Idioma:

Redox modulation of NQO1

Siegel, David ; Dehn, Donna D ; Bokatzian, Samantha S ; Quinn, Kevin ; Backos, Donald S ; Di Francesco, Andrea ; Bernier, Michel ; Reisdorph, Nichole ; de Cabo, Rafael ; Ross, David Bratton, Shawn B.

PloS one, 2018-01, Vol.13 (1), p.e0190717-e0190717 [Periódico revisado por pares]

United States: Public Library of Science

Texto completo disponível

Citações Citado por

Enviar para

Título:
Redox modulation of NQO1
Autor: Siegel, David ; Dehn, Donna D ; Bokatzian, Samantha S ; Quinn, Kevin ; Backos, Donald S ; Di Francesco, Andrea ; Bernier, Michel ; Reisdorph, Nichole ; de Cabo, Rafael ; Ross, David
Bratton, Shawn B.
Assuntos: Aging ; Antibiotics ; Antibodies ; Binding ; Biology and Life Sciences ; Catalytic Domain ; Cell division ; Cell Line ; Deacetylation ; Dissociation ; Domains ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Gene Knockdown Techniques ; Gerontology ; Humans ; Immunoglobulins ; Immunoprecipitation ; Immunoreactivity ; Laboratories ; Lapachone ; Macromolecules ; Mass Spectrometry ; Membranes ; Microtubules ; mRNA ; NAD ; NAD(P)H Dehydrogenase (Quinone) - genetics ; NAD(P)H Dehydrogenase (Quinone) - metabolism ; Naphthoquinones - pharmacology ; Native Polyacrylamide Gel Electrophoresis ; Nucleotides ; Oxidation ; Oxidation-Reduction ; Oxidoreductase ; Oxidoreductases ; Penicillin ; Pharmaceutical sciences ; Pharmacy ; Physical Sciences ; Physiological aspects ; Protein binding ; Proteins ; Proteolysis ; Pyridine nucleotides ; Pyridines ; Quinones ; Research and Analysis Methods ; RNA, Small Interfering - genetics ; Substrates ; Tubulin
É parte de: PloS one, 2018-01, Vol.13 (1), p.e0190717-e0190717
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
Competing Interests: I have read the journal's policy and the authors of this manuscript have the following competing interests: DS, DR and the University of Colorado are the licensor for the anti-NQO1 monoclonal antibody clone A180. This does not alter our adherence to PLOS ONE policies on sharing data and materials.
Descrição: NQO1 is a FAD containing NAD(P)H-dependent oxidoreductase that catalyzes the reduction of quinones and related substrates. In cells, NQO1 participates in a number of binding interactions with other proteins and mRNA and these interactions may be influenced by the concentrations of reduced pyridine nucleotides. NAD(P)H can protect NQO1 from proteolytic digestion suggesting that binding of reduced pyridine nucleotides results in a change in NQO1 structure. We have used purified NQO1 to demonstrate the addition of NAD(P)H induces a change in the structure of NQO1; this results in the loss of immunoreactivity to antibodies that bind to the C-terminal domain and to helix 7 of the catalytic core domain. Under normal cellular conditions NQO1 is not immunoprecipitated by these antibodies, however, following treatment with β-lapachone which caused rapid oxidation of NAD(P)H NQO1 could be readily pulled-down. Similarly, immunostaining for NQO1 was significantly increased in cells following treatment with β-lapachone demonstrating that under non-denaturing conditions the immunoreactivity of NQO1 is reflective of the NAD(P)+/NAD(P)H ratio. In untreated human cells, regions with high intensity immunostaining for NQO1 co-localize with acetyl α-tubulin and the NAD+-dependent deacetylase Sirt2 on the centrosome(s), the mitotic spindle and midbody during cell division. These data provide evidence that during the centriole duplication cycle NQO1 may provide NAD+ for Sirt2-mediated deacetylation of microtubules. Overall, NQO1 may act as a redox-dependent switch where the protein responds to the NAD(P)+/NAD(P)H redox environment by altering its structure promoting the binding or dissociation of NQO1 with target macromolecules.
Editor: United States: Public Library of Science
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Redox modulation of NQO1

Siegel, David ; Dehn, Donna D ; Bokatzian, Samantha S ; Quinn, Kevin ; Backos, Donald S ; Di Francesco, Andrea ; Bernier, Michel ; Reisdorph, Nichole ; de Cabo, Rafael ; Ross, David Bratton, Shawn B.

United States: Public Library of Science

Buscando em bases de dados remotas. Favor aguardar.