Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-5-24
pubmed:databankReference
pubmed:abstractText
A clone encoding the putative copper chaperone protein Sheep Atx1 Homologue (SAH) was isolated from a sheep liver cDNA library. The 466-bp cDNA encoded a predicted protein of 68 amino acids, with 44 and 81% amino acid identity to the yeast Atx1 and human Atox1 copper chaperone proteins, respectively. The characteristic MTCxxC and KTGK motifs were conserved in SAH. Northern blot analysis revealed an abundant 0.5-kb mRNA in all tissues examined. Elevated hepatic copper content did not affect the level of SAH mRNA in the liver. Analysis of SAH mRNA in the developing liver revealed low levels of expression in the foetal period, with a steady increase to adult levels occurring during development. In vitro two-hybrid analysis demonstrated SAH interacted with the amino terminal portion of the sheep Wilson's disease protein (ATP7B). The extent of this interaction was significantly reduced by the addition of the copper chelator bathocuproine disulfonic acid to the media. These results suggest SAH is a functional copper chaperone that is able to interact with ATP7B in a copper-dependent manner to facilitate copper transport into the secretory pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
1490
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Identification of the copper chaperone SAH in Ovis aries: expression analysis and in vitro interaction of SAH with ATP7B.
pubmed:affiliation
The Murdoch Institute for Research into Birth Defects, Royal Children's Hospital, Parkville, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't