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Drug-Target Interaction

Drug

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PubChem ID:5139
Structure:
Synonyms:
1071-37-0
1071-37-0 (mono-hydrobromide)
161722-89-0
2-Ethyl-2-thiopseudourea
2-Ethyl-2-thiopseudourea hydrobromide
2986-20-1
625-53-6
AC1L1JOU
AC1Q1UA8
AR-1E1436
Carbamimidothioic acid, ethyl ester
CCG-204582
CHEBI:275077
CHEBI:43633
CHEMBL321691
DB02234
DB02539
ethyl carbamimidothioate
ethyl imidothiocarbamate
ETHYLISOTHIOUREA
ethylsulfanylmethanimidamide
ethyron
etiron
HSCI1_000396
ITU
Lopac-E-3149
Lopac0_000491
NCGC00015407-01
NCGC00015407-02
NCGC00015407-03
NCGC00015407-04
NCGC00024835-01
NCGC00024835-02
Pseudourea, 2-ethyl-2-thio-
s-Ethyl isothiouronium bromide
S-Ethylisothiourea
S-Ethylisothiourea hydrobromide
S09-0122
SBB069241
SEU
STK370557
Tocris-0873
ZINC03806245

Target

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Uniprot ID:NOS3_SHEEP
Synonyms:
cNOS
Constitutive NOS
EC-NOS
Endothelial NOS
eNOS
Nitric oxide synthase, endothelial
NOS type III
NOSIII
EC-Numbers:1.14.13.39
Organism:Ovis aries
Sheep
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

18192589
Protein kinase Cdelta regulates endothelial nitric oxide synthase expression via Akt activation and nitric oxide generation.. Neetu Sud; Stephen Wedgwood; Stephen M Black (2008) American journal of physiology. Lung cellular and molecular physiology display abstract
In this study, we explore the roles of the delta isoform of PKC (PKCdelta) in the regulation of endothelial nitric oxide synthase (eNOS) activity in pulmonary arterial endothelial cells isolated from fetal lambs (FPAECs). Pharmacological inhibition of PKCdelta with either rottlerin or with the peptide, deltaV1-1, acutely attenuated NO production, and this was associated with a decrease in phosphorylation of eNOS at Ser1177 (S1177). The chronic effects of PKCdelta inhibition using either rottlerin or the overexpression of a dominant negative PKCdelta mutant included the downregulation of eNOS gene expression that was manifested by a decrease in both eNOS promoter activity and protein expression after 24 h of treatment. We also found that PKCdelta inhibition blunted Akt activation as observed by a reduction in phosphorylated Akt at position Ser473. Thus, we conclude that PKCdelta is actively involved in the activation of Akt. To determine the effect of Akt on eNOS signaling, we overexpressed a dominant negative mutant of Akt and determined its effect of NO generation, eNOS expression, and phosphorylation of eNOS at S1177. Our results demonstrated that Akt inhibition was associated with decreased NO production that correlated with reduced phosphorylation of eNOS at S1177, and decreased eNOS promoter activity. We next evaluated the effect of endogenously produced NO on eNOS expression by incubating FPAECs with the eNOS inhibitor 2-ethyl-2-thiopseudourea (ETU). ETU significantly inhibited NO production, eNOS promoter activity, and eNOS protein levels. Together, our data indicate involvement of PKCdelta-mediated Akt activation and NO generation in maintaining eNOS expression.