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DOI 10.1016/j.bbrc.2005.07.157
Title Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated integrin ligand
Creator/Author Humtsoe, Joseph O. [Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A and M University System Health Science Center, Texas Medical Center, 2121 W. Holcombe Blvd, Houston, TX 77030 (United States)] ; Bowling, Rodney A. [Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A and M University System Health Science Center, Texas Medical Center, 2121 W. Holcombe Blvd, Houston, TX 77030 (United States)] ; Feng, Shu [Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A and M University System Health Science Center, Texas Medical Center, 2121 W. Holcombe Blvd, Houston, TX 77030 (United States)] ; Wary, Kishore K. [Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A and M University System Health Science Center, Texas Medical Center, 2121 W. Holcombe Blvd, Houston, TX 77030 (United States)]. E-mail: kwary@ibt.tamhsc.edu
Publication Date2005 Sep 30
OSTI IdentifierOSTI ID: 20710999
Other Number(s)Journal ID: ISSN 0006-291X; BBRCA9; TRN: US05R4546025372
Resource TypeJournal Article
Resource RelationJournal: Biochemical and Biophysical Research Communications; Journal Volume: 335; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2005.07.157; PII: S0006-291X(05)01648-7; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Subject60 APPLIED LIFE SCIENCES; ANTIBODIES; CALCIUM SULFIDES; ENZYME IMMUNOASSAY; GLUTATHIONE; LIGANDS; LIPIDS; MICE; MUTANTS; PHOSPHATES; PHOSPHORYLATION; SUBSTRATES
Description/Abstract Lipid phosphate phosphohydrolase-3 (LPP3) is a cell surface protein that exhibits ectoenzyme activity. Previously, we identified human LPP3 in a functional assay of angiogenesis and showed that the Arg-Gly-Asp (RGD) motif in the proposed second extracellular domain interacts with a subset of integrins to mediate cell-cell adhesion. In contrast to the RGD domain of human LPP3, murine Lpp3 contains a variant sequence, Arg-Gly-Glu (RGE). Whether the RGE motif of murine Lpp3 mediates cell-cell interaction has not been studied. In this report, we test the hypothesis that the cell adhesion function of the LPP3 protein is conserved across mouse and human. A glutathione S-transferase (GST) fusion protein of the proposed second extracellular loop of the murine Lpp3 sequence (GST-mLpp3-RGE) promoted attachment of cells in a long-term cell adhesion assay. GST-mLpp3-RGE interacted with {alpha}{sub 5}{beta}{sub 1} and {alpha}{sub v}{beta}{sub 3} integrins in a solid-phase ELISA, while a mutant control, GST-hLPP3-RAD, did not. Long-term adhesion of endothelial cells to GST-mLpp3-RGE induced phosphorylation of FAK, SHC, and CAS, whereas adhesion to GST-hLPP3-RAD failed to do so. Upon long-term adhesion both the GST-hLPP3-RGD and GST-mLpp3-RGE substrates bound to the {alpha}{sub 5}{beta}{sub 1} integrin of FRT-{alpha}{sub 5}(+) cells, an interaction that was inhibited by an anti-{alpha}{sub 5} integrin antibody. In addition, a cell aggregation assay showed that the intact mLpp3-RGE protein interacts with {alpha}{sub 5}{beta}{sub 1} and {alpha}{sub v}{beta}{sub 3} integrins expressed by adjacent cells, an interaction that can be blocked by GRGDSP peptides and anti-LPP3-RGD antibodies. These data, together with the known importance of integrins in angiogenesis, provide a mechanism for the function of LPP3 in cell-cell interactions in both human and mouse.
Country of PublicationUnited States
LanguageEnglish
FormatSize: page(s) 906-919
System Entry Date2006 May 08

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