scholarly journals Hydrogen Peroxide Potentiates Volume-sensitive Excitatory Amino Acid Release via a Mechanism Involving Ca2+/Calmodulin-dependent Protein Kinase II

2004 ◽  
Vol 280 (5) ◽  
pp. 3548-3554 ◽  
Author(s):  
Renée E. Haskew-Layton ◽  
Alexander A. Mongin ◽  
Harold K. Kimelberg
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Protein Kinase ◽  
Excitatory Amino Acid ◽  
Dependent Protein Kinase ◽  
Amino Acid Release ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Acid Release

scholarly journals The amino acid sequence of a hinge region in the regulatory subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase II

FEBS Letters ◽  
1980 ◽  
Vol 114 (1) ◽  
pp. 83-88 ◽  
Author(s):  
Koji Takio ◽  
Kenneth A. Walsh ◽  
Hans Neurath ◽  
Stephen B. Smith ◽  
Edwin G. Krebs ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Amino Acid Sequence ◽  
Cardiac Muscle ◽  
Hinge Region ◽  
Regulatory Subunit ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Phosphorylation of the C-terminal domain of the Na+/H+ exchanger by Ca2+/calmodulin-dependent protein kinase II

1992 ◽  
Vol 282 (1) ◽  
pp. 139-145 ◽  
Author(s):  
L Fliegel ◽  
M P Walsh ◽  
D Singh ◽  
C Wong ◽  
A Barr
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Fusion Protein ◽  
Dependent Protein Kinase ◽  
Terminal Domain ◽  
Kinase C ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Beta Galactosidase

The Na+/H+ exchanger is a pH-regulatory protein that extrudes one H+ ion in exchange for one Na+ ion when intracellular pH declines. A number of studies have shown phorbol ester stimulation of activity in intact cells, leading to the idea that the exchanger is regulated by protein kinase C-mediated phosphorylation in vivo. cDNA encoding the protein has been cloned, and a recent model suggests a large internal cytoplasmic C-terminal domain that may be a site of regulation of the exchanger [Sardet, Franchi & Pouyssegur (1989) Cell 56, 271-280]. We examined this region of the protein using a rabbit cardiac Na+/H+ exchanger cDNA clone. cDNA of the Na+/H+ exchanger, coding for the C-terminal 178 amino acid residues, was cloned into the expression vector pEX-1 and expressed as a fusion protein with beta-galactosidase. The fusion protein reacted with an antibody produced against a synthetic peptide of the C-terminal 13 amino acid residues of the Na+/H+ exchanger, confirming the identity of the expressed protein. Control and experimental pEX-1-Na+/H+ exchanger protein was purified on a p-aminophenyl beta-D-thiogalactopyranoside-agarose column. Purified Ca2+/calmodulin-dependent protein kinase II readily phosphorylated the Na+/H+ exchanger protein in a Ca(2+)- and calmodulin-dependent manner in vitro, but this region of the protein was not a substrate for purified protein kinase C or for the catalytic subunit of cyclic AMP-dependent protein kinase. Control-expressed beta-galactosidase was phosphorylated to a maximal level of 0.77 +/- 0.17 mol of Pi/mol (mean +/- S.E.M., n = 6) whereas the fusion protein was phosphorylated to a maximal level of 4.09 +/- 0.39 mol of Pi/mol (n = 6), suggesting one site of phosphorylation in beta-galactosidase and three in the C-terminal domain of the Na+/H+ exchanger. Examination of the deduced amino acid sequence of this part of the exchanger reveals three consensus sequences for Ca2+/calmodulin-dependent protein kinase II. These results suggest that the exchanger may be directly regulated in vivo by calmodulin-dependent protein kinase II but not by protein kinase C or cyclic AMP-dependent protein kinase.

scholarly journals Critical amino acid residues of AIP, a highly specific inhibitory peptide of calmodulin-dependent protein kinase II

FEBS Letters ◽  
1998 ◽  
Vol 427 (1) ◽  
pp. 115-118 ◽  
Author(s):  
Atsuhiko Ishida ◽  
Yasushi Shigeri ◽  
Yoshiro Tatsu ◽  
Koichi Uegaki ◽  
Isamu Kameshita ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Residues ◽  
Inhibitory Peptide ◽  
Dependent Protein Kinase ◽  
Critical Amino Acid ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Molecular Characterization of Ca2+/Calmodulin-Dependent Protein Kinase II Isoforms in Three Rice Planthoppers—Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera

2019 ◽  
Vol 20 (12) ◽  
pp. 3014
Author(s):  
Wei-Xia Wang ◽  
Feng-Xiang Lai ◽  
Pin-Jun Wan ◽  
Qiang Fu ◽  
Ting-Heng Zhu
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Variable Region ◽  
Nilaparvata Lugens ◽  
Laodelphax Striatellus ◽  
Sogatella Furcifera ◽  
Dependent Protein Kinase ◽  
Rice Planthoppers ◽  
Protein Kinase Ii ◽  
Dependent Protein

This study reports the identification of splice variants for the calcium/calmodulin-dependent protein kinase II (CaMKII) gene from Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera. CaMKII is a multifunctional serine/threonine protein kinase that transduces Ca2+ signals in cells to control a range of cellular processes in the nervous system and muscular tissue. Sequence analysis showed that CaMKII was 99.0% identical at the amino acid level among three rice planthoppers, with the exception of a variable region located in the association domain. Four kinds of 20–81 amino acid “inserts” were found in the variable region. The phylogenetic tree of the deduced amino acid sequences showed that the NlCaMKII isoforms were more closely related to the LsCaMKII isoforms and were slightly distinct from SfCaMKII. CaMKII-E was the dominant type among the five main isoforms. CaMKII genes were constitutively expressed in various nymphal and adult stages and in tested tissues with the predominant transcription occurring in the head. There was no major tissue specificity of isoform expression, but the expression pattern and relative abundance of isoforms varied when compared with the RT-PCR between tissues. In addition, RNAi in N. lugens with dsRNA at a concentration of 200 ng nymph−1 induced a mortality of 77.7% on the 10th day and a reduction in the mRNA expression level of 67.2%. Unlike the holometabolous insect Helicoverpa armigera, the knockdown of NlCaMKII did not suppress the expression of 20E response genes, such as ECR, USP1, and HR3, in N. lugens. These results indicate that the role of CaMKII in hemimetabolous insects may be different from that in holometabolous insects.

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