Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-9-29
pubmed:databankReference
pubmed:abstractText
In vertebrates several proteins containing a covalently bound selenocysteine residue have been identified. Among these, selenoprotein P is the most unusual one: depending on the species, 8-12 selenocysteine residues are cotranslationally integrated into the polypeptide chain. The protein was traced in rat plasma, but its role has not been worked out so far. In order to improve our understanding on selenoprotein P we investigated its tissue-specific expression and its genomic DNA. RNA in situ hybridization analyses confirmed the liver-specific expression in mice. Selenoprotein P was also found to be expressed in testis, brain, gut, and hematopoietic cells. The murine selp gene contains five exons within 10.3 kb with a coding sequence restricted to exons 2 to 5. The complete gene including the selp promoter was sequenced. One TATA motif 38 bp upstream to exon 1 suggests transcription of selp by RNA polymerase II. Within the 1116 bp upstream of exon 1 four hepatic nuclear factor 3beta (HNF3beta) binding motifs were found, which is in line with liver-specific expression of selenoprotein P. The expression in hematopoietic cells might be due to multiple GATA-1 motifs. Two BRN-2 motifs suitable for the binding of brain-specific regulatory factors correlated to the selenoprotein P expression in the cerebellum. Selenoprotein P was also expressed in Leydig cells which could be regulated by binding proteins docking to the SRY motifs present in the promoter region.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
379
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
683-91
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Analysis of the mouse selenoprotein P gene.
pubmed:affiliation
Department of Physiological Chemistry, Technical University of Braunschweig, Germany.
pubmed:publicationType
Journal Article