Linked Life Data

21193028

Source:http://linkedlifedata.com/resource/pubmed/id/21193028

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-2-28
pubmed:abstractText
Dopamine cellular signaling via the D(1) receptor (D(1)R) involves both protein kinase A (PKA) and protein kinase C (PKC), but the PKC isoform involved has not been determined. Therefore, we tested the hypothesis that the D(1)R-mediated inhibition of NADPH oxidase activity involves cross talk between PKA and a specific PKC isoform(s). In HEK-293 cells heterologously expressing human D(1)R (HEK-hD(1)), fenoldopam, a D(1)R agonist, and phorbol 12-myristate 13-acetate (PMA), a PKC activator, inhibited oxidase activity in a time- and concentration-dependent manner. The D(1)R-mediated inhibition of oxidase activity (68.1±3.6%) was attenuated by two PKA inhibitors, H89 (10?mol/L; 88±8.1%) and Rp-cAMP (10?mol/L; 97.7±6.7%), and two PKC inhibitors, bisindolylmaleimide I (1?mol/L; 94±6%) and staurosporine (10nmol/L; 93±8%), which by themselves had no effect (n=4-8/group). The inhibitory effect of PMA (1?mol/L) on oxidase activity (73±3.2%) was blocked by H89 (100±7.8%; n=5 or 6/group). The PMA-mediated inhibition of NADPH oxidase activity was accompanied by an increase in PKC?(S676), an effect that was also blocked by H89. Fenoldopam (1?mol/L) also increased PKC?(S676) in HEK-hD(1) and human renal proximal tubule (RPT) cells. Knockdown of PKC? with siRNA in RPT cells prevented the inhibitory effect of fenoldopam on NADPH oxidase activity. Our studies demonstrate for the first time that cross talk between PKA and PKC? plays an important role in the D(1)R-mediated negative regulation of NADPH oxidase activity in human kidney cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1873-4596
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
832-40
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed-meshheading:21193028-Cell Line, Transformed, pubmed-meshheading:21193028-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:21193028-Dopamine, pubmed-meshheading:21193028-Enzyme Activation, pubmed-meshheading:21193028-Fenoldopam, pubmed-meshheading:21193028-Gene Expression, pubmed-meshheading:21193028-Humans, pubmed-meshheading:21193028-Kidney, pubmed-meshheading:21193028-NADPH Oxidase, pubmed-meshheading:21193028-Phosphorylation, pubmed-meshheading:21193028-Protein Isoforms, pubmed-meshheading:21193028-Protein Kinase C, pubmed-meshheading:21193028-Protein Kinase Inhibitors, pubmed-meshheading:21193028-RNA, Small Interfering, pubmed-meshheading:21193028-Receptors, Dopamine D1, pubmed-meshheading:21193028-Signal Transduction, pubmed-meshheading:21193028-Staurosporine, pubmed-meshheading:21193028-Tetradecanoylphorbol Acetate
pubmed:year
2011
pubmed:articleTitle
Dopamine D1 receptor-mediated inhibition of NADPH oxidase activity in human kidney cells occurs via protein kinase A-protein kinase C cross talk.
pubmed:affiliation
Center for Molecular Physiology Research, Children's National Medical Center, Department of Pediatrics, George Washington University School of Medicine, Washington, DC 20010, USA. pyu@cnmc.org
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural