2009
Maioli, Emanuela; Greci, Lucedio; Soucek, Karel; Hyzdalova, Martina; Pecorelli, Alessandra; Fortino, Vittoria; Valacchi, Giuseppe
Rottlerin inhibits ROS formation and prevents NFkappaB activation in MCF-7 and HT-29 cells. Journal Article
In: Journal of biomedicine & biotechnology, vol. 2009, pp. 742936, 2009, ISSN: 1110-7251 1110-7243, (Place: United States).
Abstract | Links | BibTeX | Tags: Acetophenones/chemistry/*pharmacology, Benzopyrans/chemistry/*pharmacology, Biphenyl Compounds/metabolism, Cell Nucleus/drug effects/metabolism, DNA/metabolism, Electron Spin Resonance Spectroscopy, Free Radical Scavengers/pharmacology, Genetic/drug effects, HT29 Cells, Humans, Hydrogen Peroxide/metabolism, Intracellular Space/drug effects/metabolism, NF-kappa B/*metabolism, Picrates/metabolism, Protein Binding/drug effects, Protein Transport/drug effects, Reactive Oxygen Species/*metabolism, Spectrophotometry, Transcription, Transfection, Tumor Necrosis Factor-alpha/pharmacology, Ultraviolet
@article{maioli_rottlerin_2009,
title = {Rottlerin inhibits ROS formation and prevents NFkappaB activation in MCF-7 and HT-29 cells.},
author = {Emanuela Maioli and Lucedio Greci and Karel Soucek and Martina Hyzdalova and Alessandra Pecorelli and Vittoria Fortino and Giuseppe Valacchi},
doi = {10.1155/2009/742936},
issn = {1110-7251 1110-7243},
year = {2009},
date = {2009-01-01},
journal = {Journal of biomedicine & biotechnology},
volume = {2009},
pages = {742936},
abstract = {Rottlerin, a polyphenol isolated from Mallotus Philippinensis, has been recently used as a selective inhibitor of PKC delta, although it can inhibit many kinases and has several biological effects. Among them, we recently found that Rottlerin inhibits the Nuclear Factor kappaB (NFkappaB), activated by either phorbol esters or H(2)O(2). Because of the redox sensitivity of NFkappaB and on the basis of Rottlerin antioxidant property, we hypothesized that Rottlerin could prevent NFkappaB activation acting as a free radicals scavenger, as other natural polyphenols. The current study confirms the antioxidant property of Rottlerin against the 2,2-diphenyl-1-picrylhydrazyl radical (DPPH) in vitro and against oxidative stress induced by H(2)O(2) and by menadione in culture cells. We also demonstrate that Rottlerin prevents TNFalpha-dependent NFkappaB activation in MCF-7 cells and in HT-29 cells transfected with the NFkappaB-driven plasmid pBIIX-LUC, suggesting that Rottlerin can inhibit NFkappaB via several pathways and in several cell types.},
note = {Place: United States},
keywords = {Acetophenones/chemistry/*pharmacology, Benzopyrans/chemistry/*pharmacology, Biphenyl Compounds/metabolism, Cell Nucleus/drug effects/metabolism, DNA/metabolism, Electron Spin Resonance Spectroscopy, Free Radical Scavengers/pharmacology, Genetic/drug effects, HT29 Cells, Humans, Hydrogen Peroxide/metabolism, Intracellular Space/drug effects/metabolism, NF-kappa B/*metabolism, Picrates/metabolism, Protein Binding/drug effects, Protein Transport/drug effects, Reactive Oxygen Species/*metabolism, Spectrophotometry, Transcription, Transfection, Tumor Necrosis Factor-alpha/pharmacology, Ultraviolet},
pubstate = {published},
tppubtype = {article}
}
Rottlerin, a polyphenol isolated from Mallotus Philippinensis, has been recently used as a selective inhibitor of PKC delta, although it can inhibit many kinases and has several biological effects. Among them, we recently found that Rottlerin inhibits the Nuclear Factor kappaB (NFkappaB), activated by either phorbol esters or H(2)O(2). Because of the redox sensitivity of NFkappaB and on the basis of Rottlerin antioxidant property, we hypothesized that Rottlerin could prevent NFkappaB activation acting as a free radicals scavenger, as other natural polyphenols. The current study confirms the antioxidant property of Rottlerin against the 2,2-diphenyl-1-picrylhydrazyl radical (DPPH) in vitro and against oxidative stress induced by H(2)O(2) and by menadione in culture cells. We also demonstrate that Rottlerin prevents TNFalpha-dependent NFkappaB activation in MCF-7 cells and in HT-29 cells transfected with the NFkappaB-driven plasmid pBIIX-LUC, suggesting that Rottlerin can inhibit NFkappaB via several pathways and in several cell types.
2005
Harper, Richart W.; Xu, Changhong; Soucek, Karel; Setiadi, Henny; Eiserich, Jason P.
A reappraisal of the genomic organization of human Nox1 and its splice variants. Journal Article
In: Archives of biochemistry and biophysics, vol. 435, no. 2, pp. 323–330, 2005, ISSN: 0003-9861, (Place: United States).
Abstract | Links | BibTeX | Tags: *DNA Primers, *Genome, Alternative Splicing, Base Sequence, Caco-2 Cells, Computational Biology, Cultured, Epithelial Cells/enzymology, human, Humans, Hydrogen Peroxide/metabolism, Isoenzymes/genetics/metabolism, Male, Molecular Sequence Data, NADPH Oxidase 1, NADPH Oxidases/*genetics/metabolism, Prostate/enzymology, Reactive Oxygen Species/metabolism, Sequence Alignment, Superoxides/metabolism, Tumor Cells
@article{harper_reappraisal_2005,
title = {A reappraisal of the genomic organization of human Nox1 and its splice variants.},
author = {Richart W. Harper and Changhong Xu and Karel Soucek and Henny Setiadi and Jason P. Eiserich},
doi = {10.1016/j.abb.2004.12.021},
issn = {0003-9861},
year = {2005},
date = {2005-03-01},
journal = {Archives of biochemistry and biophysics},
volume = {435},
number = {2},
pages = {323–330},
abstract = {The recent discovery of non-phagocytic NAD(P)H oxidases belonging to the Nox family of enzymes sharing extensive homology to the leukocyte NAD(P)H oxidase has revolutionized our understanding of oxidative signaling related to fundamental biological processes and disease states. One form of this enzyme, Nox1, is a growth factor-responsive enzyme that catalyzes formation of the reactive oxygen species superoxide (O(2)(-)) and hydrogen peroxide (H(2)O(2)). Its expression is linked to a number of biological responses including cellular proliferation, angiogenesis, and activation of cellular signaling pathways. Whereas early published studies have described three distinct isoforms of Nox1, the current body of literature fails to adequately recognize this notion. Also, functional differences between isoforms remain relatively unexplored. Herein, we report that expression of human Nox1 is restricted to two distinct isoforms derived from a single gene; that is, the full-length gene product and a shorter spliced variant which lacks one of the NAD(P)H binding domains. We have developed PCR primer sets that distinguish between the two forms of Nox1 in several human cell lines. We could not find evidence for expression of the shortest reported form of Nox1 (NOH-1S), previously identified as a proton channel, and the absence of paired splice sites in the gene suggests that it represents a reverse transcriptase artifact. A survey of the scientific literature reveals that the majority of studies related to Nox1 do not utilize molecular strategies that would adequately discern between the two Nox1 variants. The current literature suggest the two identified isoforms of human Nox1 (which we have named Nox1-L and Nox1-S) may be functionally distinct. Future studies related to Nox1 will benefit from establishing the identity of the Nox1 isoform expressed and the functions attributed to each variant.},
note = {Place: United States},
keywords = {*DNA Primers, *Genome, Alternative Splicing, Base Sequence, Caco-2 Cells, Computational Biology, Cultured, Epithelial Cells/enzymology, human, Humans, Hydrogen Peroxide/metabolism, Isoenzymes/genetics/metabolism, Male, Molecular Sequence Data, NADPH Oxidase 1, NADPH Oxidases/*genetics/metabolism, Prostate/enzymology, Reactive Oxygen Species/metabolism, Sequence Alignment, Superoxides/metabolism, Tumor Cells},
pubstate = {published},
tppubtype = {article}
}
The recent discovery of non-phagocytic NAD(P)H oxidases belonging to the Nox family of enzymes sharing extensive homology to the leukocyte NAD(P)H oxidase has revolutionized our understanding of oxidative signaling related to fundamental biological processes and disease states. One form of this enzyme, Nox1, is a growth factor-responsive enzyme that catalyzes formation of the reactive oxygen species superoxide (O(2)(-)) and hydrogen peroxide (H(2)O(2)). Its expression is linked to a number of biological responses including cellular proliferation, angiogenesis, and activation of cellular signaling pathways. Whereas early published studies have described three distinct isoforms of Nox1, the current body of literature fails to adequately recognize this notion. Also, functional differences between isoforms remain relatively unexplored. Herein, we report that expression of human Nox1 is restricted to two distinct isoforms derived from a single gene; that is, the full-length gene product and a shorter spliced variant which lacks one of the NAD(P)H binding domains. We have developed PCR primer sets that distinguish between the two forms of Nox1 in several human cell lines. We could not find evidence for expression of the shortest reported form of Nox1 (NOH-1S), previously identified as a proton channel, and the absence of paired splice sites in the gene suggests that it represents a reverse transcriptase artifact. A survey of the scientific literature reveals that the majority of studies related to Nox1 do not utilize molecular strategies that would adequately discern between the two Nox1 variants. The current literature suggest the two identified isoforms of human Nox1 (which we have named Nox1-L and Nox1-S) may be functionally distinct. Future studies related to Nox1 will benefit from establishing the identity of the Nox1 isoform expressed and the functions attributed to each variant.