PMID- 10485709
OWN - NLM
STAT- MEDLINE
DCOM- 19990927
LR  - 20171116
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 401
IP  - 6748
DP  - 1999 Sep 2
TI  - Cell transformation by the superoxide-generating oxidase Mox1.
PG  - 79-82
AB  - Reactive oxygen species (ROS) generated in some non-phagocytic cells are
      implicated in mitogenic signalling and cancer. Many cancer cells show increased
      production of ROS, and normal cells exposed to hydrogen peroxide or superoxide
      show increased proliferation and express growth-related genes. ROS are generated 
      in response to growth factors, and may affect cell growth, for example in
      vascular smooth-muscle cells. Increased ROS in Ras-transformed fibroblasts
      correlates with increased mitogenic rate. Here we describe the cloning of mox1,
      which encodes a homologue of the catalytic subunit of the superoxide-generating
      NADPH oxidase of phagocytes, gp91phox. mox1 messenger RNA is expressed in colon, 
      prostate, uterus and vascular smooth muscle, but not in peripheral blood
      leukocytes. In smooth-muscle cells, platelet-derived growth factor induces mox1
      mRNA production, while antisense mox1 mRNA decreases superoxide generation and
      serum-stimulated growth. Overexpression of mox1 in NIH3T3 cells increases
      superoxide generation and cell growth. Cells expressing mox1 have a transformed
      appearance, show anchorage-independent growth and produce tumours in athymic
      mice. These data link ROS production by Mox1 to growth control in non-phagocytic 
      cells.
FAU - Suh, Y A
AU  - Suh YA
AD  - Department of Biochemistry, Emory University Medical School, Atlanta, Georgia
      30322, USA.
FAU - Arnold, R S
AU  - Arnold RS
FAU - Lassegue, B
AU  - Lassegue B
FAU - Shi, J
AU  - Shi J
FAU - Xu, X
AU  - Xu X
FAU - Sorescu, D
AU  - Sorescu D
FAU - Chung, A B
AU  - Chung AB
FAU - Griendling, K K
AU  - Griendling KK
FAU - Lambeth, J D
AU  - Lambeth JD
LA  - eng
SI  - GENBANK/AF127763
SI  - GENBANK/AF152963
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Reactive Oxygen Species)
RN  - 11062-77-4 (Superoxides)
RN  - EC 1.6.- (NADH, NADPH Oxidoreductases)
RN  - EC 1.6.3.- (CYBB protein, human)
RN  - EC 1.6.3.- (NADPH Oxidase 2)
RN  - EC 1.6.3.- (NADPH Oxidases)
RN  - EC 1.6.99.- (superoxide-forming enzyme)
RN  - EC 4.2.1.3 (Aconitate Hydratase)
SB  - IM
MH  - 3T3 Cells
MH  - Aconitate Hydratase/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Catalysis
MH  - Cell Line
MH  - *Cell Transformation, Neoplastic
MH  - Cloning, Molecular
MH  - Colon/metabolism
MH  - Humans
MH  - Membrane Glycoproteins/genetics/metabolism
MH  - Mice
MH  - Mice, Nude
MH  - Molecular Sequence Data
MH  - NADH, NADPH Oxidoreductases/genetics/*physiology
MH  - NADPH Oxidase 2
MH  - NADPH Oxidases/chemistry
MH  - RNA, Messenger/metabolism
MH  - Rats
MH  - Reactive Oxygen Species/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Superoxides/*metabolism
MH  - Tissue Distribution
MH  - Transfection
EDAT- 1999/09/15 09:00
MHDA- 2001/03/23 10:01
CRDT- 1999/09/15 09:00
PHST- 1999/09/15 09:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/09/15 09:00 [entrez]
AID - 10.1038/43459 [doi]
PST - ppublish
SO  - Nature. 1999 Sep 2;401(6748):79-82. doi: 10.1038/43459.