| The interferon-gamma-induced murine guanylate-binding protein-2 inhibits rac activation during cell spreading on fibronectin and after platelet-derived growth factor treatment: role for phosphatidylinositol 3-kinase. | |
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MedLine Citation:
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PMID: 20505078 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Exposure of cells to certain cytokines can alter how these same cells respond to later cues from other agents, such as extracellular matrix or growth factors. Interferon (IFN)-gamma pre-exposure inhibits the spreading of fibroblasts on fibronectin. Expression of the IFN-gamma-induced GTPase murine guanylate-binding protein-2 (mGBP-2) can phenocopy this inhibition and small interfering RNA knockdown of mGBP-2 prevents IFN-gamma-mediated inhibition of cell spreading. Either IFN-gamma treatment or mGBP-2 expression inhibits Rac activation during cell spreading. Rac is required for cell spreading. mGBP-2 also inhibits the activation of Akt during cell spreading on fibronectin. mGBP-2 is incorporated into a protein complex containing the catalytic subunit of phosphatidylinositol 3-kinase (PI3-K), p110. The association of mGBP-2 with p110 seems important for the inhibition of cell spreading because S52N mGBP-2, which does not incorporate into the protein complex with p110, is unable to inhibit cell spreading. PI3-K activation during cell spreading on fibronectin was inhibited in the presence of mGBP-2. Both IFN-gamma and mGBP-2 also inhibit cell spreading initiated by platelet-derived growth factor treatment, which is also accompanied by inhibition of Rac activation by mGBP-2. This is the first report of a novel mechanism by which IFN-gamma can alter how cells respond to subsequent extracellular signals, by the induction of mGBP-2. |
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Authors:
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Angela F Messmer-Blust; Sujata Balasubramanian; Victoria Y Gorbacheva; Jonathan A Jeyaratnam; Deborah J Vestal |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-05-26 |
Journal Detail:
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Title: Molecular biology of the cell Volume: 21 ISSN: 1939-4586 ISO Abbreviation: Mol. Biol. Cell Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-07-14 Completed Date: 2010-10-21 Revised Date: 2013-05-29 |
Medline Journal Info:
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Nlm Unique ID: 9201390 Medline TA: Mol Biol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 2514-28 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, University of Toledo, Toledo, OH 43606, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution
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genetics Animals Cell Adhesion / drug effects Cell Line Cell Movement / drug effects* Enzyme Activation / drug effects Fibroblasts / cytology, drug effects, enzymology Fibronectins / pharmacology* GTP-Binding Proteins / metabolism* Humans Integrin alpha4 / metabolism Interferon-gamma / pharmacology* Melanoma / pathology Mice Phosphatidylinositol 3-Kinases / metabolism* Platelet-Derived Growth Factor / pharmacology* Proto-Oncogene Proteins c-akt / metabolism RNA, Small Interfering / metabolism Receptors, Fibronectin / metabolism rac GTP-Binding Proteins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Fibronectins; 0/Platelet-Derived Growth Factor; 0/RNA, Small Interfering; 0/Receptors, Fibronectin; 143198-26-9/Integrin alpha4; 82115-62-6/Interferon-gamma; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.1.-/Gbp2 protein, mouse; EC 3.6.5.2/rac GTP-Binding Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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