Linked Life Data

8928744

Source:http://linkedlifedata.com/resource/pubmed/id/8928744

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4 Pt 1
pubmed:dateCreated
1996-11-20
pubmed:databankReference
pubmed:abstractText
This study was designed to demonstrate the presence of the epidermal growth factor (EGF) receptor in the rat exorbital lacrimal gland. EGF receptor gene transcription was demonstrated 1) by reverse transcription-polymerase chain reaction analysis of lacrimal gland and acinar cells from RNA with a set of specific primers deduced from the rat EGF receptor sequence and 2) by Northern blot analysis of rat lacrimal gland mRNA. Lacrimal acinar cell preparations contain a low but detectable amount of specific 125I-EGF binding sites and efficiently internalize the ligand on binding at 37 degrees C. A sheep polyclonal antibody, directed against the human EGF receptor, detects a protein of 170 kDa by Western blot analysis of membrane proteins of the whole gland. This protein can be immunoprecipitated by the same antibody from whole gland membrane proteins as well as from solubilized acinar cells. Incubations of acinar cells in the presence of EGF results in an increased content of tyrosine-phosphorylated residues in immunoprecipitated 170-kDa protein. Taken together, these results demonstrate for the first time both EGF receptor gene transcription and protein expression in a lacrimal tissue, i.e., the rat exorbital lacrimal gland. These results also suggest a specific cellular location of the EGF receptor in a cell population contained in acinar cell preparations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C1164-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
EGF receptor mRNA and protein in rat lacrimal acinar cells: evidence of its EGF-dependent phosphotyrosilation.
pubmed:affiliation
Laboratoire de Biochimie des Transports Cellulaires, Centre National de la Recherche Scientifique, Unité de Recherche Associée 116, Université Paris-Sud, Orsay, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't