Linked Life Data

2448309

Source:http://linkedlifedata.com/resource/pubmed/id/2448309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-3-23
pubmed:databankReference
pubmed:abstractText
Using antisera raised against partially purified rabbit mammary gland prolactin receptor, we have isolated a cDNA from a T-47D human breast cancer cell expression library which encodes the putative calcium-binding protein, calcyclin. Since the protein encoded by this cDNA co-purified with the prolactin receptor, we have tentatively named it a prolactin receptor-associated protein (PRA). Hybrid selection and in vitro translation showed that the protein encoded by this cDNA was approximately 10 kDa, a result confirmed by the amino acid sequence derived after DNA sequencing analysis. The PRA gene product has significant sequence similarity to the S-100 proteins, the cystic fibrosis antigen, and p11 proteins. The PRA/calcyclin cDNA obtained from the T-47D human breast cancer cell library has 37 nucleotides more 5'-untranslated information than that of the calcyclin cDNA from human fibroblasts. Since the transcription start site for the calcyclin gene has been confirmed in fibroblasts, our data suggest that a different transcription start site may be used in the T-47D cells. Isolation and nucleotide sequencing of the rat PRA cDNA showed there was 96% predicted amino acid sequence similarity with the human PRA and confirmed the highly conserved nature of the PRA/calcyclin gene between species. The PRA is expressed in most but not all human breast cancer cell lines, e.g. MCF 7. Northern analyses of RNAs from rat tissue indicated that PRA mRNA levels vary widely. They are low in the liver, brain, testes, and ovary, moderate in skeletal muscle, and high in the lung, kidney, and uterus. The availability of prolactin receptor-positive human breast cancer cell lines, which do (T-47D) and do not (MCF 7) express the PRA/calcyclin gene, will allow the investigation of the role, if any, of PRA in prolactin action.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2397-401
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum.
pubmed:affiliation
Department of Physiology, University of Manitoba, Winnipeg, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't