Linked Life Data

9280060

Source:http://linkedlifedata.com/resource/pubmed/id/9280060

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1997-10-6
pubmed:abstractText
The PRL receptor (PRLR) is a member of the cytokine receptor superfamily. Rats and mice express two forms of PRLR, short (SPRLR) and long (LPRLR), which differ in the length and sequence of their cytoplasmic domains. We have analyzed the ability of each form of rat PRLR to transduce lactogenic signals in a bovine mammary gland epithelial cell line. The rat PRLR forms were expressed and detected by RT-PCR, indirect immunofluorescence, and cell surface ligand binding. When the biological activity of each form of PRLR was assessed by transient transfection, we found that the long form was able to activate the beta-casein gene promoter and that the short form was inactive. Interestingly, the coexpression of both forms of PRLR resulted in a block of PRL signal to the milk protein gene promoter as a function of the concentration of the SPRLR. Similar results were obtained when LPRLR was coexpressed with totally or partially inactive tyrosine mutants of either the Nb2 form or the LPRLR form. Thus, these results suggest that the SPRLR form has at least one clear biological function, i.e. to silence lactogenic signals and to contribute to a differential and acute PRL effect in rat tissues. Furthermore, the data derived from coexpression of LPRLR and PRLR mutants confirm a crucial role of the C-terminal tyrosine residue in lactogenic signaling and the dimerization of PRLRs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1449-57
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The short form of the prolactin (PRL) receptor silences PRL induction of the beta-casein gene promoter.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale, Unité 344 Endocrinologie Moléculaire, Faculté de Médecine Necker, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't