Linked Life Data

11279012

Source:http://linkedlifedata.com/resource/pubmed/id/11279012

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2001-6-18
pubmed:abstractText
The Drosophila Sprouty (SPRY) protein has been shown to inhibit the actions of epidermal growth factor and fibroblast growth factor. However, the role of mammalian SPRY proteins has not been clearly elucidated. We postulated that human Sprouty2 (hSPRY2) is an inhibitor of cellular migration and proliferation. Indeed, using stably transfected HeLa cells, which expressed hemagglutinin (HA)-tagged hSPRY2 or hSPRY2 tagged at the C terminus with red fluorescent protein, we demonstrated that hSPRY2 inhibits the migration of cells in response to serum, epidermal growth factor, fibroblast growth factor, and platelet-derived growth factor. Additionally, hSPRY2 also inhibited the growth of HeLa cells in response to serum. Previously, two C-terminal domains on hSPRY2, which are necessary for its colocalization with microtubules (residues 123-177) or translocation to membrane ruffles (residues 178-194), have been identified (Lim, J., Wong, E. S., Ong, S. H., Yusoff, P., Low, B. C., and Guy, G. R. (2000) J. Biol. Chem. 275, 32837-32845). Therefore, using TAT-tagged hSPRY2 and its mutants, we determined the role of these two C-terminal domains in the inhibition of cell migration and proliferation. Our data show that the deletion of either of these two regions in hSPRY2 abrogates its ability to modulate cell migration in response to different growth factors and proliferation in response to serum. Therefore, we conclude that hSPRY2 inhibits the actions of a number of growth factors, and its C terminus, which is homologous among various SPRY isoforms, is important in mediating its biological activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22742-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11279012-Amino Acid Sequence, pubmed-meshheading:11279012-Animals, pubmed-meshheading:11279012-Base Sequence, pubmed-meshheading:11279012-Blotting, Western, pubmed-meshheading:11279012-Cell Division, pubmed-meshheading:11279012-Cell Movement, pubmed-meshheading:11279012-Cloning, Molecular, pubmed-meshheading:11279012-DNA Primers, pubmed-meshheading:11279012-Drosophila Proteins, pubmed-meshheading:11279012-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11279012-Fluorescent Antibody Technique, pubmed-meshheading:11279012-Green Fluorescent Proteins, pubmed-meshheading:11279012-HeLa Cells, pubmed-meshheading:11279012-Humans, pubmed-meshheading:11279012-Insect Proteins, pubmed-meshheading:11279012-Luminescent Proteins, pubmed-meshheading:11279012-Membrane Proteins, pubmed-meshheading:11279012-Recombinant Fusion Proteins
pubmed:year
2001
pubmed:articleTitle
The C terminus of sprouty is important for modulation of cellular migration and proliferation.
pubmed:affiliation
Department of Pharmacology and the Vascular Biology Center of Excellence, The Health Science Center University of Tennessee, Memphis, Tennessee 38163, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't