Source:http://linkedlifedata.com/resource/pubmed/id/12805933
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2003-6-13
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pubmed:databankReference | |
pubmed:abstractText |
The sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs) belong to a family of active calcium transport enzymes encoded by the SERCA1, 2, and 3 genes. In this study, we describe the complete structure of the human SERCA2 gene and its 5 -regulatory region. The hSERCA2 gene is located in chromosome 12 position q24.1 in Contig NT_009770.8, spans 70 kb, and is organized in 21 exons intervened by 20 introns. The last two exons of the pre-mRNA produce by alternatively splicing the cardiac/slow-twitch muscle-specific SERCA2a isoform and the ubiquitous SERCA2b isoform. The sequence of the proximal 225-bp regulatory region of the SERCA2 genes is 80% G+C-rich and is conserved among human, rabbit, rat, and mouse species. It contains a TATA-like-box, an E-box/USF sequence, a CAAT-box, four Sp1 binding sites, and a thyroid hormone responsive element (TRE). There are two other conserved regulatory regions located between positions -410 to -661 bp and from -919 to -1410 bp. Among the DNA cis-elements present in these two regulatory regions there are potential binding sites for: GATA-4, -5, -6, Nkx-2.5/Csx, OTF-1, USF, MEF-2, SRF, PPAR/RXR, AP-2, and TREs. Upstream from position -1.5 kb, there is no significant homology among the SERCA2 genes cloned. In addition, the human gene has several repeated sequences mainly of the Alu and L2 type located upstream from position -1.7 kb, spanning in a continuous fashion for more than 40 kb. In this study, we report the cloning of 2.4 kb of 5-regulatory region and demonstrate that the proximal promoter region is sufficient for expression in cardiac myocytes, and the region from -225 to -1232 bp contains regulatory DNA elements which down-regulate the expression of the SERCA2 gene in neonatal cardiomyocytes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP2A1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ATP2A2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Atp2a1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Atp2a2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Atp2a2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcoplasmic Reticulum...,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1537-744X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1469-83
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12805933-Alternative Splicing,
pubmed-meshheading:12805933-Animals,
pubmed-meshheading:12805933-Base Sequence,
pubmed-meshheading:12805933-Calcium-Transporting ATPases,
pubmed-meshheading:12805933-Cells, Cultured,
pubmed-meshheading:12805933-Cloning, Molecular,
pubmed-meshheading:12805933-Gene Components,
pubmed-meshheading:12805933-Gene Expression Regulation,
pubmed-meshheading:12805933-Heart Diseases,
pubmed-meshheading:12805933-Humans,
pubmed-meshheading:12805933-Molecular Sequence Data,
pubmed-meshheading:12805933-Myocytes, Cardiac,
pubmed-meshheading:12805933-Promoter Regions, Genetic,
pubmed-meshheading:12805933-RNA, Messenger,
pubmed-meshheading:12805933-Rats,
pubmed-meshheading:12805933-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:12805933-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:12805933-Thyroid Hormones,
pubmed-meshheading:12805933-Transcription, Genetic
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pubmed:year |
2002
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pubmed:articleTitle |
Sarco(endo)plasmic reticulum Ca2+-ATPase-2 gene: structure and transcriptional regulation of the human gene.
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pubmed:affiliation |
Laboratorio de Biología Molecular, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México DF. angelz@bq.unam.mx
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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