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HSP90AA1 — NOS1
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
Bishop et al., Biol Bull 2001
:
Nitric oxide synthase (NOS) activity in some mammalian cells, including neurons,
depends on the molecular chaperone
heat shock protein 90 (HSP90) ; this may be so in echinoid larvae as well
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
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
Harris et al., Eur J Appl Physiol 2008
:
Hsp90 interacts directly with
nitric oxide synthases (NOS) ,
increasing NOS activity and altering the balance of superoxide versus NO production
Presley et al., Cell Stress Chaperones 2009
:
This was further extended to heat shocked cells, where
NOS was
activated by the induction/activation of (
Hsp90 ) through heat shock at an elevated temperature of 42 degrees C
Peng et al., Biochemistry 2009
:
Like the established Hsp90 enhancement of NO synthesis, Hsp90 inhibition of nNOS ubiquitination is Ca2+/calmodulin dependent, suggesting that the same interaction of
Hsp90 with the enzyme is
responsible for both enhancement of
nNOS activity and inhibition of ubiquitination
Park et al., Free Radic Biol Med 2011
:
Chk1 and
Hsp90 cooperatively
regulate phosphorylation of endothelial
nitric oxide synthase at serine 1179
Peng et al., J Biol Chem 2012
:
Overexpression of Hsp70 promotes nNOS ubiquitination and decreases nNOS protein, and overexpression of
Hsp90 inhibits nNOS ubiquitination and
increases nNOS protein, showing the opposing effects of the two chaperones as they participate in nNOS quality control in the cell
Lu et al., Life Sci 2012
(Myocardial Infarction...) :
The mechanism underlying EPO mediated alleviation of nitrosative stress was related to an increase in arginase II expression and to the suppression of
heat shock protein 90 (HSP90) dependent upregulation of endothelial and inducible
NO synthase ( NOS )
García-Cardeña et al., Nature 1998
:
Dynamic
activation of endothelial
nitric oxide synthase by
Hsp90