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Article ; Online: Exercise Metabolism.

Emambokus, Nikla / Granger, Anne / Messmer-Blust, Angela

2015 Volume 22, Issue 1, Page(s) 1

MeSH term(s)	Computational Biology ; Energy Metabolism ; Exercise ; Humans ; Oxygen Consumption
Language	English
Publishing date	2015-07-07
Publishing country	United States
Document type	Editorial ; Introductory Journal Article
ZDB-ID	2176834-1
ISSN	1932-7420 ; 1550-4131
ISSN (online)	1932-7420
ISSN	1550-4131
DOI	10.1016/j.cmet.2015.06.020
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Zs.A 6169: Show issues

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Article ; Online: The role of transcription enhancer factors in cardiovascular biology.

Jin, Yi / Messmer-Blust, Angela F / Li, Jian

Trends in cardiovascular medicine

2012 Volume 21, Issue 1, Page(s) 1–5

Abstract: The transcriptional enhancer factor (TEF) multigene family is primarily functional in muscle-specific genes through binding to MCAT elements that activate or repress transcription of many genes in response to physiological and pathological stimuli. Among ...

Abstract	The transcriptional enhancer factor (TEF) multigene family is primarily functional in muscle-specific genes through binding to MCAT elements that activate or repress transcription of many genes in response to physiological and pathological stimuli. Among the TEF family, TEF-1, RTEF-1, and DTEF-1 are critical regulators of cardiac and smooth muscle-specific genes during cardiovascular development and cardiac disorders including cardiac hypertrophy. Emerging evidence suggests that in addition to functioning as muscle-specific transcription factors, members of the TEF family may be key mediators of gene expression induced by hypoxia in endothelial cells by virtue of its multidomain organization, potential for post-translational modifications, and interactions with numerous transcription factors, which represent a cell-selective control mediator of nuclear signaling. We review the recent literature demonstrating the involvement of the TEF family of transcription factors in the regulation of differential gene expression in cardiovascular physiology and pathology.
MeSH term(s)	Animals ; Cardiovascular Diseases/genetics ; Cardiovascular Diseases/metabolism ; Cardiovascular Diseases/pathology ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Endothelial Cells/metabolism ; Gene Expression Regulation ; Humans ; Muscle, Smooth, Vascular/metabolism ; Myocytes, Cardiac/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic
Chemical Substances	DNA-Binding Proteins ; Transcription Factors
Language	English
Publishing date	2012-04-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1097434-9
ISSN	1873-2615 ; 1050-1738
ISSN (online)	1873-2615
ISSN	1050-1738
DOI	10.1016/j.tcm.2011.12.009
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Zs.A 3419: Show issues

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Article ; Online: Hypoxia-regulated angiogenic inhibitors.

Messmer-Blust, Angela / An, Xiaojin / Li, Jian

Trends in cardiovascular medicine

2010 Volume 19, Issue 8, Page(s) 252–256

Abstract: The regulation of angiogenesis by hypoxia is an essential homeostatic mechanism that depends on a precise balance between positive and negative angiogenic regulatory molecules. Proangiogenic factors are well characterized; however, several in vivo and in ...

Abstract	The regulation of angiogenesis by hypoxia is an essential homeostatic mechanism that depends on a precise balance between positive and negative angiogenic regulatory molecules. Proangiogenic factors are well characterized; however, several in vivo and in vitro studies indicate that there are feedback mechanisms in place to inhibit angiogenesis during hypoxia. Understanding the signaling pathways leading to the negative feedback of angiogenesis will undoubtedly provide important tools to develop novel therapeutic strategies not only to enhance the angiogenic response in coronary artery disease but also to hinder deregulated angiogenesis in tumorigenesis.
MeSH term(s)	Angiogenesis Inhibitors/metabolism ; Animals ; Homeostasis ; Humans ; Hypoxia/metabolism ; Hypoxia/physiopathology ; Hypoxia-Inducible Factor 1/metabolism ; Neoplasms/blood supply ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/physiopathology ; Neovascularization, Pathologic/prevention & control ; Neovascularization, Physiologic ; Signal Transduction ; Vascular Endothelial Growth Factor A/metabolism
Chemical Substances	Angiogenesis Inhibitors ; Hypoxia-Inducible Factor 1 ; Vascular Endothelial Growth Factor A
Language	English
Publishing date	2010-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1097434-9
ISSN	1873-2615 ; 1050-1738
ISSN (online)	1873-2615
ISSN	1050-1738
DOI	10.1016/j.tcm.2010.02.006
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Article ; Online: Endothelial differentiation gene-1, a new downstream gene is involved in RTEF-1 induced angiogenesis in endothelial cells.

He, Ping / Philbrick, Melissa J / An, Xiaojin / Wu, Jiaping / Messmer-Blust, Angela F / Li, Jian

PloS one

2014 Volume 9, Issue 2, Page(s) e88143

Abstract: Related Transcriptional Enhancer Factor-1 (RTEF-1) has been suggested to induce angiogenesis through regulating target genes. Whether RTEF-1 has a direct role in angiogenesis and what specific genes are involved in RTEF-1 driven angiogenisis have not ... ...

Abstract	Related Transcriptional Enhancer Factor-1 (RTEF-1) has been suggested to induce angiogenesis through regulating target genes. Whether RTEF-1 has a direct role in angiogenesis and what specific genes are involved in RTEF-1 driven angiogenisis have not been elucidated. We found that over-expressing RTEF-1 in Human dermal microvascular endothelial cells-1 (HMEC-1) significantly increased endothelial cell aggregation, growth and migration while the processes were inhibited by siRNA of RTEF-1. In addition, we observed that Endothelial differentiation gene-1 (Edg-1) expression was up-regulated by RTEF-1 at the transcriptional level. RTEF-1 could bind to Edg-1 promoter and subsequently induce its activity. Edg-1 siRNA significantly blocked RTEF-1-driven increases in endothelial cell aggregation in a Matrigel assay and retarded RTEF-1-induced endothelial cell growth and migration. Pertussis Toxin (PTX), a Gi/Go protein sensitive inhibitor, was found to inhibit RTEF-1 driven endothelial cell aggregation and migration. Our data demonstrates that Edg-1 is a potential target gene of RTEF-1 and is involved in RTEF-1-induced angiogenesis in endothelial cells. Gi/Go protein coupled receptor pathway plays a role in RTEF-1 driven angiogenesis in endothelial cells.
MeSH term(s)	Animals ; Cell Aggregation/drug effects ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; DNA-Binding Proteins/metabolism ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Gene Expression Regulation/drug effects ; HEK293 Cells ; Humans ; Mice ; Muscle Proteins/metabolism ; Neovascularization, Physiologic/drug effects ; Neovascularization, Physiologic/genetics ; Pertussis Toxin/pharmacology ; Receptors, Lysosphingolipid/genetics ; Receptors, Lysosphingolipid/metabolism ; Sphingosine-1-Phosphate Receptors ; Transcription Factors/metabolism
Chemical Substances	DNA-Binding Proteins ; Muscle Proteins ; Receptors, Lysosphingolipid ; S1PR1 protein, human ; Sphingosine-1-Phosphate Receptors ; TEAD4 protein, human ; Transcription Factors ; Pertussis Toxin (EC 2.4.2.31)
Language	English
Publishing date	2014-02-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0088143
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Article ; Online: Role of A20 in cIAP-2 protection against tumor necrosis factor α (TNF-α)-mediated apoptosis in endothelial cells.

Guo, Shuzhen / Messmer-Blust, Angela F / Wu, Jiaping / Song, Xiaoxiao / Philbrick, Melissa J / Shie, Jue-Lon / Rana, Jamal S / Li, Jian

International journal of molecular sciences

2014 Volume 15, Issue 3, Page(s) 3816–3833

Abstract: Tumor necrosis factor α (TNF-α) influences endothelial cell viability by altering the regulatory molecules involved in induction or suppression of apoptosis. However, the underlying mechanisms are still not completely understood. In this study, we ... ...

Abstract	Tumor necrosis factor α (TNF-α) influences endothelial cell viability by altering the regulatory molecules involved in induction or suppression of apoptosis. However, the underlying mechanisms are still not completely understood. In this study, we demonstrated that A20 (also known as TNFAIP3, tumor necrosis factor α-induced protein 3, and an anti-apoptotic protein) regulates the inhibitor of apoptosis protein-2 (cIAP-2) expression upon TNF-α induction in endothelial cells. Inhibition of A20 expression by its siRNA resulted in attenuating expression of TNF-α-induced cIAP-2, yet not cIAP-1 or XIAP. A20-induced cIAP-2 expression can be blocked by the inhibition of phosphatidyl inositol-3 kinase (PI3-K), but not nuclear factor (NF)-κB, while concomitantly increasing the number of endothelial apoptotic cells and caspase 3 activation. Moreover, TNF-α-mediated induction of apoptosis was enhanced by A20 inhibition, which could be rescued by cIAP-2. Taken together, these results identify A20 as a cytoprotective factor involved in cIAP-2 inhibitory pathway of TNF-α-induced apoptosis. This is consistent with the idea that endothelial cell viability is dependent on interactions between inducers and suppressors of apoptosis, susceptible to modulation by TNF-α.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Apoptosis/genetics ; Baculoviral IAP Repeat-Containing 3 Protein ; Blotting, Western ; Caspase 3/metabolism ; Cattle ; Cells, Cultured ; Chromones/pharmacology ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dose-Response Relationship, Drug ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Gene Expression/drug effects ; HEK293 Cells ; Humans ; Inhibitor of Apoptosis Proteins/genetics ; Inhibitor of Apoptosis Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Morpholines/pharmacology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphatidylinositol 3-Kinase/metabolism ; Phosphoinositide-3 Kinase Inhibitors ; RNA Interference ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction/drug effects ; Tumor Necrosis Factor alpha-Induced Protein 3 ; Tumor Necrosis Factor-alpha/pharmacology ; Ubiquitin-Protein Ligases
Chemical Substances	Chromones ; DNA-Binding Proteins ; Inhibitor of Apoptosis Proteins ; Intracellular Signaling Peptides and Proteins ; Morpholines ; Nuclear Proteins ; Phosphoinositide-3 Kinase Inhibitors ; Tumor Necrosis Factor-alpha ; 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (31M2U1DVID) ; BIRC3 protein, human (EC 2.3.2.27) ; Baculoviral IAP Repeat-Containing 3 Protein (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; TNFAIP3 protein, human (EC 3.4.19.12) ; Tumor Necrosis Factor alpha-Induced Protein 3 (EC 3.4.19.12) ; Caspase 3 (EC 3.4.22.-)
Language	English
Publishing date	2014-03-03
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms15033816
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Article ; Online: Role of GTP binding, isoprenylation, and the C-terminal α-helices in the inhibition of cell spreading by the interferon-induced GTPase, mouse guanylate-binding protein-2.

Balasubramanian, Sujata / Messmer-Blust, Angela F / Jeyaratnam, Jonathan A / Vestal, Deborah J

Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research

2011 Volume 31, Issue 3, Page(s) 291–298

Abstract: Interferon-γ pre-exposure inhibits Rac activation by either integrin engagement or platelet-derived growth factor treatment. Interferon-γ does this by inducing expression of the large guanosine triphosphatase (GTPase) mouse guanylate-binding protein ( ... ...

Abstract	Interferon-γ pre-exposure inhibits Rac activation by either integrin engagement or platelet-derived growth factor treatment. Interferon-γ does this by inducing expression of the large guanosine triphosphatase (GTPase) mouse guanylate-binding protein (mGBP-2). Inhibiting Rac results in the retardation of cell spreading. Analysis of variants of mGBP-2 containing amino acid substitutions in the guanosine triphosphate (GTP) binding domain suggests that GTP binding, and possibly dimerization, of mGBP-2 is necessary to inhibit cell spreading. However, isoprenylation is also required. Removal of the N-terminal GTP-binding globular domain from mGBP-2 yields a protein with only the extended C-terminal α-helices that lacks enzymatic activity. The ability of the C-terminal α-helices alone to inhibit cell spreading suggests that this is the domain that interacts with the downstream effectors of mGBP-2. Interestingly, mGBP-2 can inhibit cell spreading whether it is geranylgeranylated or farnesylated. This study begins to define the properties of mGBP-2 responsible for inhibiting cell spreading.
MeSH term(s)	3T3 Cells ; Amino Acid Substitution ; Animals ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/immunology ; Guanosine Triphosphate/genetics ; Guanosine Triphosphate/immunology ; Humans ; Interferon-gamma/genetics ; Interferon-gamma/immunology ; Mice ; Mutation, Missense ; Platelet-Derived Growth Factor/genetics ; Platelet-Derived Growth Factor/immunology ; Protein Prenylation/genetics ; Protein Prenylation/immunology ; Protein Structure, Secondary ; Protein Structure, Tertiary ; rac GTP-Binding Proteins/genetics ; rac GTP-Binding Proteins/immunology
Chemical Substances	Platelet-Derived Growth Factor ; Interferon-gamma (82115-62-6) ; Guanosine Triphosphate (86-01-1) ; GTP-Binding Proteins (EC 3.6.1.-) ; Gbp2 protein, mouse (EC 3.6.1.-) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1226675-9
ISSN	1557-7465 ; 1079-9907
ISSN (online)	1557-7465
ISSN	1079-9907
DOI	10.1089/jir.2010.0056
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Zs.A 1748: Show issues

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Article ; Online: 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.

Messmer-Blust, Angela F / Balasubramanian, Sujata / Gorbacheva, Victoria Y / Jeyaratnam, Jonathan A / Vestal, Deborah J

Molecular biology of the cell

2010 Volume 21, Issue 14, Page(s) 2514–2528

Abstract: 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. ... ...

Abstract	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.
MeSH term(s)	Amino Acid Substitution/genetics ; Animals ; Cell Adhesion/drug effects ; Cell Line ; Cell Movement/drug effects ; Enzyme Activation/drug effects ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/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 Substances	Fibronectins ; Platelet-Derived Growth Factor ; RNA, Small Interfering ; Receptors, Fibronectin ; Integrin alpha4 (143198-26-9) ; Interferon-gamma (82115-62-6) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; GTP-Binding Proteins (EC 3.6.1.-) ; Gbp2 protein, mouse (EC 3.6.1.-) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-05-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E09-04-0344
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Related transcriptional enhancer factor 1 increases endothelial-dependent microvascular relaxation and proliferation.

Messmer-Blust, Angela F / Zhang, Cuili / Shie, Jue-Lon / Song, Qinhui / He, Ping / Lubenec, Isabel / Liu, Yuhong / Sellke, Frank / Li, Jian

Journal of vascular research

2012 Volume 49, Issue 3, Page(s) 249–259

Abstract: Objective: Related transcriptional enhancer factor 1 (RTEF-1) is a key transcriptional regulator in endothelial function. In this study, we investigated a possible role for RTEF-1 in the regulation of microvascular relaxation and the underlying ... ...

Abstract	Objective: Related transcriptional enhancer factor 1 (RTEF-1) is a key transcriptional regulator in endothelial function. In this study, we investigated a possible role for RTEF-1 in the regulation of microvascular relaxation and the underlying mechanism involved. Activation of fibroblast growth factor receptor 1 (FGFR1) by FGFs increases vasodilation, although transcriptional control of the molecular mechanisms underlying FGFR1 is still unclear. Materials and methods: We demonstrated that RTEF-1 stimulated FGFR1 expression at the transcriptional level, specifically an area including Sp1 elements, as evidenced by promoter assays. Additionally, RTEF-1 increased FGFR1 mRNA and protein expression in vitro and in VE-cadherin-promoted RTEF-1 (VE-Cad/RTEF-1) transgenic mice, whereas RTEF-1 siRNA blocked the upregulation of FGFR1 expression. Furthermore, increased endothelial-dependent microvessel relaxation was observed in the coronary arteries of VE-Cad/RTEF-1 mice, and increased proliferation was observed in RTEF-1-overexpressing cells, both of which correlated to increased FGF/FGFR1 signaling and endothelial nitric oxide synthase (eNOS) upregulation. Our results indicate that RTEF-1 acts as a transcriptional stimulator of FGFR1 and is involved in FGF pathways by increasing microvessel dilatation via eNOS. Conclusions: These findings suggest that RTEF-1 plays an important role in FGFR1- stimulated vasodilatation. Understanding the effect of RTEF-1 in microvessel relaxation may provide beneficial knowledge in improving treatments in regards to ischemic vascular disorders.
MeSH term(s)	Animals ; Cattle ; Cell Proliferation ; Cells, Cultured ; DNA-Binding Proteins/physiology ; Endothelium, Vascular/physiology ; Humans ; Microvessels/physiology ; Muscle Proteins/physiology ; Nitric Oxide Synthase Type III/physiology ; Promoter Regions, Genetic ; Receptor, Fibroblast Growth Factor, Type 1/analysis ; Receptor, Fibroblast Growth Factor, Type 1/genetics ; Signal Transduction ; Transcription Factors/physiology ; Vasodilation
Chemical Substances	DNA-Binding Proteins ; Muscle Proteins ; TEAD4 protein, human ; Transcription Factors ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; FGFR1 protein, human (EC 2.7.10.1) ; Receptor, Fibroblast Growth Factor, Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2012-03-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1105259-4
ISSN	1423-0135 ; 1018-1172
ISSN (online)	1423-0135
ISSN	1018-1172
DOI	10.1159/000335180
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Zs.A 513: Show issues

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Article ; Online: RTEF-1 attenuates blood glucose levels by regulating insulin-like growth factor binding protein-1 in the endothelium.

Messmer-Blust, Angela F / Philbrick, Melissa J / Guo, Shuzhen / Wu, Jiaping / He, Ping / Guo, Shaodong / Li, Jian

Circulation research

2012 Volume 111, Issue 8, Page(s) 991–1001

Abstract: Rationale: Related transcriptional enhancer factor-1 (RTEF-1) plays an important role in endothelial cell function by regulating angiogenesis; however, the mechanism underlying the role of RTEF-1 in the endothelium in vivo is not well defined.: ... ...

Abstract	Rationale: Related transcriptional enhancer factor-1 (RTEF-1) plays an important role in endothelial cell function by regulating angiogenesis; however, the mechanism underlying the role of RTEF-1 in the endothelium in vivo is not well defined. Objective: We investigated the biological functions of RTEF-1 by disrupting the gene that encodes it in mice endothelium -specific RTEF-1-deficient transgenic mice (RTEF-1(-/-)). Methods and results: RTEF-1(-/-) mice showed significantly increased blood glucose levels and insulin resistance, accompanied by decreased levels of insulin-like growth factor binding protein-1 (IGFBP-1) mRNA in the endothelium and decreased serum IGFBP-1 levels. Additionally, the RTEF-1(-/-) phenotype was exacerbated when the mice were fed a high-fat diet, which correlated with decreased IGFBP-1 levels. In contrast, vascular endothelial cadherin/RTEF-1-overexpressing(1) transgenic mice (VE-Cad/RTEF1) demonstrated improved glucose clearance and insulin sensitivity in response to a high-fat diet. Furthermore, we demonstrated that RTEF-1 upregulates IGFBP-1 through selective binding and promotion of transcription from the insulin response element site. Insulin prevented RTEF-1 expression and significantly inhibited IGFBP-1 transcription in endothelial cells in a dose-dependent fashion. Conclusions: To the best of our knowledge, this is the first report demonstrating that RTEF-1 stimulates promoter activity through an insulin response element and also mediates the effects of insulin on gene expression. These results show that RTEF-1-stimulated IGFBP-1 expression may be central to the mechanism by which RTEF-1 attenuates blood glucose levels. These findings provide the basis for novel insights into the transcriptional regulation of IGFBP-1 and contribute to our understanding of the role of vascular endothelial cells in metabolism.
MeSH term(s)	Animals ; Blood Glucose/genetics ; Blood Glucose/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Glucose Intolerance/genetics ; Glucose Intolerance/metabolism ; HEK293 Cells ; Hearing/physiology ; Homeostasis/physiology ; Humans ; Insulin Resistance/physiology ; Insulin-Like Growth Factor Binding Protein 1/metabolism ; Mice ; Mice, Knockout ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Obesity/genetics ; Obesity/metabolism ; Promoter Regions, Genetic/physiology ; RNA, Small Interfering/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Blood Glucose ; DNA-Binding Proteins ; IGFBP1 protein, human ; Insulin-Like Growth Factor Binding Protein 1 ; Muscle Proteins ; RNA, Small Interfering ; TEAD4 protein, human ; Tead4 protein, mouse ; Transcription Factors
Language	English
Publishing date	2012-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.112.268110
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Article ; Online: The interferon-gamma-induced GTPase, mGBP-2, inhibits tumor necrosis factor alpha (TNF-alpha) induction of matrix metalloproteinase-9 (MMP-9) by inhibiting NF-kappaB and Rac protein.

Balasubramanian, Sujata / Fan, Meiyun / Messmer-Blust, Angela F / Yang, Chuan H / Trendel, Jill A / Jeyaratnam, Jonathan A / Pfeffer, Lawrence M / Vestal, Deborah J

The Journal of biological chemistry

2011 Volume 286, Issue 22, Page(s) 20054–20064

Abstract: Matrix metalloproteinase-9 (MMP-9) is important in numerous normal and pathological processes, including the angiogenic switch during tumor development and tumor metastasis. Whereas TNF-α and other cytokines up-regulate MMP-9 expression, interferons ( ... ...

Abstract	Matrix metalloproteinase-9 (MMP-9) is important in numerous normal and pathological processes, including the angiogenic switch during tumor development and tumor metastasis. Whereas TNF-α and other cytokines up-regulate MMP-9 expression, interferons (IFNs) inhibit MMP-9 expression. We found that IFN-γ treatment or forced expression of the IFN-induced GTPase, mGBP-2, inhibit TNF-α-induced MMP-9 expression in NIH 3T3 fibroblasts, by inhibiting MMP-9 transcription. The NF-κB transcription factor is required for full induction of MMP-9 by TNF-α. Both IFN-γ and mGBP-2 inhibit the transcription of a NF-κB-dependent reporter construct, suggesting that mGBP-2 inhibits MMP-9 induction via inhibition of NF-κB-mediated transcription. Interestingly, mGBP-2 does not inhibit TNF-α-induced degradation of IκBα or p65/RelA translocation into the nucleus. However, mGBP-2 inhibits p65 binding to a κB oligonucleotide probe in gel shift assays and to the MMP-9 promoter in chromatin immunoprecipitation assays. In addition, TNF-α activation of NF-κB in NIH 3T3 cells is dependent on Rac activation, as evidenced by the inhibition of TNF-α induction of NF-κB-mediated transcription by a dominant inhibitory form of Rac1. A role for Rac in the inhibitory action of mGBP-2 on NF-κB is further shown by the findings that mGBP-2 inhibits TNF-α activation of endogenous Rac and constitutively activate Rac can restore NF-κB transcription in the presence of mGBP-2. This is a novel mechanism by which IFNs can inhibit the cytokine induction of MMP-9 expression.
MeSH term(s)	Active Transport, Cell Nucleus/drug effects ; Active Transport, Cell Nucleus/physiology ; Animals ; Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Enzyme Induction/drug effects ; Enzyme Induction/physiology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; I-kappa B Proteins/genetics ; I-kappa B Proteins/metabolism ; Interferon-gamma/genetics ; Interferon-gamma/metabolism ; Interferon-gamma/pharmacology ; Matrix Metalloproteinase 9/biosynthesis ; Matrix Metalloproteinase 9/genetics ; Mice ; NF-KappaB Inhibitor alpha ; NIH 3T3 Cells ; Neuropeptides/genetics ; Neuropeptides/metabolism ; Transcription Factor RelA/genetics ; Transcription Factor RelA/metabolism ; Transcription, Genetic/drug effects ; Transcription, Genetic/physiology ; Tumor Necrosis Factor-alpha/genetics ; Tumor Necrosis Factor-alpha/metabolism ; rac GTP-Binding Proteins/genetics ; rac GTP-Binding Proteins/metabolism ; rac1 GTP-Binding Protein
Chemical Substances	Antiviral Agents ; I-kappa B Proteins ; Neuropeptides ; Nfkbia protein, mouse ; Rac1 protein, mouse ; Rela protein, mouse ; Transcription Factor RelA ; Tumor Necrosis Factor-alpha ; NF-KappaB Inhibitor alpha (139874-52-5) ; Interferon-gamma (82115-62-6) ; Matrix Metalloproteinase 9 (EC 3.4.24.35) ; Mmp9 protein, mouse (EC 3.4.24.35) ; GTP-Binding Proteins (EC 3.6.1.-) ; Gbp2 protein, mouse (EC 3.6.1.-) ; rac GTP-Binding Proteins (EC 3.6.5.2) ; rac1 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2011-04-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.249326
Database	MEDical Literature Analysis and Retrieval System OnLINE

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