Abstract |
ECTO-NOX (because of their cell surface location) proteins comprise a family of NAD(P)H oxidases of plants and animals that exhibit both oxidative and protein disulfide isomerase-like activities. The two biochemical activities, hydroquinone [ NAD(P)H] oxidation and protein disulfide-- thiol interchange alternate, a property unprecedented in the biochemical literature. A tumor-associated ECTO-NOX (tNOX) is cancer-specific and drug-responsive. The constitutive ECTO-NOX (CNOX) is ubiquitous and refractory to drugs. The physiological substrate for the oxidative activity appears to be hydroquinones of the plasma membrane such as reduced coenzyme Q10. ECTO-NOX proteins are growth-related and drive cell enlargement. Also indicated are roles in aging and in neurodegenerative diseases. The regular pattern of oscillations appears to be related to alpha-helix-beta-structure transitions and serves biochemical core oscillator of the cellular biological clock. Period length is independent of temperature (temperature compensated) and synchrony is achieved through entrainment.
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Authors | D James Morré, Dorothy M Morré |
Journal | Free radical research
(Free Radic Res)
Vol. 37
Issue 8
Pg. 795-808
(Aug 2003)
ISSN: 1071-5762 [Print] England |
PMID | 14567438
(Publication Type: Journal Article, Review)
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Chemical References |
- Coenzymes
- Multienzyme Complexes
- Prions
- Ubiquinone
- NADH oxidase
- NADH, NADPH Oxidoreductases
- coenzyme Q10
- Oxygen
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Topics |
- Aging
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Biological Clocks
- Cell Division
- Cell Membrane
(enzymology)
- Coenzymes
- Humans
- Models, Biological
- Molecular Sequence Data
- Multienzyme Complexes
(biosynthesis, physiology)
- NADH, NADPH Oxidoreductases
(biosynthesis, physiology)
- Neoplasms
(enzymology)
- Neurodegenerative Diseases
(enzymology)
- Oxygen
(metabolism)
- Prions
(metabolism)
- Sequence Homology, Amino Acid
- Temperature
- Time Factors
- Ubiquinone
(analogs & derivatives, metabolism)
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