PMID- 21311214
OWN - NLM
STAT- MEDLINE
DCOM- 20110726
LR  - 20220317
IS  - 1942-0994 (Electronic)
IS  - 1942-0900 (Print)
IS  - 1942-0994 (Linking)
VI  - 3
IP  - 6
DP  - 2010 Nov-Dec
TI  - Signaling of reactive oxygen and nitrogen species in Diabetes mellitus.
PG  - 361-73
AB  - Disorder of physiological signaling functions of reactive oxygen species (ROS) 
      superoxide and hydrogen peroxide and reactive nitrogen species (RNS) nitric oxide 
      and peroxynitrite is an important feature of diabetes mellitus type 1 and type 2. 
      It is now known that hyperglycemic conditions of cells are associated with the 
      enhanced levels of ROS mainly generated by mitochondria and NADPH oxidase. It has 
      been established that ROS stimulate many enzymatic cascades under normal 
      physiological conditions, but hyperglycemia causes ROS overproduction and the 
      deregulation of ROS signaling pathways initiating the development of diabetes 
      mellitus. On the other hand the deregulation of RNS signaling leads basically to 
      a decrease in NO formation with subsequent damaging disorders. In the present 
      work we will consider the pathological changes of ROS and RNS signaling in 
      enzyme/gene regulated processes catalyzed by protein kinases C and B (Akt/B), 
      phosphatidylinositol 3'-kinase (PI3-kinase), extracellular signal-regulated 
      kinase 1/2 (ERK1/2), and some others. Furthermore we will discuss a particularly 
      important role of several ROS-regulated genes and adapter proteins such as the 
      p66shc, FOXO3a, and Sirt2. The effects of low and high ROS levels in diabetes 
      will be also considered. Thus the regulation of damaging ROS levels in diabetes 
      by antioxidants and free radical scavengers must be one of promising treatment of 
      this disease, however, because of the inability of traditional antioxidative 
      vitamin E and C to interact with superoxide and hydrogen peroxide, new free 
      radical scavengers such as flavonoids, quinones and synthetic mimetics of 
      superoxide dismutase (SOD) should be intensively studied.
FAU - Afanas'ev, Igor
AU  - Afanas'ev I
AD  - Vitamin Research Institute, Moscow, Russia. iafananizer@gmail.com
LA  - eng
PT  - Journal Article
DEP - 20101101
PL  - United States
TA  - Oxid Med Cell Longev
JT  - Oxidative medicine and cellular longevity
JID - 101479826
RN  - 0 (Antioxidants)
RN  - 0 (FOXO3 protein, human)
RN  - 0 (Forkhead Box Protein O3)
RN  - 0 (Forkhead Transcription Factors)
RN  - 0 (Free Radical Scavengers)
RN  - 0 (Reactive Nitrogen Species)
RN  - 0 (Reactive Oxygen Species)
RN  - EC 1.15.1.1 (Superoxide Dismutase)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3)
RN  - EC 3.5.1.- (SIRT2 protein, human)
RN  - EC 3.5.1.- (Sirtuin 2)
SB  - IM
MH  - Antioxidants/therapeutic use
MH  - Diabetes Mellitus/*metabolism/therapy
MH  - Forkhead Box Protein O3
MH  - Forkhead Transcription Factors/metabolism
MH  - Free Radical Scavengers/therapeutic use
MH  - Humans
MH  - Mitogen-Activated Protein Kinase 1/metabolism
MH  - Mitogen-Activated Protein Kinase 3/metabolism
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Proto-Oncogene Proteins c-akt/metabolism
MH  - Reactive Nitrogen Species/*metabolism
MH  - Reactive Oxygen Species/*metabolism
MH  - Signal Transduction
MH  - Sirtuin 2/metabolism
MH  - Superoxide Dismutase/metabolism
PMC - PMC3154046
EDAT- 2011/02/12 06:00
MHDA- 2011/07/27 06:00
PMCR- 2010/11/01
CRDT- 2011/02/12 06:00
PHST- 2011/02/12 06:00 [entrez]
PHST- 2011/02/12 06:00 [pubmed]
PHST- 2011/07/27 06:00 [medline]
PHST- 2010/11/01 00:00 [pmc-release]
AID - 14415 [pii]
AID - 10.4161/oxim.3.6.14415 [doi]
PST - ppublish
SO  - Oxid Med Cell Longev. 2010 Nov-Dec;3(6):361-73. doi: 10.4161/oxim.3.6.14415. Epub 
      2010 Nov 1.