PMID- 9442023
OWN - NLM
STAT- MEDLINE
DCOM- 19980303
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 4
DP  - 1998 Jan 23
TI  - A novel protein phosphatase that dephosphorylates and regulates 
      Ca2+/calmodulin-dependent protein kinase II.
PG  - 1904-10
AB  - A synthetic peptide corresponding to the autophosphorylation site of 
      Ca2+/calmodulin-dependent protein kinase II (CaMKII) (residues 281-289) was 
      conjugated to paramagnetic particles, and phosphorylated by a constitutively 
      active CaMKII fragment. Using this phosphopeptide conjugate as a substrate, a 
      calyculin A-insensitive, Mn(2+)-dependent, and poly-L-lysine-stimulated protein 
      phosphatase activity was detected in the crude extract of rat brain. The protein 
      phosphatase (designated as CaMKII phosphatase) (CaMKIIPase) was purified to near 
      homogeneity from rat brain. CaMKIIPase showed apparent molecular weights of 
      54,000 and 65,000, on SDS-polyacrylamide gel electrophoresis and gel-filtration 
      analysis, respectively. It was not inhibited by 100 nM calyculin A or 10 microM 
      okadaic acid. Mn2+, but not Mg2+, was absolutely required for activity. 
      CaMKIIPase was potently activated by polycations. Autophosphorylated CaMKII was 
      dephosphorylated by CaMKIIPase, whereas phosphorylase kinase, mixed histones, 
      myelin basic protein, and alpha-casein (which had been phosphorylated by 
      cAMP-dependent protein kinase) and phosphorylase a (phosphorylated by 
      phosphorylase kinase) were not significantly dephosphorylated. No other proteins 
      than CaMKII in rat brain extract which had been phosphorylated by CaMKII were 
      dephosphorylated. The stimulated Ca(2+)-independent activity of 
      autophosphorylated CaMKII was reversed by the action of CaMKIIPase. Thus, 
      CaMKIIPase appears to be a specialized protein phosphatase for the regulation of 
      CaMKII.
FAU - Ishida, A
AU  - Ishida A
AD  - Department of Biochemistry, Asahikawa Medical College, Japan.
FAU - Kameshita, I
AU  - Kameshita I
FAU - Fujisawa, H
AU  - Fujisawa H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cations)
RN  - 0 (Polyamines)
RN  - 0 (Polyelectrolytes)
RN  - 0 (polycations)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 3.1.3.- (calmodulin dependent protein kinase II phosphatase)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
SB  - IM
MH  - Animals
MH  - Brain/enzymology
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/*metabolism
MH  - Cations/metabolism
MH  - Enzyme Activation
MH  - Molecular Weight
MH  - Phosphoprotein Phosphatases/chemistry/*isolation & purification/metabolism
MH  - Phosphorylation
MH  - Polyamines/metabolism
MH  - Polyelectrolytes
MH  - Rats
MH  - Substrate Specificity
EDAT- 1998/01/27 00:00
MHDA- 1998/01/27 00:01
CRDT- 1998/01/27 00:00
PHST- 1998/01/27 00:00 [pubmed]
PHST- 1998/01/27 00:01 [medline]
PHST- 1998/01/27 00:00 [entrez]
AID - S0021-9258(19)84136-4 [pii]
AID - 10.1074/jbc.273.4.1904 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 Jan 23;273(4):1904-10. doi: 10.1074/jbc.273.4.1904.