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Article ; Online: Myogenic vasoconstriction requires G

Chennupati, Ramesh / Wirth, Angela / Favre, Julie / Li, Rui / Bonnavion, Rémy / Jin, Young-June / Wietelmann, Astrid / Schweda, Frank / Wettschureck, Nina / Henrion, Daniel / Offermanns, Stefan

eLife

2019 Volume 8

Abstract: Myogenic vasoconstriction is an autoregulatory function of small arteries. Recently, G-protein ... that small arteries from mice with smooth muscle-specific loss of G ...

Abstract	Myogenic vasoconstriction is an autoregulatory function of small arteries. Recently, G-protein-coupled receptors have been involved in myogenic vasoconstriction, but the downstream signalling mechanisms and the in-vivo-function of this myogenic autoregulation are poorly understood. Here, we show that small arteries from mice with smooth muscle-specific loss of G
MeSH term(s)	Animals ; GTP-Binding Protein alpha Subunits, G12-G13/deficiency ; GTP-Binding Protein alpha Subunits, G12-G13/metabolism ; Mice, Inbred C57BL ; Rho Guanine Nucleotide Exchange Factors/deficiency ; Rho Guanine Nucleotide Exchange Factors/metabolism ; Vascular Resistance ; Vasoconstriction
Chemical Substances	Arhgef12 protein, mouse ; Rho Guanine Nucleotide Exchange Factors ; GTP-Binding Protein alpha Subunits, G12-G13 (EC 3.6.5.1)
Language	English
Publishing date	2019-09-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.49374
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Article: Centrosomal AKAP350 modulates the G

Mattaloni, Stella M / Ferretti, Anabela C / Tonucci, Facundo M / Favre, Cristián / Goldenring, James R / Larocca, M Cecilia

Cellular logistics

2013 Volume 3, Issue 1, Page(s) e26331

Abstract: ... in the progression of the cell cycle. Our results showed that interference with AKAP350 expression inhibits G ...

Abstract	AKAP350 (AKAP450/AKAP9/CG-NAP) is an A-kinase anchoring protein, which recruits multiple signaling proteins to the Golgi apparatus and the centrosomes. Several proteins recruited to the centrosomes by this scaffold participate in the regulation of the cell cycle. Previous studies indicated that AKAP350 participates in centrosome duplication. In the present study we specifically assessed the role of AKAP350 in the progression of the cell cycle. Our results showed that interference with AKAP350 expression inhibits G
Language	English
Publishing date	2013-09-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2682440-1
ISSN	2159-2799 ; 2159-2780
ISSN (online)	2159-2799
ISSN	2159-2780
DOI	10.4161/cl.26331
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Article ; Online: hnRNP A1-mediated translational regulation of the G quadruplex-containing RON receptor tyrosine kinase mRNA linked to tumor progression.

Cammas, Anne / Lacroix-Triki, Magali / Pierredon, Sandra / Le Bras, Morgane / Iacovoni, Jason S / Teulade-Fichou, Marie-Paule / Favre, Gilles / Roché, Henri / Filleron, Thomas / Millevoi, Stefania / Vagner, Stéphan

Oncotarget

2016 Volume 7, Issue 13, Page(s) 16793–16805

Abstract: ... untranslated region of the RON mRNA and activates its translation through G-quadruplex RNA secondary structures ...

Abstract	The expression and role of RNA binding proteins (RBPs) controlling mRNA translation during tumor progression remains largely uncharacterized. Analysis by immunohistochemistry of the expression of hnRNP A1, hnRNPH, RBM9/FOX2, SRSF1/ASF/SF2, SRSF2/SC35, SRSF3/SRp20, SRSF7/9G8 in breast tumors shows that the expression of hnRNP A1, but not the other tested RBPs, is associated with metastatic relapse. Strikingly, hnRNP A1, a nuclear splicing regulator, is also present in the cytoplasm of tumor cells of a subset of patients displaying exceedingly worse prognosis. Expression of a cytoplasmic mutant of hnRNP A1 leads to increased translation of the mRNA encoding the tyrosine kinase receptor RON/MTS1R, known for its function in tumor dissemination, and increases cell migration in vitro. hnRNP A1 directly binds to the 5' untranslated region of the RON mRNA and activates its translation through G-quadruplex RNA secondary structures. The correlation between hnRNP A1 and RON tumoral expression suggests that these findings hold clinical relevance.
MeSH term(s)	Breast Neoplasms/genetics ; Breast Neoplasms/mortality ; Breast Neoplasms/pathology ; Disease Progression ; Female ; Gene Expression Regulation, Neoplastic/physiology ; Heterogeneous Nuclear Ribonucleoprotein A1/genetics ; Heterogeneous Nuclear Ribonucleoprotein A1/metabolism ; Humans ; Kaplan-Meier Estimate ; Protein Biosynthesis/physiology ; RNA, Messenger ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor Protein-Tyrosine Kinases/metabolism
Chemical Substances	Heterogeneous Nuclear Ribonucleoprotein A1 ; RNA, Messenger ; hnRNPA1 protein, human ; RON protein (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2016-02-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.7589
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Article: The novel inhibitor of the heterotrimeric G-protein complex, BIM-46187, elicits anti-hyperalgesic properties and synergizes with morphine.

Favre-Guilmard, Christine / Zeroual-Hider, Hamida / Soulard, Chantal / Touvay, Caroline / Chabrier, Pierre-Etienne / Prevost, Grégoire / Auguet, Michel

European journal of pharmacology

2008 Volume 594, Issue 1-3, Page(s) 70–76

Abstract: ... 1,2a]-pyrazine dimer, hydrochloride) is an inhibitor of the heterotrimeric G-protein complex ... signalling. Since many mediators of pain act through G-protein coupled receptors, the anti-hyperalgesic ... used in pain management and act through specific G-protein-coupled receptors, the effects of BIM-46187 ...

Abstract	BIM-46187 (7-[2-amino-1-oxo-3-thio-propyl]-8-cyclohexylmethyl-2-phenyl-5,6,7,8-tetrahydro-imidazo-[1,2a]-pyrazine dimer, hydrochloride) is an inhibitor of the heterotrimeric G-protein complex signalling. Since many mediators of pain act through G-protein coupled receptors, the anti-hyperalgesic effects of BIM-46187 were assessed on experimental models of pain. In addition since opioids are widely used in pain management and act through specific G-protein-coupled receptors, the effects of BIM-46187 on the analgesic properties of morphine have also been investigated. BIM-46187 elicited a dose dependent analgesic effect in the models of carrageenan-induced hyperalgesia (0.1-1 mg/kg; i.v.) and chronic constriction injury (0.3-3 mg/kg; i.v.) in rats. BIM-46187, however, up to 10 mg/kg did not modify the paw oedema induced by carrageenan excluding an anti-inflammatory effect. In addition, at these doses, the compound was not sedative as shown by the lack of effect on the motor performance in the rotarod test. The combination of BIM-46187 and morphine (ratio 1/1) resulted in an unexpected synergistic effect in the model of carrageenan-induced hyperalgesia and in the chronic constriction injury model in rats when evaluated by isobolographic analysis. This synergy allowed a reduction of at least 20 fold in the dose of each compound. Conversely, the drug combination did not increase the side effects of morphine as assessed in the rotarod test. In conclusion, BIM-46187 elicits a potent anti-hyperalgesic effect and strongly synergizes with morphine. This work highlights the role of heterotrimeric G-protein complexes in pain and supports further investigations of the use of BIM-46187 alone, or in combination with low doses of morphine, in the management of pain.
MeSH term(s)	Analgesics, Non-Narcotic/pharmacology ; Analgesics, Opioid/pharmacology ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Carrageenan ; Constriction, Pathologic/pathology ; Cyclohexanes/pharmacology ; Drug Synergism ; Edema/chemically induced ; Edema/pathology ; Heterotrimeric GTP-Binding Proteins/antagonists & inhibitors ; Hyperalgesia/chemically induced ; Hyperalgesia/drug therapy ; Male ; Morphine/pharmacology ; Pain Measurement/drug effects ; Peripheral Nervous System Diseases/chemically induced ; Peripheral Nervous System Diseases/pathology ; Peripheral Nervous System Diseases/psychology ; Psychomotor Performance/drug effects ; Pyrazines/pharmacology ; Rats ; Rats, Sprague-Dawley
Chemical Substances	7-(2-amino-1-oxo-3-thio-propyl)-8-cyclohexylmethyl-2-phenyl-5,6,7,8-tetrahydro-imidazo-(1,2a)-pyrazine dimer, hydrochloride ; Analgesics, Non-Narcotic ; Analgesics, Opioid ; Anti-Inflammatory Agents, Non-Steroidal ; Cyclohexanes ; Pyrazines ; Morphine (76I7G6D29C) ; Carrageenan (9000-07-1) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
Language	English
Publishing date	2008-10-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80121-5
ISSN	1879-0712 ; 0014-2999
ISSN (online)	1879-0712
ISSN	0014-2999
DOI	10.1016/j.ejphar.2008.07.016
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Article ; Online: Human replication protein A unfolds telomeric G-quadruplexes.

Salas, Tonatiuh Romero / Petruseva, Irina / Lavrik, Olga / Bourdoncle, Anne / Mergny, Jean-Louis / Favre, Alain / Saintomé, Carole

Nucleic acids research

2006 Volume 34, Issue 17, Page(s) 4857–4865

Abstract: G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation ... near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures ... fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded ...

Abstract	G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation during S phase. It has been suggested that the replication protein A (RPA) could unwind and maintain single-stranded DNA in a state amenable to the binding of telomeric components. We show here that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence. Analyses by native gel electrophoresis, cross-linking and fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded. In addition, quadruplex opening by hRPA is much faster than observed with the complementary DNA, demonstrating that this protein efficiently unfolds G-quartets. A two-step mechanism accounting for the binding of hRPA to G-quadruplexes is proposed. These data point to the involvement of hRPA in regulation of telomere maintenance.
MeSH term(s)	DNA/chemistry ; DNA/metabolism ; Fluorescence Resonance Energy Transfer ; G-Quadruplexes ; Guanine/chemistry ; Humans ; Models, Biological ; Nucleic Acid Conformation ; Oligonucleotides/chemistry ; Replication Protein A/metabolism ; Telomere/chemistry
Chemical Substances	Oligonucleotides ; Replication Protein A ; Guanine (5Z93L87A1R) ; DNA (9007-49-2)
Language	English
Publishing date	2006
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205588-5
ISSN	1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
ISSN (online)	1362-4962 ; 1746-8272
ISSN	0305-1048 ; 0261-3166
DOI	10.1093/nar/gkl564
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Article ; Online: Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.

Skillman, Kristen M / Daher, Wassim / Ma, Christopher I / Soldati-Favre, Dominique / Sibley, L David

Biochemistry

2012 Volume 51, Issue 12, Page(s) 2486–2495

Abstract: Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments ... ...

Abstract	Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments required for motility relies on a small repertoire of actin-binding proteins. Previous studies have shown that apicomplexan formins and profilin exhibit canonical functions on heterologous actins from higher eukaryotes; however, their biochemical properties on parasite actins are unknown. We therefore analyzed the impact of T. gondii profilin (TgPRF) and FH1-FH2 domains of two formin isoforms in T. gondii (TgFRM1 and TgFRM2) on the polymerization of T. gondii actin (TgACTI). Our findings based on in vitro assays demonstrate that TgFRM1-FH1-FH2 and TgFRM2-FH1-FH2 dramatically enhanced TgACTI polymerization in the absence of profilin, making them the sole protein factors known to initiate polymerization of this normally unstable actin. In addition, T. gondii formin domains were shown to both initiate polymerization and induce bundling of TgACTI filaments; however, they did not rely on TgPRF for these activities. In contrast, TgPRF sequestered TgACTI monomers, thus inhibiting polymerization even in the presence of formins. Collectively, these findings provide insight into the unusual control mechanisms of actin dynamics within the parasite.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/chemistry ; Actins/metabolism ; Nucleotides/metabolism ; Profilins/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Protozoan Proteins/metabolism ; Toxoplasma/cytology ; Toxoplasma/metabolism
Chemical Substances	Actins ; Nucleotides ; Profilins ; Protozoan Proteins
Language	English
Publishing date	2012-03-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi201704y
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Article: Human replication protein A unfolds telomeric G-quadruplexes

Salas, Tonatiuh Romero / Petruseva, Irina / Lavrik, Olga / Bourdoncle, Anne / Mergny, Jean-Louis / Favre, Alain / SaintomÃ©, Carole

Nucleic acids research. 2006 Oct., v. 34, no. 17

2006

Abstract	G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation during S phase. It has been suggested that the replication protein A (RPA) could unwind and maintain single-stranded DNA in a state amenable to the binding of telomeric components. We show here that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence. Analyses by native gel electrophoresis, cross-linking and fluorescence resonance energy transfer indicate the formation of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded. In addition, quadruplex opening by hRPA is much faster than observed with the complementary DNA, demonstrating that this protein efficiently unfolds G-quartets. A two-step mechanism accounting for the binding of hRPA to G-quadruplexes is proposed. These data point to the involvement of hRPA in regulation of telomere maintenance.
Keywords	complementary DNA ; crosslinking ; energy transfer ; fluorescence ; gel electrophoresis ; humans ; interphase ; single-stranded DNA ; telomerase ; telomeres
Language	English
Dates of publication	2006-10
Size	p. 4857-4865.
Document type	Article
ZDB-ID	186809-3
ISSN	0301-5610 ; 0305-1048
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkl564
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Article: Toxoplasma gondii Profilin Acts Primarily To Sequester G-Actin While Formins Efficiently Nucleate Actin Filament Formation in Vitro

Skillman, Kristen M / Daher Wassim / Ma Christopher I / Soldati-Favre Dominique / Sibley L. David

Biochemistry. 2012 Mar. 27, v. 51, no. 12

2012

Abstract	Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments required for motility relies on a small repertoire of actin-binding proteins. Previous studies have shown that apicomplexan formins and profilin exhibit canonical functions on heterologous actins from higher eukaryotes; however, their biochemical properties on parasite actins are unknown. We therefore analyzed the impact of T. gondii profilin (TgPRF) and FH1-FH2 domains of two formin isoforms in T. gondii (TgFRM1 and TgFRM2) on the polymerization of T. gondii actin (TgACTI). Our findings based on in vitro assays demonstrate that TgFRM1-FH1-FH2 and TgFRM2-FH1-FH2 dramatically enhanced TgACTI polymerization in the absence of profilin, making them the sole protein factors known to initiate polymerization of this normally unstable actin. In addition, T. gondii formin domains were shown to both initiate polymerization and induce bundling of TgACTI filaments; however, they did not rely on TgPRF for these activities. In contrast, TgPRF sequestered TgACTI monomers, thus inhibiting polymerization even in the presence of formins. Collectively, these findings provide insight into the unusual control mechanisms of actin dynamics within the parasite.
Keywords	Toxoplasma gondii ; actin ; eukaryotic cells ; in vitro studies ; microfilaments ; parasites ; polymerization
Language	English
Dates of publication	2012-0327
Size	p. 2486-2495.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi201704y
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Book ; Thesis: Contribution à l'étude du jaune d'indigo 3 G Ciba

Favre, Francois

1943

Author's details	François Favre
Size	54 S.
Publisher	Fragnière
Publishing place	Fribourg
Publishing country	Switzerland
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Freiburg [Schweiz], Naturwiss. Diss
HBZ-ID	HT008521591
Database	Catalogue ZB MED Medicine, Health

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Article: Prognostic relevance of surface markers in adult de novo acute myeloblastic leukemias: a prospective study of the Groupe d'Etude Immunologique des Leucémies (G.E.I.L.).

Casasnovas, R O / Solary, E / Campos, L / Maynadie, M / Favre, M / Bremend, J L / Garand, R / Béné, M C / Faure, G

Leukemia & lymphoma

1994 Volume 13 Suppl 1, Page(s) 7–10

MeSH term(s)	Adolescent ; Adult ; Aged ; Antigens, Surface/analysis ; Humans ; Immunophenotyping ; Leukemia, Myeloid, Acute/immunology ; Middle Aged ; Prognosis ; Prospective Studies
Chemical Substances	Antigens, Surface
Language	English
Publishing date	1994
Publishing country	United States
Document type	Journal Article ; Multicenter Study ; Research Support, Non-U.S. Gov't
ZDB-ID	1042374-6
ISSN	1029-2403 ; 1042-8194
ISSN (online)	1029-2403
ISSN	1042-8194
DOI	10.3109/10428199409052665
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