◀ Back to NOS3
HSP90AA1 — NOS3
Pathways - manually collected, often from reviews:
-
OpenBEL Selventa BEL large corpus:
NOS3
→
HSP90AA1
(increases, HSP90AA1 Activity, NOS3 Activity)
Evidence: activation of Hsp90 seems to increase its affinity for and association with eNOS to stimulate eNOS activity
-
NCI Pathway Database VEGFR1 specific signals:
Hsp90 (HSP90AA1)
→
eNOS/Caveolin-1 complex (NOS3-CAV1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: assay, physical interaction
-
NCI Pathway Database VEGFR1 specific signals:
Hsp90 (HSP90AA1)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: assay, physical interaction
-
NCI Pathway Database VEGFR1 specific signals:
eNOS/Caveolin-1 complex (NOS3-CAV1)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: assay, physical interaction
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
None
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(reaction, collaborate)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Daher et al., J Biol Chem 2010*
Evidence: assay
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
None
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(reaction, collaborate)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Daher et al., J Biol Chem 2010*
Evidence: assay
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
None
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(reaction, collaborate)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Daher et al., J Biol Chem 2010*
Evidence: assay
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
AKT1 (AKT1)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(modification, activates)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Brouet et al., J Biol Chem 2001*
Evidence: assay
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
eNOS (NOS3)
→
Hsp90 (HSP90AA1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: physical interaction
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
eNOS (NOS3)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: physical interaction
-
NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2:
Hsp90 (HSP90AA1)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(modification, collaborate)
Brouet et al., J Biol Chem 2001*
Evidence: physical interaction
-
NCI Pathway Database VEGFR1 specific signals:
eNOS (NOS3)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(translocation, collaborate)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Urbich et al., FASEB J 2002, Michell et al., J Biol Chem 2002, Mount et al., J Mol Cell Cardiol 2007
Evidence: assay
-
NCI Pathway Database VEGFR1 specific signals:
AKT1 (AKT1)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(translocation, activates)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Urbich et al., FASEB J 2002, Michell et al., J Biol Chem 2002, Mount et al., J Mol Cell Cardiol 2007
Evidence: assay
-
NCI Pathway Database VEGFR1 specific signals:
Ca2+/CaM complex (CALM2)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(translocation, activates)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Urbich et al., FASEB J 2002, Michell et al., J Biol Chem 2002, Mount et al., J Mol Cell Cardiol 2007
Evidence: assay
-
NCI Pathway Database VEGFR1 specific signals:
PKA C-alpha (PRKACA)
→
eNOS/Hsp90 complex (NOS3-HSP90AA1)
(translocation, activates)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Dimmeler et al., FEBS Lett 2000, Urbich et al., FASEB J 2002, Michell et al., J Biol Chem 2002, Mount et al., J Mol Cell Cardiol 2007
Evidence: assay
-
Reactome Reaction:
HSP90AA1
→
NOS3
(indirect_complex)
Fulton et al., Nature 1999, Dimmeler et al., Nature 1999, Michell et al., Curr Biol 1999*, Vásquez-Vivar et al., Biochem J 2002*, Berka et al., Biochemistry 2004*, García-Cardeña et al., Nature 1998*
-
Reactome Reaction:
HSP90AA1
→
NOS3
(reaction)
García-Cardeña et al., Nature 1998*
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(direct interaction, pull down)
Harris et al., Gen Pharmacol 2000*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(physical association, affinity chromatography technology)
Stepp et al., Am J Physiol Heart Circ Physiol 2002*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(direct interaction, two hybrid)
Fontana et al., Circ Res 2002*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(direct interaction, pull down)
Fontana et al., Circ Res 2002*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(physical association, affinity chromatography technology)
Brouet et al., J Biol Chem 2001*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(physical association, affinity chromatography technology)
Venema et al., Am J Physiol Heart Circ Physiol 2003*
-
IRef Biogrid Interaction:
NOS3
—
HSP90AA1
(physical association, affinity chromatography technology)
Harris et al., Gen Pharmacol 2000*
-
MIPS CORUM eNOS-HSP90 complex, VEGF induced:
eNOS-HSP90 complex, VEGF induced complex (HSP90AA1-NOS3)
Brouet et al., J Biol Chem 2001*
-
MIPS CORUM eNOS-HSP90-AKT complex, VEGF induced:
eNOS-HSP90-AKT complex, VEGF induced complex (AKT1-HSP90AA1-NOS3)
Brouet et al., J Biol Chem 2001*
-
IRef Corum Interaction:
Complex of HSP90AA1-NOS3-AKT1
(association, anti bait coimmunoprecipitation)
Brouet et al., J Biol Chem 2001*
-
IRef Corum Interaction:
NOS3
—
HSP90AA1
(association, anti bait coimmunoprecipitation)
Brouet et al., J Biol Chem 2001*
-
IRef Hprd Interaction:
NOS3
—
HSP90AA1
(two hybrid)
Harris et al., Gen Pharmacol 2000*, Fontana et al., Circ Res 2002*, Stepp et al., Am J Physiol Heart Circ Physiol 2002*
-
IRef Hprd Interaction:
NOS3
—
HSP90AA1
(in vitro)
Harris et al., Gen Pharmacol 2000*, Fontana et al., Circ Res 2002*, Stepp et al., Am J Physiol Heart Circ Physiol 2002*
-
IRef Hprd Interaction:
NOS3
—
HSP90AA1
(in vivo)
Harris et al., Gen Pharmacol 2000*, Fontana et al., Circ Res 2002*, Stepp et al., Am J Physiol Heart Circ Physiol 2002*
-
IRef Ophid Interaction:
NOS3
—
HSP90AA1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
-
IRef Ophid Interaction:
NOS3
—
HSP90AA1
(aggregation, confirmational text mining)
Fontana et al., Circ Res 2002*
Text-mined interactions from Literome
Shah et al., Am J Physiol 1999
(Hypertension, Portal) :
Hsp90 regulation of endothelial
nitric oxide synthase contributes to vascular control in portal hypertension
Su et al., Am J Physiol Lung Cell Mol Physiol 2000
(Anoxia) :
These results indicate that the hypoxia induced reduction in
eNOS activity in PAEC is
due to a decrease in
HSP90 caused by calpain activation
Harris et al., Gen Pharmacol 2000
:
Therefore, we tested the hypotheses that ENAP-1 and Hsp90 are the same protein and that BK activation of
eNOS is
dependent on
Hsp90
Shastry et al., Am J Physiol Heart Circ Physiol 2002
:
The binding of
heat shock protein 90 (HSP90) to endothelial nitric oxide ( NO ) synthase ( eNOS ) can
enhance eNOS activation ... The results show that GA can attenuate NO-mediated dilation in human skin, suggesting a potential
role for
HSP90 in activation of
eNOS in the microcirculation
Su et al., Am J Physiol Lung Cell Mol Physiol 2002
:
The changes in
eNOS activity induced by modification of microtubules are
due , at least in part, to the altered binding of
HSP90 to eNOS protein
Harris et al., Am J Physiol Heart Circ Physiol 2003
:
Endothelial
nitric oxide ( NO ) synthase ( eNOS ) is
regulated by
heat shock protein 90 (HSP90) , a heat-inducible protein ; however, the effect of heat shock on eNOS expression and eNO release is unknown
Takahashi et al., J Biol Chem 2003
:
Synergistic
activation of
endothelial nitric-oxide synthase (eNOS) by
HSP90 and Akt : calcium independent eNOS activation involves formation of an HSP90-Akt-CaM bound eNOS complex ... We recently used purified proteins to characterize the mechanisms by which
heat shock protein 90 (HSP90) increases
eNOS activity at low and high Ca2+ levels ( Takahashi, S. and Mendelsohn, M. E. ( 2003 ) J. Biol. Chem. 278, 9339-9344 ) ... Akt was not observed in the eNOS complex in the absence of HSP90, but both active and inactive Akt associated with
eNOS in the
presence of
HSP90 ...
HSP90 and active Akt together
increased eNOS activity synergistically, which was reversed by GA ... GA prevented insulin induced association of
HSP90 , Akt and CaM with eNOS and
inhibited eNOS activation in BAECs ... These results demonstrate that
HSP90 and Akt synergistically
activate eNOS and suggest that this synergy contributes to Ca2+ independent eNOS activation in response to insulin
Jiang et al., J Biol Chem 2003
:
In addition, the molecular chaperone
Hsp90 interacts with eNOS and positively
regulates eNOS activity
Chen et al., J Appl Physiol 2004
:
We conclude that stimulated
HSP90 binding to eNOS and activation of the PI3-Akt pathway
contribute to Ang-1 induced
eNOS phosphorylation, NO production, and angiogenesis in PCAEC
Teng et al., J Biol Chem 2004
(Cell Transformation, Neoplastic) :
Heat shock protein 90 (HSP90) is
involved in the folding of proteins such as signal transduction molecules ( Src, Raf1, cdk4 ) and steroid receptors and in enhancing the activity of telomerase and
nitric-oxide synthase
Ortiz et al., American journal of physiology. Renal physiology 2004
:
We next tested whether
heat shock protein (Hsp)90 is
involved in
eNOS translocation ... We conclude that luminal flow induces eNOS translocation and activation in the THAL via PI3-kinase and that
Hsp90 is
involved in
eNOS translocation to the apical membrane
Lin et al., FEBS Lett 2004
:
Recently, it was demonstrated that
eNOS activity is highly
regulated by
heat shock protein 90 (HSP90)
Xi et al., Biochem Biophys Res Commun 2005
:
Globular adiponectin stimulated binding of HSP90 to
eNOS , and inhibition of
HSP90 significantly
suppressed globular adiponectin stimulated NO release ... These results indicate that stimulated
HSP90 binding to eNOS and activation of the PI3-Akt pathway
contribute to globular adiponectin induced
eNOS phosphorylation and NO production, and to endothelium dependent vasorelaxation
Martínez-Ruiz et al., Proc Natl Acad Sci U S A 2005
:
Hsp90 ATPase activity and its positive
effect on
eNOS activity are both inhibited by S-nitrosylation
Okano et al., J Cardiovasc Pharmacol 2006
(Body Weight) :
Tyrosine phosphorylation of
eNOS and expression of calmodulin increased, but
Hsp90 decreased with all treatments and only raloxifene treatment
increased caveolin-1 compared with OVX
Gu et al., Hypertens Pregnancy 2006
(Pre-Eclampsia) :
Using Hsp90 inhibitor geldanamycin ( GA ), we further determined the potential
role of
Hsp90 in superoxide generation,
eNOs expression, and prostacyclin production of altered EC function associated with PE pregnancies ... Inhibition of
Hsp90 by GA
resulted in an increase in superoxide generation and a decrease in
eNOs protein expression
Sud et al., Am J Physiol Lung Cell Mol Physiol 2007
:
We found that overexpression of
HSP90 significantly
increased the shear stimulated association of HSP90 with
eNOS and led to significant increases in NO production and reduced NOS dependent superoxide generation
Duval et al., Mol Biol Cell 2007
:
VEGF signaling to eNOS is principally
mediated by an Akt dependent phosphorylation of eNOS and by increased association of
eNOS to the molecular chaperone,
heat-shock protein 90 kDa (Hsp90)
Frossard et al., Am J Physiol Gastrointest Liver Physiol 2007
(Bile Duct Diseases...) :
Because
endothelial NO synthase (eNOS) is
regulated by caveolin that decreases and
heat shock protein 90 (HSP90) that increases NO production, we hypothesized that an opposite regulation of eNOS by caveolin and HSP90 might explain the opposite NO production in both organs ... Our study shows an opposite posttranslational
regulation of
eNOS by
HSP90 and caveolin in lungs and liver from rats with CBDL
Makondo et al., Eur J Pharmacol 2008
:
In the present work, the
role of
HSP90 in HGF stimulation of
eNOS was examined in an endothelial cell culture system
Mohan et al., Am J Physiol Cell Physiol 2009
(Hyperglycemia) :
The availability of NO to the vasculature is regulated by endothelial nitric oxide synthase (eNOS) activity and the
involvement of
heat shock protein-90 (Hsp-90) in the regulation of
eNOS activity has been demonstrated
Amour et al., Anesthesiology 2009
(Myocardial Infarction) :
Heat shock protein 90 (Hsp90) regulates
endothelial nitric oxide synthase (eNOS) activity
An et al., Am J Physiol Heart Circ Physiol 2009
(Disease Models, Animal...) :
SP
increased the association of
HSP90 with
NOS3
Harris et al., Eur J Appl Physiol 2010
:
Increased
Hsp90 expression, a
regulator of
eNOS activity and coupling, suggests a potential mechanism for this improvement
Park et al., Free Radic Biol Med 2011
:
Chk1 and
Hsp90 cooperatively
regulate phosphorylation of endothelial
nitric oxide synthase at serine 1179
García-Cardeña et al., Nature 1998
:
Dynamic
activation of endothelial
nitric oxide synthase by
Hsp90 ... Moreover, the binding of
Hsp90 to eNOS
enhances the activation of
eNOS