Objective: The selenoenzyme type 2 iodothyronine 5' deiodinase (DII) catalyzes the conversion of thyroxine into its active form tri-iodothyronine (T3), modulating thyroid hormone homeostasis in a local, tissue-specific manner. The amphibian, rodent and human cDNAs encoding this enzyme have been recently cloned and expressed. At present, little information regarding the genomic structure of mammalian DII is available.
Design And Methods: The complete structure, including intron-exon junctions, of the human DII (hDII) gene was obtained by long PCR and rapid amplification of cDNA ends (RACE). Chromosomal assignment of the hDII gene was performed by fluorescence in situ hybridization using a highly specific probe.
Results And Conclusions: Our data demonstrated that hDII is a single copy gene located on chromosome 14, position 14q24.3. The gene spans over 15 kb, and the 7 kb transcript is encoded by three exons of 149 bp, 273 bp and 6.6 kb separated respectively by two 274 bp and 7.4 kb introns. A restriction map of the hDII gene is also reported. These data will help in further studies of the role of DII in the maintenance of peripheral thyroid hormone homeostasis.
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Identification of two novel splicing variants of human type II iodothyronine deiodinase mRNA.
Mol Cell Endocrinol
February 2001
Department of Pharmacology, Tokyo Women's Medical University, School of Medicine 8-1 Kawada-cho, Shinjuku-ku, 162-8666, Tokyo, Japan.
Human type II iodothyronine deiodinase (hDII) belongs to a family of selenoproteins. It catalyzes 5'-deiodination of thyroxine to generate an active thyroid hormone, 3,3',5-triiodothyronine. Two novel splice variants of hDII gene transcript; namely hDII-b and hDII-c, were identified.
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Eur J Endocrinol
August 2000
I Cattedra di Endocrinologia, Dipartimento di Medicina Sperimentale e Patologia, Università degli Studi di Roma La Sapienza, Roma, Italy.
Objective: The selenoenzyme type 2 iodothyronine 5' deiodinase (DII) catalyzes the conversion of thyroxine into its active form tri-iodothyronine (T3), modulating thyroid hormone homeostasis in a local, tissue-specific manner. The amphibian, rodent and human cDNAs encoding this enzyme have been recently cloned and expressed. At present, little information regarding the genomic structure of mammalian DII is available.
View Article and Find Full Text PDFGenomic characterization of the coding region of the human type II 5'-deiodinase gene.
Mol Cell Endocrinol
June 1998
I Cattedra di Endocrinologia, Dipartimento di Medicina Sperimentale e Patologia, Università degli studi di Roma La Sapienza, Italy.
Type II 5'-Deiodinase (5'DII) is a key element in the maintenance of peripheral thyroid hormone homeostasis through the regulation of local T4 to T3 conversion in pituitary, brain, brown adipose tissue and placenta. The cDNA containing the coding region of the human 5'DII (HDII) has been recently cloned from infant brain. In the present paper we report the genomic structure, chromosomal localization and restriction map of the coding region of HDII.
View Article and Find Full Text PDFHomo-oligomerization domains in the lethal(2)giant larvae tumor suppressor protein, p127 of Drosophila.
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Department of Developmental Genetics, Deutches Krebsforschungszentrum, Heidelberg, Germany.
The p127 tumor suppressor protein encoded by the lethal(2)giant larvae, l(2)gl, gene of Drosophila melanogaster forms high molecular mass complexes consisting predominantly of p127 molecules. To determine whether p127 can self-assemble in the absence of other binding factors, we analyzed the size of in vitro synthesized p127 by gel filtration and found that p127 is always recovered in a high molecular mass form, demonstrating that p127 can oligomerize on its own. Previous studies have revealed that p127 may contain three homo-oligomerization domains.
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