PMID- 21742790
OWN - NLM
STAT- MEDLINE
DCOM- 20110906
LR  - 20220310
IS  - 1522-1210 (Electronic)
IS  - 0031-9333 (Print)
IS  - 0031-9333 (Linking)
VI  - 91
IP  - 3
DP  - 2011 Jul
TI  - CaMKII in the cardiovascular system: sensing redox states.
PG  - 889-915
LID - 10.1152/physrev.00018.2010 [doi]
AB  - The multifunctional Ca(2+)- and calmodulin-dependent protein kinase II (CaMKII) 
      is now recognized to play a central role in pathological events in the 
      cardiovascular system. CaMKII has diverse downstream targets that promote 
      vascular disease, heart failure, and arrhythmias, so improved understanding of 
      CaMKII signaling has the potential to lead to new therapies for cardiovascular 
      disease. CaMKII is a multimeric serine-threonine kinase that is initially 
      activated by binding calcified calmodulin (Ca(2+)/CaM). Under conditions of 
      sustained exposure to elevated Ca(2+)/CaM, CaMKII transitions into a 
      Ca(2+)/CaM-autonomous enzyme by two distinct but parallel processes. 
      Autophosphorylation of threonine-287 in the CaMKII regulatory domain "traps" 
      CaMKII into an open configuration even after Ca(2+)/CaM unbinding. More recently, 
      our group identified a pair of methionines (281/282) in the CaMKII regulatory 
      domain that undergo a partially reversible oxidation which, like 
      autophosphorylation, prevents CaMKII from inactivating after Ca(2+)/CaM 
      unbinding. Here we review roles of CaMKII in cardiovascular disease with an eye 
      to understanding how CaMKII may act as a transduction signal to connect 
      pro-oxidant conditions into specific downstream pathological effects that are 
      relevant to rare and common forms of cardiovascular disease.
FAU - Erickson, Jeffrey R
AU  - Erickson JR
AD  - Department of Pharmacology, University of California at Davis, Davis, California 
      95616, USA. drjerickson@ucdavis.edu
FAU - He, B Julie
AU  - He BJ
FAU - Grumbach, Isabella M
AU  - Grumbach IM
FAU - Anderson, Mark E
AU  - Anderson ME
LA  - eng
GR  - T32 HL086350/HL/NHLBI NIH HHS/United States
GR  - R01-HL-079031/HL/NHLBI NIH HHS/United States
GR  - R01 HL070250/HL/NHLBI NIH HHS/United States
GR  - T32-HL-86350/HL/NHLBI NIH HHS/United States
GR  - T32 GM007337/GM/NIGMS NIH HHS/United States
GR  - R01-HL-62494/HL/NHLBI NIH HHS/United States
GR  - R01-HL-70250/HL/NHLBI NIH HHS/United States
GR  - R01 HL062494/HL/NHLBI NIH HHS/United States
GR  - T32 GM067795/GM/NIGMS NIH HHS/United States
GR  - R01 HL079031/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Review
PL  - United States
TA  - Physiol Rev
JT  - Physiological reviews
JID - 0231714
RN  - 0 (Reactive Oxygen Species)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
SB  - IM
MH  - Blood Vessels/metabolism
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism
MH  - Cardiovascular Diseases/etiology
MH  - Cardiovascular System/*enzymology
MH  - Enzyme Activation/physiology
MH  - Heart Failure/physiopathology
MH  - Humans
MH  - Myocardial Contraction/physiology
MH  - Myocardium/enzymology
MH  - Oxidation-Reduction
MH  - Reactive Oxygen Species/metabolism
MH  - Signal Transduction/physiology
MH  - Tissue Distribution
PMC - PMC3732780
MID - NIHMS498620
EDAT- 2011/07/12 06:00
MHDA- 2011/09/07 06:00
PMCR- 2013/08/04
CRDT- 2011/07/12 06:00
PHST- 2011/07/12 06:00 [entrez]
PHST- 2011/07/12 06:00 [pubmed]
PHST- 2011/09/07 06:00 [medline]
PHST- 2013/08/04 00:00 [pmc-release]
AID - 91/3/889 [pii]
AID - 10.1152/physrev.00018.2010 [doi]
PST - ppublish
SO  - Physiol Rev. 2011 Jul;91(3):889-915. doi: 10.1152/physrev.00018.2010.