Linked Life Data

17496233

Source:http://linkedlifedata.com/resource/pubmed/id/17496233

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-5-14
pubmed:abstractText
Lysophosphatidic acid (LPA) acts via binding to specific G protein-coupled receptors and has been implicated in the biology of breast cancer. Here, we characterize LPA receptor expression patterns in common established breast cancer cell lines and their contribution to breast cancer cell motility. By measuring expression of the LPA receptors LPA1, LPA2, and LPA3 with real-time quantitative PCR, we show that the breast cancer cell lines tested can be clustered into three main groups: cells that predominantly express LPA1 (BT-549, Hs578T, MDA-MB-157, MDA-MB-231, and T47D), cells that predominantly express LPA2 (BT-20, MCF-7, MDA-MB-453, and MDA-MB-468), and a third group that shows comparable expression level of these two receptors (MDA-MB-175 and MDA-MB-435). LPA3 expression was detected primarily in MDA-MB-157 cells. Using a Transwell chemotaxis assay to monitor dose response, we find that cells predominantly expressing LPA1 have a peak migration rate at 100 nM LPA that drops off dramatically at 1 microM LPA, whereas cells predominantly expressing LPA2 show the peak migration rate at 1 microM LPA, which remains high at 10 microM. Using BT-20 cells, LPA2-specific small interfering RNA, and C3 exotransferase, we demonstrate that LPA2 can mediate LPA-stimulated cell migration and activation of the small GTPase RhoA. Using LPA2 small interfering RNA, exogenous expression of LPA1, and treatment with Ki16425 LPA receptor antagonist in the BT-20 cells, we further find that LPA1 and LPA2 cooperate to promote LPA-stimulated chemotaxis. In summary, our results suggest that the expression of both LPA1 and LPA2 may contribute to chemotaxis and may permit cells to respond optimally to a wider range of LPA concentrations, thus revealing a new aspect of LPA signaling.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0363-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
292
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C1927-33
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed-meshheading:17496233-Breast Neoplasms, pubmed-meshheading:17496233-Cell Line, Tumor, pubmed-meshheading:17496233-Chemotaxis, pubmed-meshheading:17496233-Dose-Response Relationship, Drug, pubmed-meshheading:17496233-Enzyme Activation, pubmed-meshheading:17496233-Female, pubmed-meshheading:17496233-Gene Expression Regulation, Neoplastic, pubmed-meshheading:17496233-Humans, pubmed-meshheading:17496233-Isoxazoles, pubmed-meshheading:17496233-Lysophospholipids, pubmed-meshheading:17496233-Neoplasm Invasiveness, pubmed-meshheading:17496233-Propionic Acids, pubmed-meshheading:17496233-Protein Isoforms, pubmed-meshheading:17496233-RNA, Messenger, pubmed-meshheading:17496233-RNA, Small Interfering, pubmed-meshheading:17496233-RNA Interference, pubmed-meshheading:17496233-Receptors, Lysophosphatidic Acid, pubmed-meshheading:17496233-Signal Transduction, pubmed-meshheading:17496233-rho GTP-Binding Proteins
pubmed:year
2007
pubmed:articleTitle
LPA2 (EDG4) mediates Rho-dependent chemotaxis with lower efficacy than LPA1 (EDG2) in breast carcinoma cells.
pubmed:affiliation
Department of Surgery, University of Texas Medical Branch, 301 Univ. Blvd., Galveston, TX 77555-0525, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural