncogene Proteins,
pubmed-meshheading:1846005-Receptors, Thyroid Hormone,
pubmed-meshheading:1846005-Syndrome,
pubmed-meshheading:1846005-Thyroid Hormones,
pubmed-meshheading:1846005-Thyrotropin-Releasing Hormone,
pubmed-meshheading:1846005-Triiodothyronine
|
| pubmed:year |
1991
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| pubmed:articleTitle |
A new point mutation in the 3,5,3'-triiodothyronine-binding domain of the c-erbA beta thyroid hormone receptor is tightly linked to generalized thyroid hormone resistance.
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| pubmed:affiliation |
Department of Medicine, East Carolina University School of Medicine, Greenville, North Carolina 27858-4354.
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| pubmed:publicationType |
Journal Article
|