Gene interactions and pathways from curated databases and text-mining

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HSP90AA1 — NOS3

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

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